Motif 439 (n=3,184)

Position-wise Probabilities

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uniprot	genes	site	source	protein	function
A0A087X0R7	SENP3-EIF4A1	S168	ochoa	SENP3-EIF4A1 readthrough (NMD candidate)	None
A0A0B4J203	None	S808	ochoa	receptor protein-tyrosine kinase (EC 2.7.10.1)	None
A0A0C4DFX4	None	S244	ochoa	Snf2 related CREBBP activator protein	None
A0A0C4DFX4	None	S249	ochoa	Snf2 related CREBBP activator protein	None
A0A1W2PPC1	PRR33	S73	ochoa	Proline rich 33	None
A0FGR8	ESYT2	S699	ochoa	Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)	Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:27044890). {ECO:0000269\|PubMed:17360437, ECO:0000269\|PubMed:20833364, ECO:0000269\|PubMed:23791178, ECO:0000269\|PubMed:24847877, ECO:0000269\|PubMed:27044890}.
A0FGR8	ESYT2	S743	ochoa	Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)	Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:27044890). {ECO:0000269\|PubMed:17360437, ECO:0000269\|PubMed:20833364, ECO:0000269\|PubMed:23791178, ECO:0000269\|PubMed:24847877, ECO:0000269\|PubMed:27044890}.
A0FGR8	ESYT2	S761	ochoa	Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)	Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:27044890). {ECO:0000269\|PubMed:17360437, ECO:0000269\|PubMed:20833364, ECO:0000269\|PubMed:23791178, ECO:0000269\|PubMed:24847877, ECO:0000269\|PubMed:27044890}.
A0JNW5	BLTP3B	S987	ochoa	Bridge-like lipid transfer protein family member 3B (Syntaxin-6 Habc-interacting protein of 164 kDa) (UHRF1-binding protein 1-like)	Tube-forming lipid transport protein which mediates the transfer of lipids between membranes at organelle contact sites (PubMed:35499567). Required for retrograde traffic of vesicle clusters in the early endocytic pathway to the Golgi complex (PubMed:20163565, PubMed:35499567). {ECO:0000269\|PubMed:20163565, ECO:0000269\|PubMed:35499567}.
A0MZ66	SHTN1	S512	ochoa	Shootin-1 (Shootin1)	Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons. {ECO:0000250\|UniProtKB:A0MZ67, ECO:0000250\|UniProtKB:Q8K2Q9}.
A1A4S6	ARHGAP10	S643	ochoa	Rho GTPase-activating protein 10 (GTPase regulator associated with focal adhesion kinase 2) (GRAF2) (Graf-related protein 2) (Rho-type GTPase-activating protein 10)	GTPase-activating protein that catalyzes the conversion of active GTP-bound Rho GTPases to their inactive GDP-bound form, thus suppressing various Rho GTPase-mediated cellular processes (PubMed:11432776). Also converts Cdc42 to an inactive GDP-bound state (PubMed:11432776). Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). Associates with MICAL1 on the endosomal membrane to promote Rab8-Rab10-dependent tubule extension. After dissociation with MICAL1, recruits WDR44 which connects the endoplasmic reticulum (ER) with the endosomal tubule, thereby participating in the export of a subset of neosynthesized proteins (PubMed:32344433). {ECO:0000250\|UniProtKB:Q6Y5D8, ECO:0000269\|PubMed:11432776, ECO:0000269\|PubMed:32344433}.
A1L390	PLEKHG3	S1034	ochoa	Pleckstrin homology domain-containing family G member 3 (PH domain-containing family G member 3)	Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization. {ECO:0000269\|PubMed:27555588}.
A1L390	PLEKHG3	S1046	ochoa	Pleckstrin homology domain-containing family G member 3 (PH domain-containing family G member 3)	Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization. {ECO:0000269\|PubMed:27555588}.
A3KN83	SBNO1	S839	ochoa	Protein strawberry notch homolog 1 (Monocyte protein 3) (MOP-3)	Plays a crucial role in the regulation of neural stem cells (NSCs) proliferation. Enhances the phosphorylation of GSK3B through the PI3K-Akt signaling pathway, thereby upregulating the Wnt/beta-catenin signaling pathway and promoting the proliferation of NSCs. Improves ischemic stroke recovery while inhibiting neuroinflammation through small extracellular vesicles (sEVs)-mediated mechanism. Enhances the secretion of sEVs from NSCs, which in turn inhibit both the MAPK and NF-kappaB pathways in microglia. This inhibition suppresses the pro-inflammatory M1 polarization of microglia, promoting a shift towards the M2 anti-inflammatory phenotype, which is beneficial for reducing neuroinflammation. {ECO:0000250\|UniProtKB:Q689Z5}.
A5YKK6	CNOT1	S1014	ochoa	CCR4-NOT transcription complex subunit 1 (CCR4-associated factor 1) (Negative regulator of transcription subunit 1 homolog) (NOT1H) (hNOT1)	Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of embryonic stem (ES) cell identity. Plays a role in rapid sperm motility via mediating timely mRNA turnover (By similarity). {ECO:0000250\|UniProtKB:Q6ZQ08, ECO:0000269\|PubMed:10637334, ECO:0000269\|PubMed:16778766, ECO:0000269\|PubMed:21278420, ECO:0000269\|PubMed:21976065, ECO:0000269\|PubMed:21984185, ECO:0000269\|PubMed:22367759, ECO:0000269\|PubMed:23644599, ECO:0000269\|PubMed:27558897, ECO:0000269\|PubMed:32354837}.
A6NCI8	C2orf78	S819	ochoa	Uncharacterized protein C2orf78	None
A6ND36	FAM83G	S616	ochoa	Protein FAM83G (Protein associated with SMAD1)	Substrate for type I BMP receptor kinase involved in regulation of some target genes of the BMP signaling pathway. Also regulates the expression of several non-BMP target genes, suggesting a role in other signaling pathways. {ECO:0000269\|PubMed:24554596}.
A6NEQ0	RBMY1E	S479	ochoa	RNA-binding motif protein, Y chromosome, family 1 member E	RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.
A6NKD9	CCDC85C	S213	ochoa	Coiled-coil domain-containing protein 85C	May play a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family (Probable). May play an important role in cortical development, especially in the maintenance of radial glia (By similarity). {ECO:0000250\|UniProtKB:E9Q6B2, ECO:0000305\|PubMed:25009281}.
A6NKD9	CCDC85C	S216	ochoa	Coiled-coil domain-containing protein 85C	May play a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family (Probable). May play an important role in cortical development, especially in the maintenance of radial glia (By similarity). {ECO:0000250\|UniProtKB:E9Q6B2, ECO:0000305\|PubMed:25009281}.
A6NKT7	RGPD3	S1487	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A6NKT7	RGPD3	S1586	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A6NKT7	RGPD3	S1593	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A7E2V4	ZSWIM8	S1048	ochoa	Zinc finger SWIM domain-containing protein 8	Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237). Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target (PubMed:33184234). May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation (PubMed:24012004). Plays an essential role for proper embryonic development of heart and lung (By similarity). Controls protein quality of DAB1, a key signal molecule for brain development, thus protecting its signaling strength. Mechanistically, recognizes intrinsically disordered regions of DAB1 and eliminates misfolded DAB1 that cannot be properly phosphorylated (By similarity). {ECO:0000250\|UniProtKB:Q3UHH1, ECO:0000269\|PubMed:24012004, ECO:0000269\|PubMed:33184234, ECO:0000269\|PubMed:33184237}.; FUNCTION: (Microbial infection) Participates in Zika virus inhibition of IFN signaling by acting as a scaffold protein to connect ZSWIM8/CUL3 ligase complex and STAT2, leading to STAT2 degradation. {ECO:0000269\|PubMed:39145933}.
A7KAX9	ARHGAP32	S712	ochoa	Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (GTPase regulator interacting with TrkA) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)	GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12446789, ECO:0000269\|PubMed:12454018, ECO:0000269\|PubMed:12531901, ECO:0000269\|PubMed:12788081, ECO:0000269\|PubMed:12819203, ECO:0000269\|PubMed:12857875, ECO:0000269\|PubMed:17663722}.
A8CG34	POM121C	S328	ochoa	Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
A8K855	EFCAB7	S212	ochoa	EF-hand calcium-binding domain-containing protein 7	Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling. Required for the localization of the EVC2:EVC subcomplex at the base of primary cilia. {ECO:0000250\|UniProtKB:Q8VDY4}.
A8MSY1	STIMATE-MUSTN1	S255	ochoa	Musculoskeletal embryonic nuclear protein 1	None
A8MT19	RHPN2P1	S501	ochoa	Putative rhophilin-2-like protein RHPN2P1 (Rhophilin-2 pseudogene 1)	None
B2RUZ4	SMIM1	S28	ochoa	Small integral membrane protein 1 (Vel blood group antigen)	Regulator of red blood cell formation. {ECO:0000250\|UniProtKB:B3DHH5}.
B2RUZ4	SMIM1	S33	ochoa	Small integral membrane protein 1 (Vel blood group antigen)	Regulator of red blood cell formation. {ECO:0000250\|UniProtKB:B3DHH5}.
C9JLW8	MCRIP1	S24	ochoa	Mapk-regulated corepressor-interacting protein 1 (Granulin-2) (Protein FAM195B)	The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-cadherin gene and induction of epithelial-mesenchymal transition (PubMed:25728771). {ECO:0000269\|PubMed:25728771}.
E9PCH4	None	S1126	ochoa	Rap guanine nucleotide exchange factor 6	None
F5H5P2	None	S377	ochoa	2-oxoisovalerate dehydrogenase subunit alpha (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain)	Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction. {ECO:0000256\|ARBA:ARBA00037052, ECO:0000256\|RuleBase:RU365014}.
H0YC42	None	S140	ochoa	Tumor protein D52	None
H0YHG0	None	S481	ochoa	DnaJ homolog subfamily C member 14 (Nuclear protein Hcc-1) (SAP domain-containing ribonucleoprotein)	Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway. Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export. {ECO:0000256\|ARBA:ARBA00054093}.; FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. {ECO:0000256\|ARBA:ARBA00055510}.
H3BU86	STX16-NPEPL1	S35	ochoa	Syntaxin-16	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000256\|ARBA:ARBA00037772}.
H3BU86	STX16-NPEPL1	S41	ochoa	Syntaxin-16	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000256\|ARBA:ARBA00037772}.
K7ENP7	None	S32	ochoa	INO80 complex subunit C	None
O00141	SGK1	S410	ochoa	Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)	Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na(+) transport than isoform 1. {ECO:0000269\|PubMed:11154281, ECO:0000269\|PubMed:11410590, ECO:0000269\|PubMed:11696533, ECO:0000269\|PubMed:12397388, ECO:0000269\|PubMed:12590200, ECO:0000269\|PubMed:12634932, ECO:0000269\|PubMed:12650886, ECO:0000269\|PubMed:12761204, ECO:0000269\|PubMed:12911626, ECO:0000269\|PubMed:14623317, ECO:0000269\|PubMed:14706641, ECO:0000269\|PubMed:15040001, ECO:0000269\|PubMed:15044175, ECO:0000269\|PubMed:15234985, ECO:0000269\|PubMed:15319523, ECO:0000269\|PubMed:15496163, ECO:0000269\|PubMed:15733869, ECO:0000269\|PubMed:15737648, ECO:0000269\|PubMed:15845389, ECO:0000269\|PubMed:15888551, ECO:0000269\|PubMed:16036218, ECO:0000269\|PubMed:16443776, ECO:0000269\|PubMed:16982696, ECO:0000269\|PubMed:17382906, ECO:0000269\|PubMed:18005662, ECO:0000269\|PubMed:18304449, ECO:0000269\|PubMed:18753299, ECO:0000269\|PubMed:19447520, ECO:0000269\|PubMed:19756449, ECO:0000269\|PubMed:20511718, ECO:0000269\|PubMed:20730100, ECO:0000269\|PubMed:21865597}.
O00148	DDX39A	S43	ochoa	ATP-dependent RNA helicase DDX39A (EC 3.6.4.13) (DEAD box protein 39) (Nuclear RNA helicase URH49)	Helicase that plays an essential role in mRNA export and is involved in multiple steps in RNA metabolism including alternative splicing (PubMed:33941617, PubMed:38801080). Regulates nuclear mRNA export to the cytoplasm through association with ECD (PubMed:33941617). Also involved in spliceosomal uridine-rich small nuclear RNA (U snRNA) export by stimulating the RNA binding of adapter PHAX (PubMed:39011894). Plays a role in the negative regulation of type I IFN production by increasing the nuclear retention of antiviral transcripts and thus reducing their protein expression (PubMed:32393512). Independently of the interferon pathway, plays an antiviral role against alphaviruses by binding to a 5' conserved sequence element in the viral genomic RNA (PubMed:37949067). {ECO:0000269\|PubMed:15047853, ECO:0000269\|PubMed:17548965, ECO:0000269\|PubMed:32393512, ECO:0000269\|PubMed:33941617, ECO:0000269\|PubMed:37949067, ECO:0000269\|PubMed:38801080}.
O00273	DFFA	S308	ochoa	DNA fragmentation factor subunit alpha (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) (ICAD)	Inhibitor of the caspase-activated DNase (DFF40).
O00458	IFRD1	S21	ochoa	Interferon-related developmental regulator 1 (Nerve growth factor-inducible protein PC4)	Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity). {ECO:0000250}.
O00472	ELL2	S316	ochoa	RNA polymerase II elongation factor ELL2	Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:22195968, ECO:0000269\|PubMed:23251033}.
O00478	BTN3A3	S219	ochoa	Butyrophilin subfamily 3 member A3	Plays a role in T-cell responses in the adaptive immune response. {ECO:0000269\|PubMed:22767497}.
O00571	DDX3X	S34	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S76	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S92	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S590	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S612	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S615	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S616	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O14490	DLGAP1	S595	ochoa	Disks large-associated protein 1 (DAP-1) (Guanylate kinase-associated protein) (hGKAP) (PSD-95/SAP90-binding protein 1) (SAP90/PSD-95-associated protein 1) (SAPAP1)	Part of the postsynaptic scaffold in neuronal cells.
O14497	ARID1A	S610	ochoa	AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250\|UniProtKB:A2BH40, ECO:0000303\|PubMed:12672490, ECO:0000303\|PubMed:22952240, ECO:0000303\|PubMed:26601204}.
O14497	ARID1A	S769	ochoa	AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250\|UniProtKB:A2BH40, ECO:0000303\|PubMed:12672490, ECO:0000303\|PubMed:22952240, ECO:0000303\|PubMed:26601204}.
O14523	C2CD2L	S380	ochoa	Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (C2CD2-like) (Transmembrane protein 24)	Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (PubMed:28209843). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (PubMed:28209843). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (PubMed:28209843). Positively regulates insulin secretion in response to glucose: phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (PubMed:28209843). {ECO:0000269\|PubMed:28209843}.
O14523	C2CD2L	S619	ochoa	Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (C2CD2-like) (Transmembrane protein 24)	Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (PubMed:28209843). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (PubMed:28209843). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (PubMed:28209843). Positively regulates insulin secretion in response to glucose: phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (PubMed:28209843). {ECO:0000269\|PubMed:28209843}.
O14526	FCHO1	S622	ochoa	F-BAR domain only protein 1	Functions in an early step of clathrin-mediated endocytosis (PubMed:30822429). Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. Involved in the regulation of T-cell poliferation and activation (PubMed:30822429, PubMed:32098969). Affects TCR clustering upon receptor triggering and modulates its internalisation, playing a role in TCR-dependent T-cell activation (PubMed:32098969). {ECO:0000269\|PubMed:20448150, ECO:0000269\|PubMed:30822429, ECO:0000269\|PubMed:32098969}.
O14578	CIT	S405	ochoa	Citron Rho-interacting kinase (CRIK) (EC 2.7.11.1) (Serine/threonine-protein kinase 21)	Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. {ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:27453578}.
O14639	ABLIM1	S358	ochoa	Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin)	May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269\|PubMed:9245787}.
O14639	ABLIM1	S458	ochoa	Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin)	May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269\|PubMed:9245787}.
O14641	DVL2	S141	ochoa	Segment polarity protein dishevelled homolog DVL-2 (Dishevelled-2) (DSH homolog 2)	Plays a role in the signal transduction pathways mediated by multiple Wnt genes (PubMed:24616100). Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. {ECO:0000250\|UniProtKB:Q60838, ECO:0000269\|PubMed:19252499, ECO:0000269\|PubMed:24616100}.
O14646	CHD1	S1102	ochoa	Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.-) (ATP-dependent helicase CHD1)	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250\|UniProtKB:P40201, ECO:0000269\|PubMed:18042460, ECO:0000269\|PubMed:28866611}.
O14646	CHD1	S1546	ochoa	Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.-) (ATP-dependent helicase CHD1)	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250\|UniProtKB:P40201, ECO:0000269\|PubMed:18042460, ECO:0000269\|PubMed:28866611}.
O14654	IRS4	S463	ochoa	Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)	Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. {ECO:0000269\|PubMed:10531310, ECO:0000269\|PubMed:10594015, ECO:0000269\|PubMed:12639902, ECO:0000269\|PubMed:17408801, ECO:0000269\|PubMed:9553137}.
O14654	IRS4	S937	ochoa	Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)	Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. {ECO:0000269\|PubMed:10531310, ECO:0000269\|PubMed:10594015, ECO:0000269\|PubMed:12639902, ECO:0000269\|PubMed:17408801, ECO:0000269\|PubMed:9553137}.
O14662	STX16	S35	ochoa	Syntaxin-16 (Syn16)	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269\|PubMed:18195106}.
O14662	STX16	S41	ochoa	Syntaxin-16 (Syn16)	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269\|PubMed:18195106}.
O14686	KMT2D	S48	ochoa	Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.364) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17500065, PubMed:25561738). Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (PubMed:16603732). {ECO:0000269\|PubMed:16603732, ECO:0000269\|PubMed:17500065, ECO:0000269\|PubMed:25561738}.
O14686	KMT2D	S3208	ochoa	Histone-lysine N-methyltransferase 2D (Lysine N-methyltransferase 2D) (EC 2.1.1.364) (ALL1-related protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 2)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17500065, PubMed:25561738). Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (PubMed:16603732). {ECO:0000269\|PubMed:16603732, ECO:0000269\|PubMed:17500065, ECO:0000269\|PubMed:25561738}.
O14713	ITGB1BP1	S34	ochoa	Integrin beta-1-binding protein 1 (Integrin cytoplasmic domain-associated protein 1) (ICAP-1)	Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269\|PubMed:11741838, ECO:0000269\|PubMed:11807099, ECO:0000269\|PubMed:11919189, ECO:0000269\|PubMed:12473654, ECO:0000269\|PubMed:15703214, ECO:0000269\|PubMed:17916086, ECO:0000269\|PubMed:20616313, ECO:0000269\|PubMed:21768292, ECO:0000269\|Ref.19}.
O14715	RGPD8	S1486	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14715	RGPD8	S1585	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14715	RGPD8	S1592	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14733	MAP2K7	S61	ochoa	Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (Stress-activated protein kinase kinase 4) (SAPK kinase 4) (SAPKK-4) (SAPKK4) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). {ECO:0000269\|PubMed:28111074, ECO:0000269\|PubMed:9312068, ECO:0000269\|PubMed:9372971, ECO:0000269\|PubMed:9535930, ECO:0000269\|Ref.5}.
O14733	MAP2K7	S271	psp	Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (Stress-activated protein kinase kinase 4) (SAPK kinase 4) (SAPKK-4) (SAPKK4) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). {ECO:0000269\|PubMed:28111074, ECO:0000269\|PubMed:9312068, ECO:0000269\|PubMed:9372971, ECO:0000269\|PubMed:9535930, ECO:0000269\|Ref.5}.
O14745	NHERF1	S294	ochoa	Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1)	Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269\|PubMed:10499588, ECO:0000269\|PubMed:18784102, ECO:0000269\|PubMed:9096337, ECO:0000269\|PubMed:9430655}.
O14757	CHEK1	S286	ochoa\|psp	Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758). {ECO:0000250\|UniProtKB:O35280, ECO:0000269\|PubMed:10673501, ECO:0000269\|PubMed:11535615, ECO:0000269\|PubMed:12399544, ECO:0000269\|PubMed:12446774, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12676583, ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:12759351, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:14681206, ECO:0000269\|PubMed:14988723, ECO:0000269\|PubMed:15311285, ECO:0000269\|PubMed:15650047, ECO:0000269\|PubMed:15659650, ECO:0000269\|PubMed:15665856, ECO:0000269\|PubMed:16511572, ECO:0000269\|PubMed:17296736, ECO:0000269\|PubMed:17380128, ECO:0000269\|PubMed:18451105, ECO:0000269\|PubMed:18728393, ECO:0000269\|PubMed:19734889, ECO:0000269\|PubMed:20090422, ECO:0000269\|PubMed:31316063, ECO:0000269\|PubMed:32357935, ECO:0000269\|PubMed:33108758, ECO:0000269\|PubMed:9278511}.; FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition. {ECO:0000269\|PubMed:22184239}.
O14757	CHEK1	S307	ochoa	Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758). {ECO:0000250\|UniProtKB:O35280, ECO:0000269\|PubMed:10673501, ECO:0000269\|PubMed:11535615, ECO:0000269\|PubMed:12399544, ECO:0000269\|PubMed:12446774, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12676583, ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:12759351, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:14681206, ECO:0000269\|PubMed:14988723, ECO:0000269\|PubMed:15311285, ECO:0000269\|PubMed:15650047, ECO:0000269\|PubMed:15659650, ECO:0000269\|PubMed:15665856, ECO:0000269\|PubMed:16511572, ECO:0000269\|PubMed:17296736, ECO:0000269\|PubMed:17380128, ECO:0000269\|PubMed:18451105, ECO:0000269\|PubMed:18728393, ECO:0000269\|PubMed:19734889, ECO:0000269\|PubMed:20090422, ECO:0000269\|PubMed:31316063, ECO:0000269\|PubMed:32357935, ECO:0000269\|PubMed:33108758, ECO:0000269\|PubMed:9278511}.; FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition. {ECO:0000269\|PubMed:22184239}.
O14770	MEIS2	S204	ochoa	Homeobox protein Meis2 (Meis1-related protein 1)	Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription. {ECO:0000269\|PubMed:10764806, ECO:0000269\|PubMed:11279116, ECO:0000269\|PubMed:21746878}.
O14777	NDC80	S50	ochoa\|psp	Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC)	Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327, PubMed:30409912, PubMed:9315664). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592, PubMed:30409912). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules (PubMed:23891108, PubMed:25743205). {ECO:0000269\|PubMed:12351790, ECO:0000269\|PubMed:14654001, ECO:0000269\|PubMed:14699129, ECO:0000269\|PubMed:15062103, ECO:0000269\|PubMed:15235793, ECO:0000269\|PubMed:15239953, ECO:0000269\|PubMed:15548592, ECO:0000269\|PubMed:16732327, ECO:0000269\|PubMed:23085020, ECO:0000269\|PubMed:23891108, ECO:0000269\|PubMed:25743205, ECO:0000269\|PubMed:30409912, ECO:0000269\|PubMed:9315664}.
O14777	NDC80	S75	ochoa\|psp	Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC)	Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327, PubMed:30409912, PubMed:9315664). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592, PubMed:30409912). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules (PubMed:23891108, PubMed:25743205). {ECO:0000269\|PubMed:12351790, ECO:0000269\|PubMed:14654001, ECO:0000269\|PubMed:14699129, ECO:0000269\|PubMed:15062103, ECO:0000269\|PubMed:15235793, ECO:0000269\|PubMed:15239953, ECO:0000269\|PubMed:15548592, ECO:0000269\|PubMed:16732327, ECO:0000269\|PubMed:23085020, ECO:0000269\|PubMed:23891108, ECO:0000269\|PubMed:25743205, ECO:0000269\|PubMed:30409912, ECO:0000269\|PubMed:9315664}.
O14828	SCAMP3	S91	ochoa	Secretory carrier-associated membrane protein 3 (Secretory carrier membrane protein 3)	Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
O14893	GEMIN2	S87	ochoa	Gem-associated protein 2 (Gemin-2) (Component of gems 2) (Survival of motor neuron protein-interacting protein 1) (SMN-interacting protein 1)	The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9323129). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A (PubMed:18984161, PubMed:9323129). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound (PubMed:16314521, PubMed:21816274, PubMed:31799625). {ECO:0000269\|PubMed:16314521, ECO:0000269\|PubMed:18984161, ECO:0000269\|PubMed:21816274, ECO:0000269\|PubMed:31799625, ECO:0000269\|PubMed:9323129}.
O14920	IKBKB	S695	ochoa	Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697). {ECO:0000250\|UniProtKB:O88351, ECO:0000269\|PubMed:11297557, ECO:0000269\|PubMed:14673179, ECO:0000269\|PubMed:15084260, ECO:0000269\|PubMed:17213322, ECO:0000269\|PubMed:19716809, ECO:0000269\|PubMed:20410276, ECO:0000269\|PubMed:20434986, ECO:0000269\|PubMed:20797629, ECO:0000269\|PubMed:21138416, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:30337470, ECO:0000269\|PubMed:32209697, ECO:0000269\|PubMed:38621137, ECO:0000269\|PubMed:9346484}.
O14924	RGS12	S856	ochoa	Regulator of G-protein signaling 12 (RGS12)	Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. {ECO:0000250\|UniProtKB:O08774}.; FUNCTION: [Isoform 5]: Behaves as a cell cycle-dependent transcriptional repressor, promoting inhibition of S-phase DNA synthesis. {ECO:0000269\|PubMed:12024043}.
O14964	HGS	S315	ochoa	Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) (Protein pp110)	Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as a sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.
O14965	AURKA	S284	psp	Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Breast tumor-amplified kinase) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)	Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013). Phosphorylates MCRS1 which is required for MCRS1-mediated kinetochore fiber assembly and mitotic progression (PubMed:27192185). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735). {ECO:0000250\|UniProtKB:A0A8I3S724, ECO:0000269\|PubMed:11039908, ECO:0000269\|PubMed:11551964, ECO:0000269\|PubMed:12390251, ECO:0000269\|PubMed:13678582, ECO:0000269\|PubMed:14523000, ECO:0000269\|PubMed:14702041, ECO:0000269\|PubMed:15128871, ECO:0000269\|PubMed:15147269, ECO:0000269\|PubMed:15987997, ECO:0000269\|PubMed:17125279, ECO:0000269\|PubMed:17360485, ECO:0000269\|PubMed:17604723, ECO:0000269\|PubMed:18056443, ECO:0000269\|PubMed:18615013, ECO:0000269\|PubMed:19351716, ECO:0000269\|PubMed:19668197, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:20643351, ECO:0000269\|PubMed:26246606, ECO:0000269\|PubMed:27192185, ECO:0000269\|PubMed:27335426, ECO:0000269\|PubMed:28218735}.
O14974	PPP1R12A	S478	ochoa\|psp	Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269\|PubMed:18477460, ECO:0000269\|PubMed:19245366, ECO:0000269\|PubMed:20354225}.
O14974	PPP1R12A	S479	ochoa	Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269\|PubMed:18477460, ECO:0000269\|PubMed:19245366, ECO:0000269\|PubMed:20354225}.
O14980	XPO1	S397	ochoa	Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homolog)	Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. {ECO:0000269\|PubMed:15574332, ECO:0000269\|PubMed:20921223, ECO:0000269\|PubMed:9311922, ECO:0000269\|PubMed:9323133}.; FUNCTION: (Microbial infection) Mediates the export of unspliced or incompletely spliced RNAs out of the nucleus from different viruses including HIV-1, HTLV-1 and influenza A. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization. {ECO:0000269\|PubMed:14612415, ECO:0000269\|PubMed:9837918}.
O15013	ARHGEF10	S1289	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15013	ARHGEF10	S1291	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15014	ZNF609	S810	ochoa	Zinc finger protein 609	Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others. {ECO:0000250\|UniProtKB:Q8BZ47}.; FUNCTION: [Isoform 2]: Involved in the regulation of myoblast proliferation during myogenesis. {ECO:0000269\|PubMed:28344082}.
O15014	ZNF609	S842	ochoa	Zinc finger protein 609	Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others. {ECO:0000250\|UniProtKB:Q8BZ47}.; FUNCTION: [Isoform 2]: Involved in the regulation of myoblast proliferation during myogenesis. {ECO:0000269\|PubMed:28344082}.
O15027	SEC16A	S1250	psp	Protein transport protein Sec16A (SEC16 homolog A) (p250)	Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17005010, PubMed:17192411, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the cell membrane in adipocytes (By similarity). {ECO:0000250\|UniProtKB:E9QAT4, ECO:0000269\|PubMed:17005010, ECO:0000269\|PubMed:17192411, ECO:0000269\|PubMed:17428803, ECO:0000269\|PubMed:21768384, ECO:0000269\|PubMed:22355596, ECO:0000269\|PubMed:28067262, ECO:0000269\|PubMed:28442536, ECO:0000269\|PubMed:29300766}.
O15047	SETD1A	S534	ochoa	Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.364) (Lysine N-methyltransferase 2F) (SET domain-containing protein 1A) (hSET1A) (Set1/Ash2 histone methyltransferase complex subunit SET1)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:12670868, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:29937342, PubMed:31197650, PubMed:32346159). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis (By similarity) (PubMed:31197650). Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent nucleosome remodeling and RAD51 nucleofilaments stabilization at reversed forks, protecting them from nucleolytic degradation (PubMed:29937342, PubMed:32346159). Does not methylate 'Lys-4' of histone H3 if the neighboring 'Lys-9' residue is already methylated (PubMed:12670868). Binds RNAs involved in RNA processing and the DNA damage response (PubMed:38003223). {ECO:0000250\|UniProtKB:E9PYH6, ECO:0000269\|PubMed:12670868, ECO:0000269\|PubMed:25561738, ECO:0000269\|PubMed:29937342, ECO:0000269\|PubMed:31197650, ECO:0000269\|PubMed:32346159, ECO:0000269\|PubMed:38003223}.
O15055	PER2	S668	psp	Period circadian protein homolog 2 (hPER2) (Circadian clock protein PERIOD 2)	Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250\|UniProtKB:O54943}.
O15061	SYNM	S1217	ochoa	Synemin (Desmuslin)	Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteromeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells. {ECO:0000269\|PubMed:11353857, ECO:0000269\|PubMed:16777071, ECO:0000269\|PubMed:18028034}.
O15068	MCF2L	S981	ochoa	Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein)	Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42 (PubMed:15157669). {ECO:0000250\|UniProtKB:Q63406, ECO:0000269\|PubMed:15157669}.; FUNCTION: [Isoform 3]: Does not catalyze guanine nucleotide exchange on CDC42 (PubMed:15157669). {ECO:0000269\|PubMed:15157669}.
O15075	DCLK1	S313	ochoa	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
O15075	DCLK1	S352	ochoa	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
O15075	DCLK1	S353	ochoa	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
O15075	DCLK1	S358	ochoa	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
O15084	ANKRD28	S993	ochoa	Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A (PP6-ARS-A) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A) (Ankyrin repeat domain-containing protein 28) (Phosphatase interactor targeting protein hnRNP K) (PITK)	Regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation. Involved in the PP6-mediated dephosphorylation of MOB1 and induced focal adhesion assembly during cell migration (PubMed:35512830). {ECO:0000269\|PubMed:16564677, ECO:0000269\|PubMed:18186651, ECO:0000269\|PubMed:35512830}.
O15085	ARHGEF11	S35	ochoa	Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269\|PubMed:21670212}.
O15085	ARHGEF11	S657	ochoa	Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269\|PubMed:21670212}.
O15085	ARHGEF11	S1458	ochoa	Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269\|PubMed:21670212}.
O15119	TBX3	S438	ochoa	T-box transcription factor TBX3 (T-box protein 3)	Transcriptional repressor involved in developmental processes (PubMed:10468588). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:12000749). Probably plays a role in limb pattern formation (PubMed:10468588). Required for mammary placode induction, and maintenance of the mammary buds during development (By similarity). Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX2 (By similarity). Required, together with TBX2, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (By similarity). Involved in modulating early inner ear development, acting independently of, and also redundantly with, TBX2 in different subregions of the developing ear (By similarity). Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537). {ECO:0000250\|UniProtKB:P70324, ECO:0000269\|PubMed:10468588, ECO:0000269\|PubMed:12000749, ECO:0000269\|PubMed:22002537}.
O15143	ARPC1B	S336	ochoa	Actin-related protein 2/3 complex subunit 1B (Arp2/3 complex 41 kDa subunit) (p41-ARC)	Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:11741539, PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269\|PubMed:11741539, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:9230079}.
O15164	TRIM24	S660	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15164	TRIM24	S693	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15164	TRIM24	S773	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15327	INPP4B	S496	ochoa	Inositol polyphosphate 4-phosphatase type II (Type II inositol 3,4-bisphosphate 4-phosphatase) (EC 3.1.3.66)	Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 3,4-trisphosphate (PubMed:24070612, PubMed:24591580). Plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3,4-bisphosphate in membrane ruffles (PubMed:24591580). The lipid phosphatase activity is critical for tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:19647222, PubMed:24070612). {ECO:0000269\|PubMed:19647222, ECO:0000269\|PubMed:24070612, ECO:0000269\|PubMed:24591580}.
O15355	PPM1G	S201	ochoa	Protein phosphatase 1G (EC 3.1.3.16) (Protein phosphatase 1C) (Protein phosphatase 2C isoform gamma) (PP2C-gamma) (Protein phosphatase magnesium-dependent 1 gamma)	None
O15400	STX7	S81	ochoa	Syntaxin-7	May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.
O15400	STX7	S131	ochoa	Syntaxin-7	May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.
O15417	TNRC18	S269	ochoa	Trinucleotide repeat-containing gene 18 protein (Long CAG trinucleotide repeat-containing gene 79 protein)	None
O15417	TNRC18	S1863	ochoa	Trinucleotide repeat-containing gene 18 protein (Long CAG trinucleotide repeat-containing gene 79 protein)	None
O15439	ABCC4	S661	ochoa	ATP-binding cassette sub-family C member 4 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (MRP/cMOAT-related ABC transporter) (Multi-specific organic anion transporter B) (MOAT-B) (Multidrug resistance-associated protein 4)	ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins (PubMed:11856762, PubMed:12523936, PubMed:12835412, PubMed:12883481, PubMed:15364914, PubMed:15454390, PubMed:16282361, PubMed:17959747, PubMed:18300232, PubMed:26721430). Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4 (PubMed:17959747). Mediates the cotransport of bile acids with reduced glutathione (GSH) (PubMed:12523936, PubMed:12883481, PubMed:16282361). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (PubMed:11856762, PubMed:12105214, PubMed:15454390, PubMed:17344354, PubMed:18300232). Confers resistance to anticancer agents such as methotrexate (PubMed:11106685). {ECO:0000269\|PubMed:11106685, ECO:0000269\|PubMed:11856762, ECO:0000269\|PubMed:12105214, ECO:0000269\|PubMed:12523936, ECO:0000269\|PubMed:12835412, ECO:0000269\|PubMed:12883481, ECO:0000269\|PubMed:15364914, ECO:0000269\|PubMed:15454390, ECO:0000269\|PubMed:16282361, ECO:0000269\|PubMed:17344354, ECO:0000269\|PubMed:17959747, ECO:0000269\|PubMed:18300232, ECO:0000269\|PubMed:26721430}.
O15504	NUP42	S88	ochoa	Nucleoporin NUP42 (NLP-1) (NUP42 homolog) (Nucleoporin hCG1) (Nucleoporin-42) (Nucleoporin-like protein 2)	Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000269\|PubMed:10610322, ECO:0000269\|PubMed:16000379}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. {ECO:0000269\|PubMed:12228227}.
O15516	CLOCK	S437	psp	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O15516	CLOCK	S440	ochoa	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O15534	PER1	S815	ochoa	Period circadian protein homolog 1 (hPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)	Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/BMAL1 target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by BMAL1:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. {ECO:0000269\|PubMed:24005054}.
O15550	KDM6A	S824	ochoa	Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously-transcribed TPR protein on the X chromosome) (Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A)	Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17713478, PubMed:17761849, PubMed:17851529). Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27' (PubMed:17713478, PubMed:17761849, PubMed:17851529). Plays a central role in regulation of posterior development, by regulating HOX gene expression (PubMed:17851529). Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (PubMed:17761849). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (By similarity). {ECO:0000250\|UniProtKB:O70546, ECO:0000269\|PubMed:17713478, ECO:0000269\|PubMed:17761849, ECO:0000269\|PubMed:17851529, ECO:0000269\|PubMed:18003914}.
O43166	SIPA1L1	S1468	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43166	SIPA1L1	S1472	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43182	ARHGAP6	S335	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43182	ARHGAP6	S336	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43182	ARHGAP6	S338	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43182	ARHGAP6	S673	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43303	CCP110	S372	ochoa\|psp	Centriolar coiled-coil protein of 110 kDa (Centrosomal protein of 110 kDa) (CP110) (Cep110)	Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation (PubMed:17681131, PubMed:17719545, PubMed:23486064, PubMed:30375385, PubMed:35301795). Also involved in promoting ciliogenesis. May play a role in the assembly of the mother centriole subdistal appendages (SDA) thereby effecting the fusion of recycling endosomes to basal bodies during cilia formation (By similarity). Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (PubMed:16760425). {ECO:0000250\|UniProtKB:Q7TSH4, ECO:0000269\|PubMed:12361598, ECO:0000269\|PubMed:16760425, ECO:0000269\|PubMed:17681131, ECO:0000269\|PubMed:17719545, ECO:0000269\|PubMed:23486064, ECO:0000269\|PubMed:30375385, ECO:0000269\|PubMed:35301795}.
O43312	MTSS1	S322	psp	Protein MTSS 1 (Metastasis suppressor YGL-1) (Metastasis suppressor protein 1) (Missing in metastasis protein)	May be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton.
O43314	PPIP5K2	S1172	ochoa	Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (hsVIP2)	Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Required for normal hearing (PubMed:29590114). {ECO:0000269\|PubMed:17690096, ECO:0000269\|PubMed:17702752, ECO:0000269\|PubMed:21222653, ECO:0000269\|PubMed:29590114}.
O43353	RIPK2	S363	ochoa	Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)	Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269\|PubMed:14638696, ECO:0000269\|PubMed:17054981, ECO:0000269\|PubMed:17562858, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:21123652, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:22607974, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:28545134, ECO:0000269\|PubMed:28656966, ECO:0000269\|PubMed:29452636, ECO:0000269\|PubMed:30026309, ECO:0000269\|PubMed:30279485, ECO:0000269\|PubMed:30478312, ECO:0000269\|PubMed:9575181, ECO:0000269\|PubMed:9642260}.
O43379	WDR62	S1232	ochoa	WD repeat-containing protein 62	Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269\|PubMed:20729831, ECO:0000269\|PubMed:20890278, ECO:0000269\|PubMed:26297806}.
O43379	WDR62	S1255	ochoa	WD repeat-containing protein 62	Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function also seems to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269\|PubMed:20729831, ECO:0000269\|PubMed:20890278, ECO:0000269\|PubMed:26297806}.
O43516	WIPF1	S244	ochoa	WAS/WASL-interacting protein family member 1 (Protein PRPL-2) (Wiskott-Aldrich syndrome protein-interacting protein) (WASP-interacting protein)	Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus. {ECO:0000250, ECO:0000269\|PubMed:10878810, ECO:0000269\|PubMed:19910490, ECO:0000269\|PubMed:9405671}.
O43520	ATP8B1	S1232	ochoa	Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (Familial intrahepatic cholestasis type 1) (P4-ATPase flippase complex alpha subunit ATP8B1)	Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (PubMed:17948906, PubMed:25315773). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane (By similarity). Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (By similarity). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity (PubMed:20512993). Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (PubMed:25239307, PubMed:27301931). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (PubMed:20510206). Required for the preservation of cochlear hair cells in the inner ear (By similarity). May act as cardiolipin transporter during inflammatory injury (By similarity). {ECO:0000250\|UniProtKB:Q148W0, ECO:0000269\|PubMed:17948906, ECO:0000269\|PubMed:20510206, ECO:0000269\|PubMed:20512993, ECO:0000269\|PubMed:25239307, ECO:0000269\|PubMed:27301931}.
O43521	BCL2L11	S98	psp	Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)	Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis. {ECO:0000269\|PubMed:11997495, ECO:0000269\|PubMed:15486195, ECO:0000269\|PubMed:15661735, ECO:0000269\|PubMed:9430630}.
O43524	FOXO3	S215	psp	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43524	FOXO3	S300	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43524	FOXO3	S321	psp	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43524	FOXO3	S438	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43561	LAT	S41	ochoa	Linker for activation of T-cells family member 1 (36 kDa phosphotyrosine adapter protein) (pp36) (p36-38)	Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development (PubMed:23514740, PubMed:25907557). Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. {ECO:0000269\|PubMed:10072481, ECO:0000269\|PubMed:23514740, ECO:0000269\|PubMed:25907557}.
O43566	RGS14	S45	ochoa	Regulator of G-protein signaling 14 (RGS14)	Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. May be involved in visual memory processing capacity and hippocampal-based learning and memory. {ECO:0000269\|PubMed:15917656, ECO:0000269\|PubMed:17635935}.
O43663	PRC1	S500	ochoa	Protein regulator of cytokinesis 1	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269\|PubMed:12082078, ECO:0000269\|PubMed:15297875, ECO:0000269\|PubMed:15625105, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:17409436, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:20691902, ECO:0000269\|PubMed:9885575}.
O43663	PRC1	S563	ochoa	Protein regulator of cytokinesis 1	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269\|PubMed:12082078, ECO:0000269\|PubMed:15297875, ECO:0000269\|PubMed:15625105, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:17409436, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:20691902, ECO:0000269\|PubMed:9885575}.
O43663	PRC1	S577	psp	Protein regulator of cytokinesis 1	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269\|PubMed:12082078, ECO:0000269\|PubMed:15297875, ECO:0000269\|PubMed:15625105, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:17409436, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:20691902, ECO:0000269\|PubMed:9885575}.
O43683	BUB1	S602	ochoa	Mitotic checkpoint serine/threonine-protein kinase BUB1 (hBUB1) (EC 2.7.11.1) (BUB1A)	Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (PubMed:35044816). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269\|PubMed:10198256, ECO:0000269\|PubMed:15020684, ECO:0000269\|PubMed:15525512, ECO:0000269\|PubMed:15723797, ECO:0000269\|PubMed:16760428, ECO:0000269\|PubMed:17158872, ECO:0000269\|PubMed:19487456, ECO:0000269\|PubMed:20739936, ECO:0000269\|PubMed:35044816}.
O43683	BUB1	S608	ochoa	Mitotic checkpoint serine/threonine-protein kinase BUB1 (hBUB1) (EC 2.7.11.1) (BUB1A)	Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (PubMed:35044816). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269\|PubMed:10198256, ECO:0000269\|PubMed:15020684, ECO:0000269\|PubMed:15525512, ECO:0000269\|PubMed:15723797, ECO:0000269\|PubMed:16760428, ECO:0000269\|PubMed:17158872, ECO:0000269\|PubMed:19487456, ECO:0000269\|PubMed:20739936, ECO:0000269\|PubMed:35044816}.
O43683	BUB1	S667	psp	Mitotic checkpoint serine/threonine-protein kinase BUB1 (hBUB1) (EC 2.7.11.1) (BUB1A)	Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (PubMed:35044816). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269\|PubMed:10198256, ECO:0000269\|PubMed:15020684, ECO:0000269\|PubMed:15525512, ECO:0000269\|PubMed:15723797, ECO:0000269\|PubMed:16760428, ECO:0000269\|PubMed:17158872, ECO:0000269\|PubMed:19487456, ECO:0000269\|PubMed:20739936, ECO:0000269\|PubMed:35044816}.
O43707	ACTN4	S269	ochoa	Alpha-actinin-4 (Non-muscle alpha-actinin 4)	F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000250\|UniProtKB:P57780, ECO:0000269\|PubMed:15772161, ECO:0000269\|PubMed:22351778, ECO:0000269\|PubMed:22689882, ECO:0000305\|PubMed:9508771}.
O43719	HTATSF1	S391	ochoa	17S U2 SnRNP complex component HTATSF1 (HIV Tat-specific factor 1) (Tat-SF1)	Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). {ECO:0000269\|PubMed:10454543, ECO:0000269\|PubMed:10913173, ECO:0000269\|PubMed:11780068, ECO:0000269\|PubMed:30567737, ECO:0000269\|PubMed:32494006, ECO:0000269\|PubMed:34822310, ECO:0000269\|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:11420046, ECO:0000269\|PubMed:15905670, ECO:0000269\|PubMed:8849451, ECO:0000269\|PubMed:9765201}.
O43719	HTATSF1	S409	ochoa	17S U2 SnRNP complex component HTATSF1 (HIV Tat-specific factor 1) (Tat-SF1)	Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). {ECO:0000269\|PubMed:10454543, ECO:0000269\|PubMed:10913173, ECO:0000269\|PubMed:11780068, ECO:0000269\|PubMed:30567737, ECO:0000269\|PubMed:32494006, ECO:0000269\|PubMed:34822310, ECO:0000269\|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:11420046, ECO:0000269\|PubMed:15905670, ECO:0000269\|PubMed:8849451, ECO:0000269\|PubMed:9765201}.
O43719	HTATSF1	S485	ochoa	17S U2 SnRNP complex component HTATSF1 (HIV Tat-specific factor 1) (Tat-SF1)	Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). {ECO:0000269\|PubMed:10454543, ECO:0000269\|PubMed:10913173, ECO:0000269\|PubMed:11780068, ECO:0000269\|PubMed:30567737, ECO:0000269\|PubMed:32494006, ECO:0000269\|PubMed:34822310, ECO:0000269\|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:11420046, ECO:0000269\|PubMed:15905670, ECO:0000269\|PubMed:8849451, ECO:0000269\|PubMed:9765201}.
O43752	STX6	S133	ochoa	Syntaxin-6	SNARE promoting movement of transport vesicles to target membranes. Targets endosomes to the trans-Golgi network, and may therefore function in retrograde trafficking. Together with SNARE STX12, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. {ECO:0000250\|UniProtKB:Q63635}.
O43815	STRN	S382	ochoa	Striatin	Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). {ECO:0000269\|PubMed:18782753, ECO:0000305\|PubMed:26876214}.
O43865	AHCYL1	S74	psp	S-adenosylhomocysteine hydrolase-like protein 1 (DC-expressed AHCY-like molecule) (IP(3)Rs binding protein released with IP(3)) (IRBIT) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2)	Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate, competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. Promotes the formation of contact points between the endoplasmic reticulum (ER) and mitochondria, facilitating transfer of Ca(2+) from the ER to mitochondria (PubMed:27995898). Under normal cellular conditions, functions cooperatively with BCL2L10 to limit ITPR1-mediated Ca(2+) release but, under apoptotic stress conditions, dephosphorylated which promotes dissociation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes, inhibits BCL2L10 interaction with ITPR1 and leads to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates from ITPR1 to interact with CFTR and SLC26A6, mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (By similarity). {ECO:0000250\|UniProtKB:B5DFN2, ECO:0000250\|UniProtKB:Q80SW1, ECO:0000269\|PubMed:16769890, ECO:0000269\|PubMed:16793548, ECO:0000269\|PubMed:18829453, ECO:0000269\|PubMed:19224921, ECO:0000269\|PubMed:20584908, ECO:0000269\|PubMed:25237103, ECO:0000269\|PubMed:27995898}.
O43865	AHCYL1	S77	psp	S-adenosylhomocysteine hydrolase-like protein 1 (DC-expressed AHCY-like molecule) (IP(3)Rs binding protein released with IP(3)) (IRBIT) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2)	Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate, competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. Promotes the formation of contact points between the endoplasmic reticulum (ER) and mitochondria, facilitating transfer of Ca(2+) from the ER to mitochondria (PubMed:27995898). Under normal cellular conditions, functions cooperatively with BCL2L10 to limit ITPR1-mediated Ca(2+) release but, under apoptotic stress conditions, dephosphorylated which promotes dissociation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes, inhibits BCL2L10 interaction with ITPR1 and leads to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates from ITPR1 to interact with CFTR and SLC26A6, mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (By similarity). {ECO:0000250\|UniProtKB:B5DFN2, ECO:0000250\|UniProtKB:Q80SW1, ECO:0000269\|PubMed:16769890, ECO:0000269\|PubMed:16793548, ECO:0000269\|PubMed:18829453, ECO:0000269\|PubMed:19224921, ECO:0000269\|PubMed:20584908, ECO:0000269\|PubMed:25237103, ECO:0000269\|PubMed:27995898}.
O60238	BNIP3L	S91	ochoa	BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (Adenovirus E1B19K-binding protein B5) (BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A) (NIP3-like protein X) (NIP3L)	Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269\|PubMed:10381623, ECO:0000269\|PubMed:21264228}.
O60245	PCDH7	S982	ochoa	Protocadherin-7 (Brain-heart protocadherin) (BH-Pcdh)	None
O60268	KIAA0513	S79	ochoa	Uncharacterized protein KIAA0513	None
O60268	KIAA0513	S80	ochoa	Uncharacterized protein KIAA0513	None
O60271	SPAG9	S364	ochoa	C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (Cancer/testis antigen 89) (CT89) (Human lung cancer oncogene 6 protein) (HLC-6) (JNK-associated leucine-zipper protein) (JLP) (Mitogen-activated protein kinase 8-interacting protein 4) (Proliferation-inducing protein 6) (Protein highly expressed in testis) (PHET) (Sperm surface protein) (Sperm-associated antigen 9) (Sperm-specific protein) (Sunday driver 1)	The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250\|UniProtKB:Q58A65, ECO:0000269\|PubMed:14743216, ECO:0000269\|PubMed:29146937}.
O60271	SPAG9	S1244	ochoa	C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (Cancer/testis antigen 89) (CT89) (Human lung cancer oncogene 6 protein) (HLC-6) (JNK-associated leucine-zipper protein) (JLP) (Mitogen-activated protein kinase 8-interacting protein 4) (Proliferation-inducing protein 6) (Protein highly expressed in testis) (PHET) (Sperm surface protein) (Sperm-associated antigen 9) (Sperm-specific protein) (Sunday driver 1)	The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250\|UniProtKB:Q58A65, ECO:0000269\|PubMed:14743216, ECO:0000269\|PubMed:29146937}.
O60307	MAST3	S91	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S107	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S760	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S782	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S927	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S1099	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S1105	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60343	TBC1D4	S597	ochoa	TBC1 domain family member 4 (Akt substrate of 160 kDa) (AS160)	May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake. {ECO:0000269\|PubMed:15971998, ECO:0000269\|PubMed:18771725, ECO:0000269\|PubMed:22908308}.
O60343	TBC1D4	S757	ochoa	TBC1 domain family member 4 (Akt substrate of 160 kDa) (AS160)	May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake. {ECO:0000269\|PubMed:15971998, ECO:0000269\|PubMed:18771725, ECO:0000269\|PubMed:22908308}.
O60353	FZD6	S626	ochoa	Frizzled-6 (Fz-6) (hFz6)	Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear (By similarity). {ECO:0000250\|UniProtKB:Q61089}.
O60499	STX10	S140	ochoa	Syntaxin-10 (Syn10)	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269\|PubMed:18195106}.
O60499	STX10	S146	ochoa	Syntaxin-10 (Syn10)	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269\|PubMed:18195106}.
O60508	CDC40	S20	ochoa	Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (EH-binding protein 3) (Ehb3) (PRP17 homolog) (hPRP17)	Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:33220177, ECO:0000269\|PubMed:9830021}.
O60508	CDC40	S22	ochoa	Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (EH-binding protein 3) (Ehb3) (PRP17 homolog) (hPRP17)	Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:33220177, ECO:0000269\|PubMed:9830021}.
O60508	CDC40	S24	ochoa	Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (EH-binding protein 3) (Ehb3) (PRP17 homolog) (hPRP17)	Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:33220177, ECO:0000269\|PubMed:9830021}.
O60508	CDC40	S49	ochoa	Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (EH-binding protein 3) (Ehb3) (PRP17 homolog) (hPRP17)	Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:33220177, ECO:0000269\|PubMed:9830021}.
O60563	CCNT1	S569	ochoa	Cyclin-T1 (CycT1) (Cyclin-T)	Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539). {ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:29849146, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:35393539}.; FUNCTION: (Microbial infection) In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269\|PubMed:10329125, ECO:0000269\|PubMed:10329126}.
O60566	BUB1B	S676	ochoa\|psp	Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)	Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269\|PubMed:10477750, ECO:0000269\|PubMed:11702782, ECO:0000269\|PubMed:14706340, ECO:0000269\|PubMed:15020684, ECO:0000269\|PubMed:19411850, ECO:0000269\|PubMed:19503101}.
O60583	CCNT2	S480	ochoa	Cyclin-T2 (CycT2)	Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II) (PubMed:15563843, PubMed:9499409). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity). {ECO:0000250\|UniProtKB:Q7TQK0, ECO:0000269\|PubMed:11713533, ECO:0000269\|PubMed:15563843, ECO:0000269\|PubMed:16331689, ECO:0000269\|PubMed:9499409}.; FUNCTION: (Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters. {ECO:0000269\|PubMed:21509660}.
O60641	SNAP91	S306	ochoa	Clathrin coat assembly protein AP180 (91 kDa synaptosomal-associated protein) (Clathrin coat-associated protein AP180) (Phosphoprotein F1-20)	Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats (By similarity). {ECO:0000250}.
O60664	PLIN3	S37	ochoa	Perilipin-3 (47 kDa mannose 6-phosphate receptor-binding protein) (47 kDa MPR-binding protein) (Cargo selection protein TIP47) (Mannose-6-phosphate receptor-binding protein 1) (Placental protein 17) (PP17)	Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets (PubMed:34077757). Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network (PubMed:9590177). {ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:9590177}.
O60711	LPXN	S194	ochoa	Leupaxin	Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269\|PubMed:17640867, ECO:0000269\|PubMed:18451096, ECO:0000269\|PubMed:18497331, ECO:0000269\|PubMed:20543562}.
O60716	CTNND1	S352	ochoa	Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas))	Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). {ECO:0000269\|PubMed:10207085, ECO:0000269\|PubMed:14610055, ECO:0000269\|PubMed:17344476, ECO:0000269\|PubMed:18343367, ECO:0000269\|PubMed:20371349}.
O60716	CTNND1	Y865	ochoa	Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas))	Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). {ECO:0000269\|PubMed:10207085, ECO:0000269\|PubMed:14610055, ECO:0000269\|PubMed:17344476, ECO:0000269\|PubMed:18343367, ECO:0000269\|PubMed:20371349}.
O60716	CTNND1	S868	ochoa	Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas))	Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). {ECO:0000269\|PubMed:10207085, ECO:0000269\|PubMed:14610055, ECO:0000269\|PubMed:17344476, ECO:0000269\|PubMed:18343367, ECO:0000269\|PubMed:20371349}.
O60825	PFKFB2	S472	ochoa	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)]	Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269\|PubMed:11069105}.
O60885	BRD4	S494	psp	Bromodomain-containing protein 4 (Protein HUNK1)	Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250\|UniProtKB:Q9ESU6, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:19103749, ECO:0000269\|PubMed:19596240, ECO:0000269\|PubMed:22334664, ECO:0000269\|PubMed:22509028, ECO:0000269\|PubMed:23086925, ECO:0000269\|PubMed:23317504, ECO:0000269\|PubMed:23589332, ECO:0000269\|PubMed:24360279, ECO:0000269\|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269\|PubMed:23728299}.
O60885	BRD4	S1051	ochoa	Bromodomain-containing protein 4 (Protein HUNK1)	Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250\|UniProtKB:Q9ESU6, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:19103749, ECO:0000269\|PubMed:19596240, ECO:0000269\|PubMed:22334664, ECO:0000269\|PubMed:22509028, ECO:0000269\|PubMed:23086925, ECO:0000269\|PubMed:23317504, ECO:0000269\|PubMed:23589332, ECO:0000269\|PubMed:24360279, ECO:0000269\|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269\|PubMed:23728299}.
O60885	BRD4	S1070	ochoa	Bromodomain-containing protein 4 (Protein HUNK1)	Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250\|UniProtKB:Q9ESU6, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:19103749, ECO:0000269\|PubMed:19596240, ECO:0000269\|PubMed:22334664, ECO:0000269\|PubMed:22509028, ECO:0000269\|PubMed:23086925, ECO:0000269\|PubMed:23317504, ECO:0000269\|PubMed:23589332, ECO:0000269\|PubMed:24360279, ECO:0000269\|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269\|PubMed:23728299}.
O60934	NBN	S347	ochoa	Nibrin (Cell cycle regulatory protein p95) (Nijmegen breakage syndrome protein 1) (hNbs1)	Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:10888888, PubMed:15616588, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:23115235, PubMed:28216226, PubMed:28867292, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19759395, PubMed:28867292, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:19759395, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:19759395, PubMed:28867292, PubMed:9705271). Within the MRN complex, NBN acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed:12419185, PubMed:15616588, PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:19804756, PubMed:23762398, PubMed:24534091, PubMed:27814491, PubMed:27889449, PubMed:33836577). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (PubMed:12419185, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:24534091, PubMed:26438602). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed:15064416, PubMed:15616588, PubMed:15790808, PubMed:16622404, PubMed:22464731, PubMed:30952868, PubMed:35076389). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (PubMed:19759395, PubMed:27814491, PubMed:27889449, PubMed:33836577). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). The MRN complex is also required for the processing of R-loops (PubMed:31537797). NBN also functions in telomere length maintenance via its interaction with TERF2: interaction with TERF2 during G1 phase preventing recruitment of DCLRE1B/Apollo to telomeres (PubMed:10888888, PubMed:28216226). NBN also promotes DNA repair choice at dysfunctional telomeres: NBN phosphorylation by CDK2 promotes non-homologous end joining repair at telomeres, while unphosphorylated NBN promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (PubMed:23762398). {ECO:0000269\|PubMed:10888888, ECO:0000269\|PubMed:12419185, ECO:0000269\|PubMed:15064416, ECO:0000269\|PubMed:15616588, ECO:0000269\|PubMed:15790808, ECO:0000269\|PubMed:16622404, ECO:0000269\|PubMed:18411307, ECO:0000269\|PubMed:18582474, ECO:0000269\|PubMed:18583988, ECO:0000269\|PubMed:18678890, ECO:0000269\|PubMed:19759395, ECO:0000269\|PubMed:19804756, ECO:0000269\|PubMed:22464731, ECO:0000269\|PubMed:23115235, ECO:0000269\|PubMed:23762398, ECO:0000269\|PubMed:24534091, ECO:0000269\|PubMed:26438602, ECO:0000269\|PubMed:27814491, ECO:0000269\|PubMed:27889449, ECO:0000269\|PubMed:28216226, ECO:0000269\|PubMed:28867292, ECO:0000269\|PubMed:30787182, ECO:0000269\|PubMed:30952868, ECO:0000269\|PubMed:31537797, ECO:0000269\|PubMed:33836577, ECO:0000269\|PubMed:35076389, ECO:0000269\|PubMed:9705271}.
O75037	KIF21B	S1264	ochoa	Kinesin-like protein KIF21B	Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface. {ECO:0000250\|UniProtKB:Q9QXL1}.
O75037	KIF21B	S1275	ochoa	Kinesin-like protein KIF21B	Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface. {ECO:0000250\|UniProtKB:Q9QXL1}.
O75044	SRGAP2	S858	ochoa	SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)	Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250\|UniProtKB:Q91Z67, ECO:0000269\|PubMed:20810653, ECO:0000269\|PubMed:21148482, ECO:0000269\|PubMed:22559944, ECO:0000269\|PubMed:27373832, ECO:0000269\|PubMed:28333212}.
O75044	SRGAP2	S860	ochoa	SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)	Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250\|UniProtKB:Q91Z67, ECO:0000269\|PubMed:20810653, ECO:0000269\|PubMed:21148482, ECO:0000269\|PubMed:22559944, ECO:0000269\|PubMed:27373832, ECO:0000269\|PubMed:28333212}.
O75044	SRGAP2	S882	ochoa	SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)	Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250\|UniProtKB:Q91Z67, ECO:0000269\|PubMed:20810653, ECO:0000269\|PubMed:21148482, ECO:0000269\|PubMed:22559944, ECO:0000269\|PubMed:27373832, ECO:0000269\|PubMed:28333212}.
O75061	DNAJC6	S624	ochoa	Auxilin (EC 3.1.3.-) (DnaJ homolog subfamily C member 6)	May act as a protein phosphatase and/or a lipid phosphatase. Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intracellular trafficking (PubMed:18489706). Firstly, binds tightly to the clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion. The HSPA8:ATP complex then binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8 per triskelion leading to ATP hydrolysis stimulation and causing a conformational change in the HSPA8. This cycle is repeated three times to drive to a complex containing the clathrin-auxilin cage associated to three HSPA8:ADP complex. The ATP hydrolysis of the third HSPA8:ATP complex leads to a concerted dismantling of the cage into component triskelia. Then, dissociates from the released triskelia and be recycled to initiate another cycle of HSPA8's recruitment. Also acts during the early steps of clathrin-coated vesicle (CCV) formation through its interaction with the GTP bound form of DNM1 (By similarity). {ECO:0000250\|UniProtKB:Q27974, ECO:0000269\|PubMed:18489706}.
O75064	DENND4B	S1074	ochoa	DENN domain-containing protein 4B	Guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269\|PubMed:20937701}.
O75069	TMCC2	S475	ochoa	Transmembrane and coiled-coil domains protein 2 (Cerebral protein 11)	May be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE. {ECO:0000269\|PubMed:21593558}.
O75122	CLASP2	S316	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S330	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S529	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S1013	ochoa\|psp	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75140	DEPDC5	S503	ochoa	GATOR1 complex protein DEPDC5 (DEP domain-containing protein 5)	As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:31548394, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide-binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (PubMed:29590090, PubMed:35338845). However, it does not execute the GAP activity, which is mediated by NPRL2 (PubMed:29590090). {ECO:0000269\|PubMed:23723238, ECO:0000269\|PubMed:25457612, ECO:0000269\|PubMed:29590090, ECO:0000269\|PubMed:29769719, ECO:0000269\|PubMed:31548394, ECO:0000269\|PubMed:35338845}.
O75143	ATG13	S361	ochoa	Autophagy-related protein 13	Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269\|PubMed:18936157, ECO:0000269\|PubMed:19211835, ECO:0000269\|PubMed:19225151, ECO:0000269\|PubMed:19287211, ECO:0000269\|PubMed:21795849, ECO:0000269\|PubMed:21855797}.
O75152	ZC3H11A	S495	ochoa	Zinc finger CCCH domain-containing protein 11A	Through its association with TREX complex components, may participate in the export and post-transcriptional coordination of selected mRNA transcripts, including those required to maintain the metabolic processes in embryonic cells (PubMed:22928037, PubMed:37356722). Binds RNA (PubMed:29610341, PubMed:37356722). {ECO:0000269\|PubMed:22928037, ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.; FUNCTION: (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA export (PubMed:29610341). May be required for proper polyadenylation of adenovirus type 5/HAdV-5 capsid mRNA (PubMed:37356722). {ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.
O75152	ZC3H11A	S743	ochoa	Zinc finger CCCH domain-containing protein 11A	Through its association with TREX complex components, may participate in the export and post-transcriptional coordination of selected mRNA transcripts, including those required to maintain the metabolic processes in embryonic cells (PubMed:22928037, PubMed:37356722). Binds RNA (PubMed:29610341, PubMed:37356722). {ECO:0000269\|PubMed:22928037, ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.; FUNCTION: (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA export (PubMed:29610341). May be required for proper polyadenylation of adenovirus type 5/HAdV-5 capsid mRNA (PubMed:37356722). {ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.
O75164	KDM4A	S520	ochoa	Lysine-specific demethylase 4A (EC 1.14.11.66) (EC 1.14.11.69) (JmjC domain-containing histone demethylation protein 3A) (Jumonji domain-containing protein 2A) ([histone H3]-trimethyl-L-lysine(36) demethylase 4A) ([histone H3]-trimethyl-L-lysine(9) demethylase 4A)	Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:26741168, PubMed:21768309). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively. {ECO:0000269\|PubMed:16024779, ECO:0000269\|PubMed:16603238, ECO:0000269\|PubMed:21768309, ECO:0000269\|PubMed:26741168}.; FUNCTION: [Isoform 2]: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain. {ECO:0000269\|PubMed:21694756}.
O75164	KDM4A	S523	ochoa	Lysine-specific demethylase 4A (EC 1.14.11.66) (EC 1.14.11.69) (JmjC domain-containing histone demethylation protein 3A) (Jumonji domain-containing protein 2A) ([histone H3]-trimethyl-L-lysine(36) demethylase 4A) ([histone H3]-trimethyl-L-lysine(9) demethylase 4A)	Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:26741168, PubMed:21768309). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively. {ECO:0000269\|PubMed:16024779, ECO:0000269\|PubMed:16603238, ECO:0000269\|PubMed:21768309, ECO:0000269\|PubMed:26741168}.; FUNCTION: [Isoform 2]: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain. {ECO:0000269\|PubMed:21694756}.
O75175	CNOT3	S297	ochoa	CCR4-NOT transcription complex subunit 3 (CCR4-associated factor 3) (Leukocyte receptor cluster member 2)	Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269\|PubMed:14707134, ECO:0000269\|PubMed:22342980, ECO:0000269\|PubMed:22367759}.
O75179	ANKRD17	S2065	ochoa	Ankyrin repeat domain-containing protein 17 (Gene trap ankyrin repeat protein) (Serologically defined breast cancer antigen NY-BR-16)	Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250\|UniProtKB:Q99NH0, ECO:0000269\|PubMed:17276651, ECO:0000269\|PubMed:19150984, ECO:0000269\|PubMed:22328336, ECO:0000269\|PubMed:23711367}.
O75179	ANKRD17	S2457	ochoa	Ankyrin repeat domain-containing protein 17 (Gene trap ankyrin repeat protein) (Serologically defined breast cancer antigen NY-BR-16)	Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250\|UniProtKB:Q99NH0, ECO:0000269\|PubMed:17276651, ECO:0000269\|PubMed:19150984, ECO:0000269\|PubMed:22328336, ECO:0000269\|PubMed:23711367}.
O75362	ZNF217	S253	ochoa	Zinc finger protein 217	Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'. {ECO:0000269\|PubMed:16203743, ECO:0000269\|PubMed:16940172, ECO:0000269\|PubMed:17259635, ECO:0000269\|PubMed:18625718}.
O75362	ZNF217	S816	ochoa	Zinc finger protein 217	Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'. {ECO:0000269\|PubMed:16203743, ECO:0000269\|PubMed:16940172, ECO:0000269\|PubMed:17259635, ECO:0000269\|PubMed:18625718}.
O75369	FLNB	S1529	ochoa	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
O75369	FLNB	S2113	ochoa	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
O75369	FLNB	S2487	ochoa	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
O75369	FLNB	S2503	ochoa	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
O75376	NCOR1	S1117	ochoa	Nuclear receptor corepressor 1 (N-CoR) (N-CoR1)	Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250\|UniProtKB:Q60974, ECO:0000269\|PubMed:14527417, ECO:0000269\|PubMed:20812024}.
O75376	NCOR1	S1958	ochoa	Nuclear receptor corepressor 1 (N-CoR) (N-CoR1)	Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250\|UniProtKB:Q60974, ECO:0000269\|PubMed:14527417, ECO:0000269\|PubMed:20812024}.
O75376	NCOR1	S2259	ochoa	Nuclear receptor corepressor 1 (N-CoR) (N-CoR1)	Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250\|UniProtKB:Q60974, ECO:0000269\|PubMed:14527417, ECO:0000269\|PubMed:20812024}.
O75376	NCOR1	S2358	ochoa	Nuclear receptor corepressor 1 (N-CoR) (N-CoR1)	Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250\|UniProtKB:Q60974, ECO:0000269\|PubMed:14527417, ECO:0000269\|PubMed:20812024}.
O75381	PEX14	S268	ochoa	Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14)	Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:24235149, PubMed:28765278, PubMed:9653144). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role for peroxisome movement through a direct interaction with tubulin (PubMed:21525035). {ECO:0000250\|UniProtKB:P53112, ECO:0000269\|PubMed:21525035, ECO:0000269\|PubMed:24235149, ECO:0000269\|PubMed:28765278, ECO:0000269\|PubMed:9653144}.
O75381	PEX14	S271	ochoa	Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14)	Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:24235149, PubMed:28765278, PubMed:9653144). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role for peroxisome movement through a direct interaction with tubulin (PubMed:21525035). {ECO:0000250\|UniProtKB:P53112, ECO:0000269\|PubMed:21525035, ECO:0000269\|PubMed:24235149, ECO:0000269\|PubMed:28765278, ECO:0000269\|PubMed:9653144}.
O75385	ULK1	S544	ochoa	Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1)	Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708). {ECO:0000269\|PubMed:11146101, ECO:0000269\|PubMed:18936157, ECO:0000269\|PubMed:20921139, ECO:0000269\|PubMed:21460634, ECO:0000269\|PubMed:21795849, ECO:0000269\|PubMed:23524951, ECO:0000269\|PubMed:25040165, ECO:0000269\|PubMed:25126726, ECO:0000269\|PubMed:28821708, ECO:0000269\|PubMed:29487085, ECO:0000269\|PubMed:31123703, ECO:0000269\|PubMed:37306101}.
O75385	ULK1	S781	ochoa	Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1)	Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708). {ECO:0000269\|PubMed:11146101, ECO:0000269\|PubMed:18936157, ECO:0000269\|PubMed:20921139, ECO:0000269\|PubMed:21460634, ECO:0000269\|PubMed:21795849, ECO:0000269\|PubMed:23524951, ECO:0000269\|PubMed:25040165, ECO:0000269\|PubMed:25126726, ECO:0000269\|PubMed:28821708, ECO:0000269\|PubMed:29487085, ECO:0000269\|PubMed:31123703, ECO:0000269\|PubMed:37306101}.
O75391	SPAG7	S17	ochoa	Sperm-associated antigen 7	None
O75400	PRPF40A	S40	ochoa	Pre-mRNA-processing factor 40 homolog A (Fas ligand-associated factor 1) (Formin-binding protein 11) (Formin-binding protein 3) (Huntingtin yeast partner A) (Huntingtin-interacting protein 10) (HIP-10) (Huntingtin-interacting protein A) (Renal carcinoma antigen NY-REN-6)	Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269\|PubMed:21834987}.
O75400	PRPF40A	S42	ochoa	Pre-mRNA-processing factor 40 homolog A (Fas ligand-associated factor 1) (Formin-binding protein 11) (Formin-binding protein 3) (Huntingtin yeast partner A) (Huntingtin-interacting protein 10) (HIP-10) (Huntingtin-interacting protein A) (Renal carcinoma antigen NY-REN-6)	Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269\|PubMed:21834987}.
O75410	TACC1	S305	ochoa	Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1)	Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways (PubMed:20078863). Might promote the nuclear localization of the receptors (PubMed:20078863). Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. {ECO:0000269\|PubMed:20078863}.
O75410	TACC1	S497	ochoa	Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1)	Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways (PubMed:20078863). Might promote the nuclear localization of the receptors (PubMed:20078863). Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. {ECO:0000269\|PubMed:20078863}.
O75420	GIGYF1	S412	ochoa	GRB10-interacting GYF protein 1 (PERQ amino acid-rich with GYF domain-containing protein 1)	May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12771153}.
O75427	LRCH4	S313	ochoa	Leucine-rich repeat and calponin homology domain-containing protein 4 (Leucine-rich repeat neuronal protein 4) (Leucine-rich neuronal protein)	Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250\|UniProtKB:Q921G6}.
O75427	LRCH4	S506	ochoa	Leucine-rich repeat and calponin homology domain-containing protein 4 (Leucine-rich repeat neuronal protein 4) (Leucine-rich neuronal protein)	Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250\|UniProtKB:Q921G6}.
O75427	LRCH4	S521	ochoa	Leucine-rich repeat and calponin homology domain-containing protein 4 (Leucine-rich repeat neuronal protein 4) (Leucine-rich neuronal protein)	Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250\|UniProtKB:Q921G6}.
O75473	LGR5	S854	ochoa\|psp	Leucine-rich repeat-containing G-protein coupled receptor 5 (G-protein coupled receptor 49) (G-protein coupled receptor 67) (G-protein coupled receptor HG38)	Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269\|PubMed:21693646, ECO:0000269\|PubMed:21727895, ECO:0000269\|PubMed:21909076, ECO:0000269\|PubMed:22815884, ECO:0000269\|PubMed:23809763}.
O75581	LRP6	S1496	ochoa	Low-density lipoprotein receptor-related protein 6 (LRP-6)	Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931, PubMed:19801552, PubMed:28341812). Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931, PubMed:19801552, PubMed:28341812). The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalosomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin (PubMed:16513652). Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250\|UniProtKB:O88572, ECO:0000269\|PubMed:11357136, ECO:0000269\|PubMed:11448771, ECO:0000269\|PubMed:15778503, ECO:0000269\|PubMed:16341017, ECO:0000269\|PubMed:16513652, ECO:0000269\|PubMed:17326769, ECO:0000269\|PubMed:17400545, ECO:0000269\|PubMed:19107203, ECO:0000269\|PubMed:19293931, ECO:0000269\|PubMed:19801552, ECO:0000269\|PubMed:28341812}.
O75626	PRDM1	S342	ochoa	PR domain zinc finger protein 1 (EC 2.1.1.-) (BLIMP-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) (Positive regulatory domain I-binding factor 1) (PRDI-BF1) (PRDI-binding factor 1)	Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (By similarity). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (PubMed:1851123). Drives the maturation of B-lymphocytes into Ig secreting cells (PubMed:12626569). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (By similarity). Binds to the promoter and acts as a transcriptional repressor of IRF8, thereby promotes transcription of osteoclast differentiation factors such as NFATC1 and EEIG1 (By similarity). {ECO:0000250\|UniProtKB:Q60636, ECO:0000269\|PubMed:12626569, ECO:0000269\|PubMed:1851123}.
O75626	PRDM1	S361	ochoa	PR domain zinc finger protein 1 (EC 2.1.1.-) (BLIMP-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) (Positive regulatory domain I-binding factor 1) (PRDI-BF1) (PRDI-binding factor 1)	Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (By similarity). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (PubMed:1851123). Drives the maturation of B-lymphocytes into Ig secreting cells (PubMed:12626569). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (By similarity). Binds to the promoter and acts as a transcriptional repressor of IRF8, thereby promotes transcription of osteoclast differentiation factors such as NFATC1 and EEIG1 (By similarity). {ECO:0000250\|UniProtKB:Q60636, ECO:0000269\|PubMed:12626569, ECO:0000269\|PubMed:1851123}.
O75665	OFD1	S669	ochoa	Centriole and centriolar satellite protein OFD1 (Oral-facial-digital syndrome 1 protein) (Protein 71-7A)	Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164 (By similarity). Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis (PubMed:33934390). Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250\|UniProtKB:Q80Z25, ECO:0000269\|PubMed:33934390}.
O75665	OFD1	S850	ochoa	Centriole and centriolar satellite protein OFD1 (Oral-facial-digital syndrome 1 protein) (Protein 71-7A)	Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164 (By similarity). Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis (PubMed:33934390). Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250\|UniProtKB:Q80Z25, ECO:0000269\|PubMed:33934390}.
O75764	TCEA3	S145	ochoa	Transcription elongation factor A protein 3 (Transcription elongation factor S-II protein 3) (Transcription elongation factor TFIIS.h)	Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
O75925	PIAS1	S503	ochoa	E3 SUMO-protein ligase PIAS1 (EC 2.3.2.-) (DEAD/H box-binding protein 1) (E3 SUMO-protein transferase PIAS1) (Gu-binding protein) (GBP) (Protein inhibitor of activated STAT protein 1) (RNA helicase II-binding protein)	Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2 and PML (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway (PubMed:11583632, PubMed:11867732). In vitro, binds A/T-rich DNA (PubMed:15133049). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Mediates sumoylation of MRE11, stabilizing MRE11 on chromatin during end resection (PubMed:36050397). Sumoylates PML (at 'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation (By similarity). PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678). Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (By similarity). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumoylation activity (By similarity). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (By similarity). {ECO:0000250\|UniProtKB:O88907, ECO:0000269\|PubMed:11583632, ECO:0000269\|PubMed:11867732, ECO:0000269\|PubMed:14500712, ECO:0000269\|PubMed:15133049, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:36050397}.; FUNCTION: (Microbial infection) Restricts Epstein-Barr virus (EBV) lytic replication by acting as an inhibitor for transcription factors involved in lytic gene expression (PubMed:29262325). The virus can use apoptotic caspases to antagonize PIAS1-mediated restriction and express its lytic genes (PubMed:29262325). {ECO:0000269\|PubMed:29262325}.
O75970	MPDZ	S1593	ochoa	Multiple PDZ domain protein (Multi-PDZ domain protein 1)	Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250\|UniProtKB:O55164, ECO:0000269\|PubMed:11150294, ECO:0000269\|PubMed:15312654}.
O94804	STK10	S369	ochoa	Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269\|PubMed:11903060, ECO:0000269\|PubMed:12639966, ECO:0000269\|PubMed:19255442}.
O94804	STK10	S454	ochoa	Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269\|PubMed:11903060, ECO:0000269\|PubMed:12639966, ECO:0000269\|PubMed:19255442}.
O94806	PRKD3	S37	ochoa	Serine/threonine-protein kinase D3 (EC 2.7.11.13) (Protein kinase C nu type) (Protein kinase EPK2) (nPKC-nu)	Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). {ECO:0000250}.
O94875	SORBS2	S245	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94875	SORBS2	S1023	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94880	PHF14	S302	ochoa	PHD finger protein 14	Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity). {ECO:0000250\|UniProtKB:A0A286Y9D1, ECO:0000250\|UniProtKB:Q9D4H9, ECO:0000269\|PubMed:23688586}.
O94885	SASH1	S335	ochoa	SAM and SH3 domain-containing protein 1 (Proline-glutamate repeat-containing protein)	Is a positive regulator of NF-kappa-B signaling downstream of TLR4 activation. It acts as a scaffold molecule to assemble a molecular complex that includes TRAF6, MAP3K7, CHUK and IKBKB, thereby facilitating NF-kappa-B signaling activation (PubMed:23776175). Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:23776175). Involved in the regulation of cell mobility (PubMed:23333244, PubMed:23776175, PubMed:25315659). Regulates lipolysaccharide (LPS)-induced endothelial cell migration (PubMed:23776175). Is involved in the regulation of skin pigmentation through the control of melanocyte migration in the epidermis (PubMed:23333244). {ECO:0000269\|PubMed:23333244, ECO:0000269\|PubMed:23776175, ECO:0000269\|PubMed:25315659}.
O94887	FARP2	S408	ochoa	FERM, ARHGEF and pleckstrin domain-containing protein 2 (FERM domain-including RhoGEF) (FIR) (FERM, RhoGEF and pleckstrin domain-containing protein 2) (Pleckstrin homology domain-containing family C member 3) (PH domain-containing family C member 3)	Functions as a guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity). {ECO:0000250}.
O94915	FRYL	S218	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94915	FRYL	S1941	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94915	FRYL	S1978	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94915	FRYL	S2336	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94915	FRYL	S2338	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94916	NFAT5	S652	ochoa	Nuclear factor of activated T-cells 5 (NF-AT5) (T-cell transcription factor NFAT5) (Tonicity-responsive enhancer-binding protein) (TonE-binding protein) (TonEBP)	Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes. Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3' (PubMed:10377394). Mediates the transcriptional response to hypertonicity (PubMed:10051678). Positively regulates the transcription of LCN2 and S100A4 genes; optimal transactivation of these genes requires the presence of DDX5/DDX17 (PubMed:22266867). Also involved in the DNA damage response by preventing formation of R-loops; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:34049076). {ECO:0000269\|PubMed:10051678, ECO:0000269\|PubMed:10377394, ECO:0000269\|PubMed:22266867, ECO:0000269\|PubMed:34049076}.
O94929	ABLIM3	S379	ochoa	Actin-binding LIM protein 3 (abLIM-3) (Actin-binding LIM protein family member 3)	May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269\|PubMed:17194709}.
O94972	TRIM37	S803	ochoa	E3 ubiquitin-protein ligase TRIM37 (EC 2.3.2.27) (Mulibrey nanism protein) (RING-type E3 ubiquitin transferase TRIM37) (Tripartite motif-containing protein 37)	E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome (PubMed:28724525). Has anti-HIV activity (PubMed:24317724). {ECO:0000269\|PubMed:15885686, ECO:0000269\|PubMed:23769972, ECO:0000269\|PubMed:24317724, ECO:0000269\|PubMed:25470042, ECO:0000269\|PubMed:28724525}.
O95049	TJP3	S112	ochoa	Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250\|UniProtKB:O62683, ECO:0000250\|UniProtKB:Q9QXY1, ECO:0000269\|PubMed:16129888, ECO:0000269\|PubMed:21411630}.
O95071	UBR5	S618	ochoa	E3 ubiquitin-protein ligase UBR5 (EC 2.3.2.26) (E3 ubiquitin-protein ligase, HECT domain-containing 1) (Hyperplastic discs protein homolog) (hHYD) (Progestin-induced protein)	E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm and nucleus (PubMed:29033132, PubMed:33208877, PubMed:37478846, PubMed:37478862). Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates (PubMed:29033132, PubMed:37409633). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (By similarity). Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His) (By similarity). Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4 (PubMed:29033132). Together with ITCH, catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP, leading to its degradation: UBR5 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by ITCH (PubMed:29378950). Catalytic component of a nuclear protein quality control pathway that mediates ubiquitination and degradation of unpaired transcription factors (i.e. transcription factors that are not assembled into functional multiprotein complexes): specifically recognizes and binds degrons that are not accessible when transcription regulators are associated with their coactivators (PubMed:37478846, PubMed:37478862). Ubiquitinates various unpaired transcription regulator (MYC, SUPT4H1, SUPT5H, CDC20 and MCRS1), as well as ligand-bound nuclear receptors (ESR1, NR1H3, NR3C1, PGR, RARA, RXRA AND VDR) that are not associated with their nuclear receptor coactivators (NCOAs) (PubMed:33208877, PubMed:37478846, PubMed:37478862). Involved in maturation and/or transcriptional regulation of mRNA by mediating polyubiquitination and activation of CDK9 (PubMed:21127351). Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response (PubMed:11714696). Ubiquitinates acetylated PCK1 (PubMed:21726808). Acts as a positive regulator of the canonical Wnt signaling pathway by mediating (1) ubiquitination and stabilization of CTNNB1, and (2) 'Lys-48'-linked ubiquitination and degradation of TLE3 (PubMed:21118991, PubMed:28689657). Promotes disassembly of the mitotic checkpoint complex (MCC) from the APC/C complex by catalyzing ubiquitination of BUB1B, BUB3 and CDC20 (PubMed:35217622). Plays an essential role in extraembryonic development (By similarity). Required for the maintenance of skeletal tissue homeostasis by acting as an inhibitor of hedgehog (HH) signaling (By similarity). {ECO:0000250\|UniProtKB:Q80TP3, ECO:0000269\|PubMed:11714696, ECO:0000269\|PubMed:21118991, ECO:0000269\|PubMed:21127351, ECO:0000269\|PubMed:21726808, ECO:0000269\|PubMed:22884692, ECO:0000269\|PubMed:28689657, ECO:0000269\|PubMed:29033132, ECO:0000269\|PubMed:29378950, ECO:0000269\|PubMed:33208877, ECO:0000269\|PubMed:35217622, ECO:0000269\|PubMed:37409633, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:37478862}.
O95071	UBR5	S1741	ochoa	E3 ubiquitin-protein ligase UBR5 (EC 2.3.2.26) (E3 ubiquitin-protein ligase, HECT domain-containing 1) (Hyperplastic discs protein homolog) (hHYD) (Progestin-induced protein)	E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm and nucleus (PubMed:29033132, PubMed:33208877, PubMed:37478846, PubMed:37478862). Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates (PubMed:29033132, PubMed:37409633). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (By similarity). Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His) (By similarity). Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4 (PubMed:29033132). Together with ITCH, catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP, leading to its degradation: UBR5 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by ITCH (PubMed:29378950). Catalytic component of a nuclear protein quality control pathway that mediates ubiquitination and degradation of unpaired transcription factors (i.e. transcription factors that are not assembled into functional multiprotein complexes): specifically recognizes and binds degrons that are not accessible when transcription regulators are associated with their coactivators (PubMed:37478846, PubMed:37478862). Ubiquitinates various unpaired transcription regulator (MYC, SUPT4H1, SUPT5H, CDC20 and MCRS1), as well as ligand-bound nuclear receptors (ESR1, NR1H3, NR3C1, PGR, RARA, RXRA AND VDR) that are not associated with their nuclear receptor coactivators (NCOAs) (PubMed:33208877, PubMed:37478846, PubMed:37478862). Involved in maturation and/or transcriptional regulation of mRNA by mediating polyubiquitination and activation of CDK9 (PubMed:21127351). Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response (PubMed:11714696). Ubiquitinates acetylated PCK1 (PubMed:21726808). Acts as a positive regulator of the canonical Wnt signaling pathway by mediating (1) ubiquitination and stabilization of CTNNB1, and (2) 'Lys-48'-linked ubiquitination and degradation of TLE3 (PubMed:21118991, PubMed:28689657). Promotes disassembly of the mitotic checkpoint complex (MCC) from the APC/C complex by catalyzing ubiquitination of BUB1B, BUB3 and CDC20 (PubMed:35217622). Plays an essential role in extraembryonic development (By similarity). Required for the maintenance of skeletal tissue homeostasis by acting as an inhibitor of hedgehog (HH) signaling (By similarity). {ECO:0000250\|UniProtKB:Q80TP3, ECO:0000269\|PubMed:11714696, ECO:0000269\|PubMed:21118991, ECO:0000269\|PubMed:21127351, ECO:0000269\|PubMed:21726808, ECO:0000269\|PubMed:22884692, ECO:0000269\|PubMed:28689657, ECO:0000269\|PubMed:29033132, ECO:0000269\|PubMed:29378950, ECO:0000269\|PubMed:33208877, ECO:0000269\|PubMed:35217622, ECO:0000269\|PubMed:37409633, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:37478862}.
O95155	UBE4B	S105	ochoa	Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250\|UniProtKB:P54860, ECO:0000250\|UniProtKB:Q9ES00, ECO:0000269\|PubMed:17369820}.
O95155	UBE4B	S317	ochoa	Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250\|UniProtKB:P54860, ECO:0000250\|UniProtKB:Q9ES00, ECO:0000269\|PubMed:17369820}.
O95197	RTN3	S23	ochoa	Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII)	May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules (PubMed:25612671). Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition. {ECO:0000269\|PubMed:15286784, ECO:0000269\|PubMed:16054885, ECO:0000269\|PubMed:17031492, ECO:0000269\|PubMed:17191123, ECO:0000269\|PubMed:25612671}.; FUNCTION: (Microbial infection) Plays a positive role in viral replication and pathogenesis of enteroviruses. {ECO:0000269\|PubMed:17182608}.
O95208	EPN2	S178	ochoa	Epsin-2 (EPS-15-interacting protein 2)	Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269\|PubMed:10567358}.
O95208	EPN2	S479	ochoa	Epsin-2 (EPS-15-interacting protein 2)	Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269\|PubMed:10567358}.
O95210	STBD1	S61	ochoa	Starch-binding domain-containing protein 1 (Genethonin-1) (Glycophagy cargo receptor STBD1)	Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000269\|PubMed:20810658, ECO:0000269\|PubMed:21893048, ECO:0000269\|PubMed:24837458}.
O95232	LUC7L3	S116	ochoa	Luc7-like protein 3 (Cisplatin resistance-associated-overexpressed protein) (Luc7A) (Okadaic acid-inducible phosphoprotein OA48-18) (cAMP regulatory element-associated protein 1) (CRE-associated protein 1) (CREAP-1)	Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. {ECO:0000269\|PubMed:16462885}.
O95235	KIF20A	S47	ochoa	Kinesin-like protein KIF20A (GG10_2) (Mitotic kinesin-like protein 2) (MKlp2) (Rab6-interacting kinesin-like protein) (Rabkinesin-6)	Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269\|PubMed:12939256}.
O95235	KIF20A	S244	psp	Kinesin-like protein KIF20A (GG10_2) (Mitotic kinesin-like protein 2) (MKlp2) (Rab6-interacting kinesin-like protein) (Rabkinesin-6)	Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269\|PubMed:12939256}.
O95297	MPZL1	S210	ochoa	Myelin protein zero-like protein 1 (Protein zero-related)	Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269\|PubMed:11751924, ECO:0000269\|PubMed:12410637}.
O95359	TACC2	S2092	ochoa	Transforming acidic coiled-coil-containing protein 2 (Anti-Zuai-1) (AZU-1)	Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. {ECO:0000250, ECO:0000269\|PubMed:10749935}.
O95359	TACC2	S2256	ochoa	Transforming acidic coiled-coil-containing protein 2 (Anti-Zuai-1) (AZU-1)	Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. {ECO:0000250, ECO:0000269\|PubMed:10749935}.
O95425	SVIL	S86	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95425	SVIL	S227	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95425	SVIL	S237	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95425	SVIL	S920	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95475	SIX6	S227	ochoa	Homeobox protein SIX6 (Homeodomain protein OPTX2) (Optic homeobox 2) (Sine oculis homeobox homolog 6)	May be involved in eye development.
O95487	SEC24B	S325	ochoa	Protein transport protein Sec24B (SEC24-related protein B)	Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:18843296, PubMed:20427317). Plays a central role in cargo selection within the COPII complex and together with SEC24A may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may also recognize conformational epitopes (PubMed:17499046, PubMed:18843296). {ECO:0000269\|PubMed:17499046, ECO:0000269\|PubMed:18843296, ECO:0000269\|PubMed:20427317}.
O95490	ADGRL2	S1387	ochoa	Adhesion G protein-coupled receptor L2 (Calcium-independent alpha-latrotoxin receptor 2) (CIRL-2) (Latrophilin homolog 1) (Latrophilin-2) (Lectomedin-1)	Orphan adhesion G-protein coupled receptor (aGPCR), which mediates synapse specificity (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (By similarity). Following G-protein coupled receptor activation, associates with cell adhesion molecules that are expressed at the surface of adjacent cells to direct synapse specificity. Specifically mediates the establishment of perforant-path synapses on CA1-region pyramidal neurons in the hippocampus. Localizes to postsynaptic spines in excitatory synapses in the S.lacunosum-moleculare and interacts with presynaptic cell adhesion molecules, such as teneurins, promoting synapse formation (By similarity). {ECO:0000250\|UniProtKB:Q80TS3, ECO:0000250\|UniProtKB:Q8JZZ7}.
O95613	PCNT	S2195	ochoa	Pericentrin (Kendrin) (Pericentrin-B)	Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269\|PubMed:10823944, ECO:0000269\|PubMed:11171385, ECO:0000269\|PubMed:18955030, ECO:0000269\|PubMed:20599736, ECO:0000269\|PubMed:30420784}.
O95613	PCNT	S2327	ochoa	Pericentrin (Kendrin) (Pericentrin-B)	Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269\|PubMed:10823944, ECO:0000269\|PubMed:11171385, ECO:0000269\|PubMed:18955030, ECO:0000269\|PubMed:20599736, ECO:0000269\|PubMed:30420784}.
O95674	CDS2	S41	ochoa	Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2)	Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (PubMed:25375833). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (PubMed:25375833). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540, PubMed:31548309). {ECO:0000269\|PubMed:25375833, ECO:0000269\|PubMed:26946540, ECO:0000269\|PubMed:31548309}.
O95684	CEP43	S166	ochoa	Centrosomal protein 43 (FGFR1 oncogene partner)	Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385). {ECO:0000269\|PubMed:16314388, ECO:0000269\|PubMed:28625565, ECO:0000269\|PubMed:28659385}.
O95684	CEP43	S215	ochoa	Centrosomal protein 43 (FGFR1 oncogene partner)	Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385). {ECO:0000269\|PubMed:16314388, ECO:0000269\|PubMed:28625565, ECO:0000269\|PubMed:28659385}.
O95772	STARD3NL	S21	ochoa	STARD3 N-terminal-like protein (MLN64 N-terminal domain homolog)	Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (PubMed:24105263). {ECO:0000269\|PubMed:24105263}.
O95810	CAVIN2	S293	ochoa	Caveolae-associated protein 2 (Cavin-2) (PS-p68) (Phosphatidylserine-binding protein) (Serum deprivation-response protein)	Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity). {ECO:0000250\|UniProtKB:Q66H98, ECO:0000269\|PubMed:19525939}.
O95816	BAG2	S25	ochoa	BAG family molecular chaperone regulator 2 (BAG-2) (Bcl-2-associated athanogene 2)	Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release (PubMed:24318877, PubMed:9873016). {ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S187	ochoa\|psp	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S190	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S289	ochoa\|psp	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95999	BCL10	S144	psp	B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)	Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:24074955, PubMed:25365219). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:24074955). Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (PubMed:24074955). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:18287044, PubMed:24074955, PubMed:27777308). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity (PubMed:26488816). Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (PubMed:18264101, PubMed:18287044, PubMed:24074955, PubMed:27777308). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (PubMed:10187815). {ECO:0000269\|PubMed:10187770, ECO:0000269\|PubMed:10187815, ECO:0000269\|PubMed:10364242, ECO:0000269\|PubMed:10400625, ECO:0000269\|PubMed:18264101, ECO:0000269\|PubMed:18287044, ECO:0000269\|PubMed:24074955, ECO:0000269\|PubMed:25365219, ECO:0000269\|PubMed:26488816, ECO:0000269\|PubMed:27777308}.
P00533	EGFR	S1042	ochoa\|psp	Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)	Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity). {ECO:0000250\|UniProtKB:Q01279, ECO:0000269\|PubMed:10805725, ECO:0000269\|PubMed:11116146, ECO:0000269\|PubMed:11483589, ECO:0000269\|PubMed:11602604, ECO:0000269\|PubMed:12297049, ECO:0000269\|PubMed:12297050, ECO:0000269\|PubMed:12620237, ECO:0000269\|PubMed:12873986, ECO:0000269\|PubMed:15374980, ECO:0000269\|PubMed:15590694, ECO:0000269\|PubMed:15611079, ECO:0000269\|PubMed:17115032, ECO:0000269\|PubMed:17909029, ECO:0000269\|PubMed:19560417, ECO:0000269\|PubMed:20462955, ECO:0000269\|PubMed:20837704, ECO:0000269\|PubMed:21258366, ECO:0000269\|PubMed:27153536, ECO:0000269\|PubMed:2790960, ECO:0000269\|PubMed:35538033, ECO:0000269\|PubMed:7679104, ECO:0000269\|PubMed:8144591, ECO:0000269\|PubMed:9419975}.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269\|PubMed:21516087}.
P00533	EGFR	S1045	ochoa	Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)	Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity). {ECO:0000250\|UniProtKB:Q01279, ECO:0000269\|PubMed:10805725, ECO:0000269\|PubMed:11116146, ECO:0000269\|PubMed:11483589, ECO:0000269\|PubMed:11602604, ECO:0000269\|PubMed:12297049, ECO:0000269\|PubMed:12297050, ECO:0000269\|PubMed:12620237, ECO:0000269\|PubMed:12873986, ECO:0000269\|PubMed:15374980, ECO:0000269\|PubMed:15590694, ECO:0000269\|PubMed:15611079, ECO:0000269\|PubMed:17115032, ECO:0000269\|PubMed:17909029, ECO:0000269\|PubMed:19560417, ECO:0000269\|PubMed:20462955, ECO:0000269\|PubMed:20837704, ECO:0000269\|PubMed:21258366, ECO:0000269\|PubMed:27153536, ECO:0000269\|PubMed:2790960, ECO:0000269\|PubMed:35538033, ECO:0000269\|PubMed:7679104, ECO:0000269\|PubMed:8144591, ECO:0000269\|PubMed:9419975}.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269\|PubMed:21516087}.
P01833	PIGR	S708	ochoa	Polymeric immunoglobulin receptor (PIgR) (Poly-Ig receptor) (Hepatocellular carcinoma-associated protein TB6) [Cleaved into: Secretory component]	[Polymeric immunoglobulin receptor]: Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. {ECO:0000269\|PubMed:10229845, ECO:0000269\|PubMed:15530357, ECO:0000269\|PubMed:9379029}.; FUNCTION: [Secretory component]: Through its N-linked glycans ensures anchoring of secretory IgA (sIgA) molecules to mucus lining the epithelial surface to neutralize extracellular pathogens (PubMed:12150896). On its own (free form) may act as a non-specific microbial scavenger to prevent pathogen interaction with epithelial cells (PubMed:16543244). {ECO:0000269\|PubMed:12150896, ECO:0000269\|PubMed:16543244}.
P02545	LMNA	S307	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P02545	LMNA	S398	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P02545	LMNA	S618	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P02545	LMNA	S619	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P02671	FGA	S291	ochoa	Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]	Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250\|UniProtKB:E9PV24}.
P02671	FGA	S297	ochoa	Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]	Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250\|UniProtKB:E9PV24}.
P02730	SLC4A1	S356	ochoa	Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233)	Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). {ECO:0000269\|PubMed:10926824, ECO:0000269\|PubMed:14734552, ECO:0000269\|PubMed:1538405, ECO:0000269\|PubMed:16227998, ECO:0000269\|PubMed:20151848, ECO:0000269\|PubMed:24121512, ECO:0000269\|PubMed:28387307, ECO:0000269\|PubMed:35835865}.; FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305). {ECO:0000269\|PubMed:12692305, ECO:0000269\|PubMed:14630931}.
P02765	AHSG	S334	ochoa	Alpha-2-HS-glycoprotein (Alpha-2-Z-globulin) (Ba-alpha-2-glycoprotein) (Fetuin-A) [Cleaved into: Alpha-2-HS-glycoprotein chain A; Alpha-2-HS-glycoprotein chain B]	Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.
P03952	KLKB1	S67	ochoa	Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) (PKK) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light chain]	Participates in the surface-dependent activation of blood coagulation. Activates, in a reciprocal reaction, coagulation factor XII/F12 after binding to negatively charged surfaces. Releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
P04004	VTN	S403	ochoa	Vitronectin (VN) (S-protein) (Serum-spreading factor) (V75) [Cleaved into: Vitronectin V65 subunit; Vitronectin V10 subunit; Somatomedin-B]	Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
P04049	RAF1	S289	ochoa\|psp	RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269\|PubMed:11427728, ECO:0000269\|PubMed:11719507, ECO:0000269\|PubMed:15385642, ECO:0000269\|PubMed:15618521, ECO:0000269\|PubMed:15849194, ECO:0000269\|PubMed:16892053, ECO:0000269\|PubMed:16924233, ECO:0000269\|PubMed:9360956}.
P04049	RAF1	S295	ochoa	RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269\|PubMed:11427728, ECO:0000269\|PubMed:11719507, ECO:0000269\|PubMed:15385642, ECO:0000269\|PubMed:15618521, ECO:0000269\|PubMed:15849194, ECO:0000269\|PubMed:16892053, ECO:0000269\|PubMed:16924233, ECO:0000269\|PubMed:9360956}.
P04439	HLA-A	S343	psp	HLA class I histocompatibility antigen, A alpha chain (Human leukocyte antigen A) (HLA-A)	Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:1402688, PubMed:15893615, PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, PubMed:24395804, PubMed:2456340, PubMed:2784196, PubMed:28250417, PubMed:7504010, PubMed:7694806, PubMed:9862734). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, PubMed:7679507). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17079320, PubMed:17189421, PubMed:20364150, PubMed:26929325, PubMed:27049119). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:7504010, PubMed:9862734). {ECO:0000269\|PubMed:10449296, ECO:0000269\|PubMed:12138174, ECO:0000269\|PubMed:12393434, ECO:0000269\|PubMed:12796775, ECO:0000269\|PubMed:1402688, ECO:0000269\|PubMed:15893615, ECO:0000269\|PubMed:17079320, ECO:0000269\|PubMed:17189421, ECO:0000269\|PubMed:18275829, ECO:0000269\|PubMed:19542454, ECO:0000269\|PubMed:19543285, ECO:0000269\|PubMed:20364150, ECO:0000269\|PubMed:21498667, ECO:0000269\|PubMed:24192765, ECO:0000269\|PubMed:24395804, ECO:0000269\|PubMed:2456340, ECO:0000269\|PubMed:25880248, ECO:0000269\|PubMed:26929325, ECO:0000269\|PubMed:27049119, ECO:0000269\|PubMed:2784196, ECO:0000269\|PubMed:28250417, ECO:0000269\|PubMed:7504010, ECO:0000269\|PubMed:7506728, ECO:0000269\|PubMed:7679507, ECO:0000269\|PubMed:7694806, ECO:0000269\|PubMed:9862734}.; FUNCTION: Allele A01:01: Presents a restricted peptide repertoire including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY), IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon protein (LTDLGQNLLY), SARS-CoV-2 3a/ORF3a (FTSDYYQLY) as well as tumor peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and WT1 (TSEKRPFMCAY), all having in common a canonical motif with a negatively charged Asp or Glu residue at position 3 and a Tyr anchor residue at the C-terminus (PubMed:1402688, PubMed:17189421, PubMed:19177349, PubMed:20364150, PubMed:24395804, PubMed:25880248, PubMed:26758806, PubMed:30530481, PubMed:32887977, PubMed:7504010). A number of HLA-A01:01-restricted peptides carry a post-translational modification with oxidation and N-terminal acetylation being the most frequent (PubMed:25880248). Fails to present highly immunogenic peptides from the EBV latent antigens (PubMed:18779413). {ECO:0000269\|PubMed:1402688, ECO:0000269\|PubMed:17189421, ECO:0000269\|PubMed:18779413, ECO:0000269\|PubMed:19177349, ECO:0000269\|PubMed:20364150, ECO:0000269\|PubMed:24395804, ECO:0000269\|PubMed:25880248, ECO:0000269\|PubMed:26758806, ECO:0000269\|PubMed:30530481, ECO:0000269\|PubMed:7504010}.; FUNCTION: Allele A02:01: A major allele in human populations, presents immunodominant viral epitopes derived from IAV M/matrix protein 1 (GILGFVFTL), HIV-1 env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1 Tax (LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65 (NLVPMVATV) as well as tumor peptide antigens including MAGEA4 (GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all having in common hydrophobic amino acids at position 2 and at the C-terminal anchors. {ECO:0000269\|PubMed:11502003, ECO:0000269\|PubMed:12138174, ECO:0000269\|PubMed:12796775, ECO:0000269\|PubMed:17079320, ECO:0000269\|PubMed:18275829, ECO:0000269\|PubMed:19542454, ECO:0000269\|PubMed:20619457, ECO:0000269\|PubMed:22245737, ECO:0000269\|PubMed:26929325, ECO:0000269\|PubMed:2784196, ECO:0000269\|PubMed:28250417, ECO:0000269\|PubMed:7694806, ECO:0000269\|PubMed:7935798, ECO:0000269\|PubMed:8630735, ECO:0000269\|PubMed:8805302, ECO:0000269\|PubMed:8906788, ECO:0000269\|PubMed:9177355}.; FUNCTION: Allele A03:01: Presents viral epitopes derived from IAV NP (ILRGSVAHK), HIV-1 nef (QVPLRPMTYK), HIV-1 gag-pol (AIFQSSMTK), SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) as well as tumor peptide antigens including PMEL (LIYRRRLMK), NODAL (HAYIQSLLK), TRP-2 (RMYNMVPFF), all having in common hydrophobic amino acids at position 2 and Lys or Arg anchor residues at the C-terminus (PubMed:19543285, PubMed:21943705, PubMed:2456340, PubMed:32887977, PubMed:7504010, PubMed:7679507, PubMed:9862734). May also display spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (PubMed:27049119). {ECO:0000269\|PubMed:19543285, ECO:0000269\|PubMed:21943705, ECO:0000269\|PubMed:2456340, ECO:0000269\|PubMed:27049119, ECO:0000269\|PubMed:7504010, ECO:0000269\|PubMed:7679507, ECO:0000269\|PubMed:9862734}.; FUNCTION: Allele A11:01: Presents several immunodominant epitopes derived from HIV-1 gag-pol and HHV-4 EBNA4, containing the peptide motif with Val, Ile, Thr, Leu, Tyr or Phe at position 2 and Lys anchor residue at the C-terminus. Important in the control of HIV-1, EBV and HBV infections (PubMed:10449296). Presents an immunodominant epitope derived from SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) (PubMed:32887977). {ECO:0000269\|PubMed:10449296, ECO:0000269\|PubMed:32887977}.; FUNCTION: Allele A23:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response. {ECO:0000269\|PubMed:17182537}.; FUNCTION: Allele A24:02: Presents viral epitopes derived from HIV-1 nef (RYPLTFGWCF), EBV lytic- and latent-cycle antigens BRLF1 (TYPVLEEMF), BMLF1 (DYNFVKQLF) and LMP2 (IYVLVMLVL), SARS-CoV nucleocapsid/N (QFKDNVILL), as well as tumor peptide antigens including PRAME (LYVDSLFFL), all sharing a common signature motif, namely an aromatic residue Tyr or Phe at position 2 and a nonhydrophobic anchor residue Phe, Leu or Iso at the C-terminus (PubMed:12393434, PubMed:20844028, PubMed:24192765, PubMed:9047241). Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response (PubMed:17182537, PubMed:18502829). {ECO:0000269\|PubMed:12393434, ECO:0000269\|PubMed:17182537, ECO:0000269\|PubMed:18502829, ECO:0000269\|PubMed:20844028, ECO:0000269\|PubMed:24192765, ECO:0000269\|PubMed:9047241}.; FUNCTION: Allele A26:01: Presents several epitopes derived from HIV-1 gag-pol (EVIPMFSAL, ETKLGKAGY) and env (LVSDGGPNLY), carrying as anchor residues preferentially Glu at position 1, Val or Thr at position 2 and Tyr at the C-terminus. {ECO:0000269\|PubMed:15893615}.; FUNCTION: Allele A29:02: Presents peptides having a common motif, namely a Glu residue at position 2 and Tyr or Leu anchor residues at the C-terminus. {ECO:0000269\|PubMed:8622959}.; FUNCTION: Allele A32:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response. {ECO:0000269\|PubMed:17182537}.; FUNCTION: Allele A68:01: Presents viral epitopes derived from IAV NP (KTGGPIYKR) and HIV-1 tat (ITKGLGISYGR), having a common signature motif namely, Val or Thr at position 2 and positively charged residues Arg or Lys at the C-terminal anchor. {ECO:0000269\|PubMed:1448153, ECO:0000269\|PubMed:1448154, ECO:0000269\|PubMed:2784196}.; FUNCTION: Allele A74:01: Presents immunodominant HIV-1 epitopes derived from gag-pol (GQMVHQAISPR, QIYPGIKVR) and rev (RQIHSISER), carrying an aliphatic residue at position 2 and Arg anchor residue at the C-terminus. May contribute to viral load control in chronic HIV-1 infection. {ECO:0000269\|PubMed:21498667}.
P04920	SLC4A2	S150	ochoa	Anion exchange protein 2 (AE 2) (Anion exchanger 2) (Non-erythroid band 3-like protein) (BND3L) (Solute carrier family 4 member 2)	Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity). {ECO:0000250\|UniProtKB:P13808, ECO:0000269\|PubMed:15184086, ECO:0000269\|PubMed:34668226}.
P04920	SLC4A2	S449	ochoa	Anion exchange protein 2 (AE 2) (Anion exchanger 2) (Non-erythroid band 3-like protein) (BND3L) (Solute carrier family 4 member 2)	Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity). {ECO:0000250\|UniProtKB:P13808, ECO:0000269\|PubMed:15184086, ECO:0000269\|PubMed:34668226}.
P05549	TFAP2A	S225	ochoa	Transcription factor AP-2-alpha (AP2-alpha) (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (AP-2)	Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. {ECO:0000269\|PubMed:11694877, ECO:0000269\|PubMed:12586840}.
P06748	NPM1	S88	ochoa\|psp	Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)	Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250\|UniProtKB:Q61937, ECO:0000269\|PubMed:12882984, ECO:0000269\|PubMed:16107701, ECO:0000269\|PubMed:17015463, ECO:0000269\|PubMed:18809582, ECO:0000269\|PubMed:19188445, ECO:0000269\|PubMed:20352051, ECO:0000269\|PubMed:21084279, ECO:0000269\|PubMed:22002061, ECO:0000269\|PubMed:22528486, ECO:0000269\|PubMed:25956029}.
P07332	FES	S70	ochoa	Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Feline sarcoma/Fujinami avian sarcoma oncogene homolog) (Proto-oncogene c-Fes) (Proto-oncogene c-Fps) (p93c-fes)	Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. {ECO:0000269\|PubMed:11509660, ECO:0000269\|PubMed:15302586, ECO:0000269\|PubMed:15485904, ECO:0000269\|PubMed:16455651, ECO:0000269\|PubMed:17595334, ECO:0000269\|PubMed:18046454, ECO:0000269\|PubMed:19001085, ECO:0000269\|PubMed:19051325, ECO:0000269\|PubMed:20111072, ECO:0000269\|PubMed:2656706, ECO:0000269\|PubMed:8955135}.
P07814	EPRS1	S819	ochoa	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P07814	EPRS1	S886	ochoa\|psp	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P07814	EPRS1	S891	ochoa	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P07910	HNRNPC	S121	ochoa	Heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2)	Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269\|PubMed:12509468, ECO:0000269\|PubMed:16010978, ECO:0000269\|PubMed:25719671, ECO:0000269\|PubMed:7567451, ECO:0000269\|PubMed:8264621}.
P07947	YES1	S46	ochoa	Tyrosine-protein kinase Yes (EC 2.7.10.2) (Proto-oncogene c-Yes) (p61-Yes)	Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (PubMed:26979622). {ECO:0000269\|PubMed:11901164, ECO:0000269\|PubMed:18479465, ECO:0000269\|PubMed:19276087, ECO:0000269\|PubMed:21566460, ECO:0000269\|PubMed:21713032, ECO:0000269\|PubMed:26979622}.
P07949	RET	S696	ochoa\|psp	Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]	Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (PubMed:20064382, PubMed:20616503, PubMed:20702524, PubMed:21357690, PubMed:21454698, PubMed:24560924, PubMed:28846097, PubMed:28846099, PubMed:28953886, PubMed:31118272). In contrast to most receptor tyrosine kinases, RET requires not only its cognate ligands but also coreceptors, for activation (PubMed:21994944, PubMed:23333276, PubMed:28846097, PubMed:28846099, PubMed:28953886). GDNF ligands (GDNF, NRTN, ARTN, PSPN and GDF15) first bind their corresponding GDNFR coreceptors (GFRA1, GFRA2, GFRA3, GFRA4 and GFRAL, respectively), triggering RET autophosphorylation and activation, leading to activation of downstream signaling pathways, including the MAPK- and AKT-signaling pathways (PubMed:21994944, PubMed:23333276, PubMed:24560924, PubMed:25242331, PubMed:28846097, PubMed:28846099, PubMed:28953886). Acts as a dependence receptor via the GDNF-GFRA1 signaling: in the presence of the ligand GDNF in somatotrophs within pituitary, promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF (PubMed:20616503, PubMed:21994944). Required for the molecular mechanisms orchestration during intestine organogenesis via the ARTN-GFRA3 signaling: involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which triggers an aversive response, characterized by nausea, vomiting, and/or loss of appetite in response to various stresses (PubMed:28846097, PubMed:28846099, PubMed:28953886). Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner (PubMed:20702524, PubMed:21357690). Also active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage (PubMed:21357690). Triggers the differentiation of rapidly adapting (RA) mechanoreceptors (PubMed:20064382). Involved in the development of the neural crest (By similarity). Regulates nociceptor survival and size (By similarity). Phosphorylates PTK2/FAK1 (PubMed:21454698). {ECO:0000250\|UniProtKB:P35546, ECO:0000269\|PubMed:20064382, ECO:0000269\|PubMed:20616503, ECO:0000269\|PubMed:20702524, ECO:0000269\|PubMed:21357690, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:21994944, ECO:0000269\|PubMed:23333276, ECO:0000269\|PubMed:24560924, ECO:0000269\|PubMed:25242331, ECO:0000269\|PubMed:28846097, ECO:0000269\|PubMed:28846099, ECO:0000269\|PubMed:28953886, ECO:0000269\|PubMed:31118272}.; FUNCTION: [Isoform 1]: Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. {ECO:0000269\|PubMed:28846099}.
P07949	RET	S835	ochoa	Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]	Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (PubMed:20064382, PubMed:20616503, PubMed:20702524, PubMed:21357690, PubMed:21454698, PubMed:24560924, PubMed:28846097, PubMed:28846099, PubMed:28953886, PubMed:31118272). In contrast to most receptor tyrosine kinases, RET requires not only its cognate ligands but also coreceptors, for activation (PubMed:21994944, PubMed:23333276, PubMed:28846097, PubMed:28846099, PubMed:28953886). GDNF ligands (GDNF, NRTN, ARTN, PSPN and GDF15) first bind their corresponding GDNFR coreceptors (GFRA1, GFRA2, GFRA3, GFRA4 and GFRAL, respectively), triggering RET autophosphorylation and activation, leading to activation of downstream signaling pathways, including the MAPK- and AKT-signaling pathways (PubMed:21994944, PubMed:23333276, PubMed:24560924, PubMed:25242331, PubMed:28846097, PubMed:28846099, PubMed:28953886). Acts as a dependence receptor via the GDNF-GFRA1 signaling: in the presence of the ligand GDNF in somatotrophs within pituitary, promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF (PubMed:20616503, PubMed:21994944). Required for the molecular mechanisms orchestration during intestine organogenesis via the ARTN-GFRA3 signaling: involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which triggers an aversive response, characterized by nausea, vomiting, and/or loss of appetite in response to various stresses (PubMed:28846097, PubMed:28846099, PubMed:28953886). Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner (PubMed:20702524, PubMed:21357690). Also active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage (PubMed:21357690). Triggers the differentiation of rapidly adapting (RA) mechanoreceptors (PubMed:20064382). Involved in the development of the neural crest (By similarity). Regulates nociceptor survival and size (By similarity). Phosphorylates PTK2/FAK1 (PubMed:21454698). {ECO:0000250\|UniProtKB:P35546, ECO:0000269\|PubMed:20064382, ECO:0000269\|PubMed:20616503, ECO:0000269\|PubMed:20702524, ECO:0000269\|PubMed:21357690, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:21994944, ECO:0000269\|PubMed:23333276, ECO:0000269\|PubMed:24560924, ECO:0000269\|PubMed:25242331, ECO:0000269\|PubMed:28846097, ECO:0000269\|PubMed:28846099, ECO:0000269\|PubMed:28953886, ECO:0000269\|PubMed:31118272}.; FUNCTION: [Isoform 1]: Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. {ECO:0000269\|PubMed:28846099}.
P08047	SP1	S47	ochoa	Transcription factor Sp1	Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Also binds the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21046154, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity). {ECO:0000250\|UniProtKB:O89090, ECO:0000250\|UniProtKB:Q01714, ECO:0000269\|PubMed:10391891, ECO:0000269\|PubMed:11371615, ECO:0000269\|PubMed:11904305, ECO:0000269\|PubMed:14593115, ECO:0000269\|PubMed:16377629, ECO:0000269\|PubMed:16478997, ECO:0000269\|PubMed:16943418, ECO:0000269\|PubMed:17049555, ECO:0000269\|PubMed:18171990, ECO:0000269\|PubMed:18199680, ECO:0000269\|PubMed:18239466, ECO:0000269\|PubMed:18513490, ECO:0000269\|PubMed:18619531, ECO:0000269\|PubMed:19193796, ECO:0000269\|PubMed:20091743, ECO:0000269\|PubMed:21046154, ECO:0000269\|PubMed:21798247}.
P08047	SP1	S48	ochoa	Transcription factor Sp1	Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Also binds the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21046154, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity). {ECO:0000250\|UniProtKB:O89090, ECO:0000250\|UniProtKB:Q01714, ECO:0000269\|PubMed:10391891, ECO:0000269\|PubMed:11371615, ECO:0000269\|PubMed:11904305, ECO:0000269\|PubMed:14593115, ECO:0000269\|PubMed:16377629, ECO:0000269\|PubMed:16478997, ECO:0000269\|PubMed:16943418, ECO:0000269\|PubMed:17049555, ECO:0000269\|PubMed:18171990, ECO:0000269\|PubMed:18199680, ECO:0000269\|PubMed:18239466, ECO:0000269\|PubMed:18513490, ECO:0000269\|PubMed:18619531, ECO:0000269\|PubMed:19193796, ECO:0000269\|PubMed:20091743, ECO:0000269\|PubMed:21046154, ECO:0000269\|PubMed:21798247}.
P08138	NGFR	S311	ochoa\|psp	Tumor necrosis factor receptor superfamily member 16 (Gp80-LNGFR) (Low affinity neurotrophin receptor p75NTR) (Low-affinity nerve growth factor receptor) (NGF receptor) (Low-affinity nerve growth factor receptor p75NGFR) (Low-affinity nerve growth factor receptor p75NGR) (p75 ICD) (CD antigen CD271)	Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells. Plays a role in the inactivation of RHOA (PubMed:26646181). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCmgetaN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138). Together with BFAR negatively regulates NF-kappa-B and JNK-related signaling pathways (PubMed:22566094). {ECO:0000250, ECO:0000250\|UniProtKB:Q9Z0W1, ECO:0000269\|PubMed:14966521, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24908487, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:3022937}.
P08172	CHRM2	S288	psp	Muscarinic acetylcholine receptor M2	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269\|PubMed:24256733, ECO:0000269\|PubMed:3443095}.
P08172	CHRM2	S294	psp	Muscarinic acetylcholine receptor M2	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269\|PubMed:24256733, ECO:0000269\|PubMed:3443095}.
P08183	ABCB1	S661	ochoa\|psp	ATP-dependent translocase ABCB1 (ATP-binding cassette sub-family B member 1) (Multidrug resistance protein 1) (EC 7.6.2.2) (P-glycoprotein 1) (Phospholipid transporter ABCB1) (EC 7.6.2.1) (CD antigen CD243)	Translocates drugs and phospholipids across the membrane (PubMed:2897240, PubMed:35970996, PubMed:8898203, PubMed:9038218, PubMed:35507548). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:35970996, PubMed:9038218). {ECO:0000269\|PubMed:2897240, ECO:0000269\|PubMed:35507548, ECO:0000269\|PubMed:35970996, ECO:0000269\|PubMed:8898203, ECO:0000269\|PubMed:9038218}.
P08238	HSP90AB1	S468	ochoa	Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3)	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269\|PubMed:16478993, ECO:0000269\|PubMed:18239673, ECO:0000269\|PubMed:19696785, ECO:0000269\|PubMed:20353823, ECO:0000269\|PubMed:24613385, ECO:0000269\|PubMed:32272059, ECO:0000303\|PubMed:25973397, ECO:0000303\|PubMed:26991466, ECO:0000303\|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269\|PubMed:21949862, ECO:0000305\|PubMed:22066472}.
P08651	NFIC	S279	ochoa	Nuclear factor 1 C-type (NF1-C) (Nuclear factor 1/C) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/C) (NF-I/C) (NFI-C) (TGGCA-binding protein)	Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
P08670	VIM	S72	ochoa\|psp	Vimentin	Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250\|UniProtKB:A0A8C0N8E3, ECO:0000250\|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269\|PubMed:21746880}.
P09651	HNRNPA1	S197	ochoa	Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (Helix-destabilizing protein) (Single-strand RNA-binding protein) (hnRNP core protein A1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed]	Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:20010808, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:31498791}.; FUNCTION: (Microbial infection) May play a role in HCV RNA replication. {ECO:0000269\|PubMed:17229681}.; FUNCTION: (Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis. {ECO:0000269\|PubMed:17229681}.
P0C7P1	RBMY1D	S479	ochoa	RNA-binding motif protein, Y chromosome, family 1 member D	RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.
P0CG40	SP9	S61	ochoa	Transcription factor Sp9	Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity). {ECO:0000250}.
P0DJD0	RGPD1	S1471	ochoa	RANBP2-like and GRIP domain-containing protein 1 (Ran-binding protein 2-like 6) (RanBP2-like 6) (RanBP2L6)	None
P0DJD1	RGPD2	S1479	ochoa	RANBP2-like and GRIP domain-containing protein 2 (Ran-binding protein 2-like 2) (RanBP2-like 2) (RanBP2L2)	None
P0DJD3	RBMY1A1	S479	ochoa	RNA-binding motif protein, Y chromosome, family 1 member A1 (RNA-binding motif protein 1) (RNA-binding motif protein 2) (Y chromosome RNA recognition motif 1) (hRBMY)	RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:8269511}.
P0DJD4	RBMY1C	S479	ochoa	RNA-binding motif protein, Y chromosome, family 1 member C	RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs.
P0DPH7	TUBA3C	S54	ochoa	Tubulin alpha-3C chain (EC 3.6.5.-) (Alpha-tubulin 2) (Alpha-tubulin 3C) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-3C chain]	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P0DPH8	TUBA3D	S54	ochoa	Tubulin alpha-3D chain (EC 3.6.5.-) (Alpha-tubulin 3D) [Cleaved into: Detyrosinated tubulin alpha-3D chain]	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P10244	MYBL2	S401	ochoa	Myb-related protein B (B-Myb) (Myb-like protein 2)	Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene. {ECO:0000269\|PubMed:10770937}.
P10451	SPP1	S126	psp	Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin)	Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250\|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. {ECO:0000250\|UniProtKB:P10923}.
P10451	SPP1	S129	psp	Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin)	Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250\|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. {ECO:0000250\|UniProtKB:P10923}.
P10586	PTPRF	S1305	ochoa	Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR)	Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; FUNCTION: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.
P10586	PTPRF	S1311	ochoa	Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR)	Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; FUNCTION: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.
P10588	NR2F6	S40	ochoa	Nuclear receptor subfamily 2 group F member 6 (V-erbA-related protein 2) (EAR-2)	Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC). {ECO:0000269\|PubMed:10644740, ECO:0000269\|PubMed:10713182, ECO:0000269\|PubMed:11682620, ECO:0000269\|PubMed:18701084}.
P10636	MAPT	S238	ochoa	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P10636	MAPT	S443	ochoa	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P10636	MAPT	S444	ochoa	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P10636	MAPT	S739	ochoa\|psp	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P11137	MAP2	S1808	ochoa	Microtubule-associated protein 2 (MAP-2)	The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
P11142	HSPA8	S544	ochoa	Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Heat shock protein family A member 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)	Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity). {ECO:0000250\|UniProtKB:P19120, ECO:0000269\|PubMed:10722728, ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:11559757, ECO:0000269\|PubMed:12526792, ECO:0000269\|PubMed:15894275, ECO:0000269\|PubMed:21148293, ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:23018488, ECO:0000269\|PubMed:23990462, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27916661, ECO:0000269\|PubMed:2799391, ECO:0000269\|PubMed:36586411, ECO:0000303\|PubMed:24121476, ECO:0000303\|PubMed:26865365}.
P11274	BCR	S221	ochoa	Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)	Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119). {ECO:0000250\|UniProtKB:Q6PAJ1, ECO:0000269\|PubMed:1657398, ECO:0000269\|PubMed:17116687, ECO:0000269\|PubMed:1903516, ECO:0000269\|PubMed:23940119, ECO:0000269\|PubMed:7479768}.
P11274	BCR	S468	ochoa	Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)	Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119). {ECO:0000250\|UniProtKB:Q6PAJ1, ECO:0000269\|PubMed:1657398, ECO:0000269\|PubMed:17116687, ECO:0000269\|PubMed:1903516, ECO:0000269\|PubMed:23940119, ECO:0000269\|PubMed:7479768}.
P11388	TOP2A	S1393	ochoa\|psp	DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme)	Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity). {ECO:0000250\|UniProtKB:Q01320, ECO:0000269\|PubMed:17567603, ECO:0000269\|PubMed:18790802, ECO:0000269\|PubMed:22013166, ECO:0000269\|PubMed:22323612}.
P11532	DMD	S3621	ochoa	Dystrophin	Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000250\|UniProtKB:P11531, ECO:0000269\|PubMed:16710609}.
P11532	DMD	S3623	ochoa\|psp	Dystrophin	Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000250\|UniProtKB:P11531, ECO:0000269\|PubMed:16710609}.
P12270	TPR	S528	ochoa	Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269\|PubMed:11952838, ECO:0000269\|PubMed:15654337, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18794356, ECO:0000269\|PubMed:18981471, ECO:0000269\|PubMed:19273613, ECO:0000269\|PubMed:20133940, ECO:0000269\|PubMed:20407419, ECO:0000269\|PubMed:21613532, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:9864356}.
P12270	TPR	S637	ochoa	Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269\|PubMed:11952838, ECO:0000269\|PubMed:15654337, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18794356, ECO:0000269\|PubMed:18981471, ECO:0000269\|PubMed:19273613, ECO:0000269\|PubMed:20133940, ECO:0000269\|PubMed:20407419, ECO:0000269\|PubMed:21613532, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:9864356}.
P12270	TPR	S652	ochoa	Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269\|PubMed:11952838, ECO:0000269\|PubMed:15654337, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18794356, ECO:0000269\|PubMed:18981471, ECO:0000269\|PubMed:19273613, ECO:0000269\|PubMed:20133940, ECO:0000269\|PubMed:20407419, ECO:0000269\|PubMed:21613532, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:9864356}.
P12270	TPR	S2054	ochoa	Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269\|PubMed:11952838, ECO:0000269\|PubMed:15654337, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18794356, ECO:0000269\|PubMed:18981471, ECO:0000269\|PubMed:19273613, ECO:0000269\|PubMed:20133940, ECO:0000269\|PubMed:20407419, ECO:0000269\|PubMed:21613532, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:9864356}.
P12694	BCKDHA	S343	ochoa	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha)	Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction. {ECO:0000269\|PubMed:10745006, ECO:0000269\|PubMed:7883996, ECO:0000269\|PubMed:9582350}.
P12814	ACTN1	S250	ochoa	Alpha-actinin-1 (Alpha-actinin cytoskeletal isoform) (F-actin cross-linking protein) (Non-muscle alpha-actinin-1)	F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000269\|PubMed:22689882}.
P12830	CDH1	S844	psp	Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]	Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (PubMed:29999492). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250\|UniProtKB:F1PAA9, ECO:0000269\|PubMed:11976333, ECO:0000269\|PubMed:16417575, ECO:0000269\|PubMed:29999492}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000269\|PubMed:16417575}.; FUNCTION: (Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria. {ECO:0000269\|PubMed:10406800, ECO:0000269\|PubMed:17540170, ECO:0000269\|PubMed:8601315}.
P12830	CDH1	S850	psp	Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]	Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (PubMed:29999492). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250\|UniProtKB:F1PAA9, ECO:0000269\|PubMed:11976333, ECO:0000269\|PubMed:16417575, ECO:0000269\|PubMed:29999492}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000269\|PubMed:16417575}.; FUNCTION: (Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria. {ECO:0000269\|PubMed:10406800, ECO:0000269\|PubMed:17540170, ECO:0000269\|PubMed:8601315}.
P12830	CDH1	S853	psp	Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]	Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (PubMed:29999492). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250\|UniProtKB:F1PAA9, ECO:0000269\|PubMed:11976333, ECO:0000269\|PubMed:16417575, ECO:0000269\|PubMed:29999492}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000269\|PubMed:16417575}.; FUNCTION: (Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria. {ECO:0000269\|PubMed:10406800, ECO:0000269\|PubMed:17540170, ECO:0000269\|PubMed:8601315}.
P12883	MYH7	S648	ochoa	Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta)	Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305\|PubMed:26150528, ECO:0000305\|PubMed:26246073}.
P12883	MYH7	S1469	ochoa	Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta)	Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305\|PubMed:26150528, ECO:0000305\|PubMed:26246073}.
P12931	SRC	S75	ochoa\|psp	Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)	Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors (PubMed:34234773). Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Phosphorylates PKP3 at 'Tyr-195' in response to reactive oxygen species, which may cause the release of PKP3 from desmosome cell junctions into the cytoplasm (PubMed:25501895). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14585963, PubMed:8755529). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (PubMed:35927303). Phosphorylates caspase CASP8 at 'Tyr-380' which negatively regulates CASP8 processing and activation, down-regulating CASP8 proapoptotic function (PubMed:16619028). {ECO:0000250\|UniProtKB:P05480, ECO:0000250\|UniProtKB:Q9WUD9, ECO:0000269\|PubMed:11389730, ECO:0000269\|PubMed:12615910, ECO:0000269\|PubMed:14585963, ECO:0000269\|PubMed:16186108, ECO:0000269\|PubMed:16619028, ECO:0000269\|PubMed:18586953, ECO:0000269\|PubMed:19307596, ECO:0000269\|PubMed:19419966, ECO:0000269\|PubMed:20100835, ECO:0000269\|PubMed:20525694, ECO:0000269\|PubMed:21309750, ECO:0000269\|PubMed:21411625, ECO:0000269\|PubMed:22710723, ECO:0000269\|PubMed:25501895, ECO:0000269\|PubMed:25731159, ECO:0000269\|PubMed:34234773, ECO:0000269\|PubMed:35927303, ECO:0000269\|PubMed:7853507, ECO:0000269\|PubMed:8755529, ECO:0000269\|PubMed:8759729, ECO:0000305\|PubMed:11964124, ECO:0000305\|PubMed:8672527, ECO:0000305\|PubMed:9442882}.; FUNCTION: [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000250\|UniProtKB:Q9WUD9}.; FUNCTION: [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). {ECO:0000250\|UniProtKB:Q9WUD9}.; FUNCTION: [Isoform 3]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity). {ECO:0000250\|UniProtKB:Q9WUD9}.
P13010	XRCC5	S585	ochoa	X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (86 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 2) (ATP-dependent DNA helicase II 80 kDa subunit) (CTC box-binding factor 85 kDa subunit) (CTC85) (CTCBF) (DNA repair protein XRCC5) (Ku80) (Ku86) (Lupus Ku autoantigen protein p86) (Nuclear factor IV) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining))	Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). Required for double-strand break repair and V(D)J recombination (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). Also has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). It works in the 3'-5' direction (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). Binding to DNA may be mediated by XRCC6 (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (PubMed:11493912, PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). The XRCC5-XRRC6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks (PubMed:20383123). XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:12145306). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). {ECO:0000269\|PubMed:11493912, ECO:0000269\|PubMed:12145306, ECO:0000269\|PubMed:20383123, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32103174, ECO:0000269\|PubMed:7957065, ECO:0000269\|PubMed:8621488}.
P13533	MYH6	S650	ochoa	Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha)	Muscle contraction.
P13533	MYH6	S1471	ochoa	Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha)	Muscle contraction.
P13796	LCP1	S117	ochoa	Plastin-2 (L-plastin) (LC64P) (Lymphocyte cytosolic protein 1) (LCP-1)	Actin-binding protein (PubMed:16636079, PubMed:17294403, PubMed:28493397). Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). Modulates the cell surface expression of IL2RA/CD25 and CD69 (PubMed:17294403). {ECO:0000269\|PubMed:16636079, ECO:0000269\|PubMed:17294403, ECO:0000269\|PubMed:28493397}.
P13804	ETFA	S185	ochoa	Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF)	Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:10356313, PubMed:15159392, PubMed:15975918, PubMed:27499296, PubMed:9334218). It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:9334218). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism (PubMed:12815589, PubMed:1430199, PubMed:1882842). {ECO:0000269\|PubMed:10356313, ECO:0000269\|PubMed:12815589, ECO:0000269\|PubMed:1430199, ECO:0000269\|PubMed:15159392, ECO:0000269\|PubMed:15975918, ECO:0000269\|PubMed:27499296, ECO:0000269\|PubMed:9334218, ECO:0000303\|PubMed:17941859, ECO:0000305\|PubMed:1882842}.
P14598	NCF1	S310	psp	Neutrophil cytosol factor 1 (NCF-1) (47 kDa autosomal chronic granulomatous disease protein) (47 kDa neutrophil oxidase factor) (NCF-47K) (Neutrophil NADPH oxidase factor 1) (Nox organizer 2) (Nox-organizing protein 2) (SH3 and PX domain-containing protein 1A) (p47-phox)	Subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:2547247, PubMed:2550933, PubMed:38355798). In the activated complex, electrons are first transferred from NADPH to flavin adenine dinucleotide (FAD) and subsequently transferred via two heme molecules to molecular oxygen, producing superoxide through an outer-sphere reaction (PubMed:38355798). Activation of the NADPH oxidase complex is initiated by the assembly of cytosolic subunits of the NADPH oxidase complex with the core NADPH oxidase complex to form a complex at the plasma membrane or phagosomal membrane (PubMed:38355798). This activation process is initiated by phosphorylation dependent binding of the cytosolic NCF1/p47-phox subunit to the C-terminus of CYBA/p22-phox (PubMed:12732142, PubMed:19801500). {ECO:0000269\|PubMed:12732142, ECO:0000269\|PubMed:19801500, ECO:0000269\|PubMed:2547247, ECO:0000269\|PubMed:2550933, ECO:0000269\|PubMed:38355798}.
P14859	POU2F1	S364	ochoa	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P14859	POU2F1	S370	ochoa	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P14859	POU2F1	S448	ochoa	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P14921	ETS1	S257	ochoa\|psp	Protein C-ets-1 (p54)	Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269\|PubMed:10698492, ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000303\|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269\|PubMed:19377509}.
P14921	ETS1	S273	ochoa\|psp	Protein C-ets-1 (p54)	Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269\|PubMed:10698492, ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000303\|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269\|PubMed:19377509}.
P14921	ETS1	S276	psp	Protein C-ets-1 (p54)	Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269\|PubMed:10698492, ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000303\|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269\|PubMed:19377509}.
P14923	JUP	S671	ochoa	Junction plakoglobin (Catenin gamma) (Desmoplakin III) (Desmoplakin-3)	Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). {ECO:0000250}.
P15056	BRAF	S405	ochoa	Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (p94) (v-Raf murine sarcoma viral oncogene homolog B1)	Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway (PubMed:21441910, PubMed:29433126). Phosphorylates PFKFB2 (PubMed:36402789). May play a role in the postsynaptic responses of hippocampal neurons (PubMed:1508179). {ECO:0000269\|PubMed:1508179, ECO:0000269\|PubMed:21441910, ECO:0000269\|PubMed:29433126, ECO:0000269\|PubMed:36402789, ECO:0000305}.
P15822	HIVEP1	S577	ochoa	Zinc finger protein 40 (Cirhin interaction protein) (CIRIP) (Gate keeper of apoptosis-activating protein) (GAAP) (Human immunodeficiency virus type I enhancer-binding protein 1) (HIV-EP1) (Major histocompatibility complex-binding protein 1) (MBP-1) (Positive regulatory domain II-binding factor 1) (PRDII-BF1)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.
P15822	HIVEP1	S687	ochoa	Zinc finger protein 40 (Cirhin interaction protein) (CIRIP) (Gate keeper of apoptosis-activating protein) (GAAP) (Human immunodeficiency virus type I enhancer-binding protein 1) (HIV-EP1) (Major histocompatibility complex-binding protein 1) (MBP-1) (Positive regulatory domain II-binding factor 1) (PRDII-BF1)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.
P15822	HIVEP1	S1319	ochoa	Zinc finger protein 40 (Cirhin interaction protein) (CIRIP) (Gate keeper of apoptosis-activating protein) (GAAP) (Human immunodeficiency virus type I enhancer-binding protein 1) (HIV-EP1) (Major histocompatibility complex-binding protein 1) (MBP-1) (Positive regulatory domain II-binding factor 1) (PRDII-BF1)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.
P15884	TCF4	S318	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15884	TCF4	S511	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15923	TCF3	S352	ochoa\|psp	Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)	Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (By similarity). Together with TCF15, required for the mesenchymal to epithelial transition (By similarity). Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (By similarity). Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (PubMed:2493990). Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (By similarity). {ECO:0000250\|UniProtKB:P15806, ECO:0000269\|PubMed:2493990}.; FUNCTION: [Isoform E47]: Facilitates ATOH7 binding to DNA at the consensus sequence 5'-CAGGTG-3', and positively regulates transcriptional activity. {ECO:0000269\|PubMed:31696227}.
P15924	DSP	S38	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2589	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2616	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2815	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2831	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15941	MUC1	S1233	ochoa	Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]	The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.; FUNCTION: The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.
P16144	ITGB4	S1517	ochoa	Integrin beta-4 (GP150) (CD antigen CD104)	Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:19403692, ECO:0000269\|PubMed:20682778, ECO:0000269\|PubMed:22351760, ECO:0000269\|PubMed:28873464}.
P16144	ITGB4	S1521	ochoa	Integrin beta-4 (GP150) (CD antigen CD104)	Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:19403692, ECO:0000269\|PubMed:20682778, ECO:0000269\|PubMed:22351760, ECO:0000269\|PubMed:28873464}.
P16220	CREB1	S103	psp	Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)	Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation (PubMed:14536081). Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells (By similarity). Regulates the expression of apoptotic and inflammatory response factors in cardiomyocytes in response to ERFE-mediated activation of AKT signaling (By similarity). {ECO:0000250\|UniProtKB:P27925, ECO:0000250\|UniProtKB:Q01147, ECO:0000269\|PubMed:14536081}.
P16234	PDGFRA	S1048	ochoa	Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)	Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269\|PubMed:10734113, ECO:0000269\|PubMed:10947961, ECO:0000269\|PubMed:11297552, ECO:0000269\|PubMed:12522257, ECO:0000269\|PubMed:1646396, ECO:0000269\|PubMed:17087943, ECO:0000269\|PubMed:1709159, ECO:0000269\|PubMed:17141222, ECO:0000269\|PubMed:20972453, ECO:0000269\|PubMed:21224473, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:2554309, ECO:0000269\|PubMed:8188664, ECO:0000269\|PubMed:8760137, ECO:0000269\|PubMed:8943348}.
P16284	PECAM1	S653	ochoa	Platelet endothelial cell adhesion molecule (PECAM-1) (EndoCAM) (GPIIA') (PECA1) (CD antigen CD31)	Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:17580308, PubMed:19342684). Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis (By similarity). {ECO:0000250\|UniProtKB:Q08481, ECO:0000269\|PubMed:12110892, ECO:0000269\|PubMed:17580308, ECO:0000269\|PubMed:18672896, ECO:0000269\|PubMed:19342684, ECO:0000269\|PubMed:27958302}.; FUNCTION: [Isoform Delta15]: Does not protect against apoptosis. {ECO:0000269\|PubMed:18388311}.
P16333	NCK1	S91	ochoa	SH2/SH3 adapter protein NCK1 (Cytoplasmic protein NCK1) (NCK adapter protein 1) (Nck-1) (SH2/SH3 adapter protein NCK-alpha)	Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors. {ECO:0000269\|PubMed:10026169, ECO:0000269\|PubMed:16835242, ECO:0000269\|PubMed:17803907, ECO:0000269\|PubMed:18835251, ECO:0000269\|PubMed:23358419, ECO:0000269\|PubMed:9430661}.
P16383	GCFC2	S122	ochoa	Intron Large complex component GCFC2 (GC-rich sequence DNA-binding factor) (GC-rich sequence DNA-binding factor 2) (Transcription factor 9) (TCF-9)	Involved in pre-mRNA splicing through regulating spliceosome C complex formation (PubMed:24304693). May play a role during late-stage splicing events and turnover of excised introns (PubMed:24304693). {ECO:0000269\|PubMed:24304693}.
P16989	YBX3	S324	ochoa	Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB)	Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}.
P17661	DES	S48	ochoa	Desmin	Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (PubMed:25358400). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity). {ECO:0000250\|UniProtKB:P31001, ECO:0000269\|PubMed:24200904, ECO:0000269\|PubMed:25394388, ECO:0000269\|PubMed:26724190, ECO:0000303\|PubMed:25358400}.
P17676	CEBPB	S229	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P17676	CEBPB	S231	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P17812	CTPS1	S568	ochoa	CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1)	This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000269\|PubMed:16179339, ECO:0000269\|PubMed:24870241}.
P17936	IGFBP3	S151	ochoa	Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3)	Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including proliferation, differentiation, and apoptosis in a cell-type specific manner (PubMed:10874028, PubMed:19556345). Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R (PubMed:20353938). Inhibits the positive effect of humanin on insulin sensitivity (PubMed:19623253). Promotes testicular germ cell apoptosis (PubMed:19952275). Acts via LRP-1/alpha2M receptor, also known as TGF-beta type V receptor, to mediate cell growth inhibition independent of IGF1 (PubMed:9252371). Mechanistically, induces serine-specific dephosphorylation of IRS1 or IRS2 upon ligation to its receptor, leading to the inhibitory cascade (PubMed:15371331). In the nucleus, interacts with transcription factors such as retinoid X receptor-alpha/RXRA to regulate transcriptional signaling and apoptosis (PubMed:10874028). {ECO:0000269\|PubMed:10874028, ECO:0000269\|PubMed:15371331, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19556345, ECO:0000269\|PubMed:19623253, ECO:0000269\|PubMed:19952275, ECO:0000269\|PubMed:20353938}.
P18583	SON	S160	ochoa	Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3)	RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269\|PubMed:20581448, ECO:0000269\|PubMed:21504830, ECO:0000269\|PubMed:27545680}.
P18583	SON	S1780	ochoa	Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3)	RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269\|PubMed:20581448, ECO:0000269\|PubMed:21504830, ECO:0000269\|PubMed:27545680}.
P18846	ATF1	S47	psp	Cyclic AMP-dependent transcription factor ATF-1 (cAMP-dependent transcription factor ATF-1) (Activating transcription factor 1) (Protein TREB36)	This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269\|PubMed:18794154, ECO:0000269\|PubMed:20980392}.
P18846	ATF1	S50	psp	Cyclic AMP-dependent transcription factor ATF-1 (cAMP-dependent transcription factor ATF-1) (Activating transcription factor 1) (Protein TREB36)	This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269\|PubMed:18794154, ECO:0000269\|PubMed:20980392}.
P18850	ATF6	S104	ochoa\|psp	Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha]	[Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464). {ECO:0000269\|PubMed:10564271, ECO:0000269\|PubMed:11158310, ECO:0000269\|PubMed:11779464}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR (PubMed:10564271, PubMed:11158310, PubMed:11163209, PubMed:11779464). Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3') (PubMed:10564271, PubMed:11158310, PubMed:11779464). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor (PubMed:10564271, PubMed:11158310, PubMed:11779464). May play a role in foveal development and cone function in the retina (PubMed:26029869). {ECO:0000269\|PubMed:10564271, ECO:0000269\|PubMed:11158310, ECO:0000269\|PubMed:11163209, ECO:0000269\|PubMed:11779464, ECO:0000269\|PubMed:26029869}.
P18887	XRCC1	S210	ochoa\|psp	DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1)	Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (PubMed:11163244, PubMed:28002403). Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity (PubMed:28002403, PubMed:34102106, PubMed:34811483). Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483). {ECO:0000269\|PubMed:11163244, ECO:0000269\|PubMed:14500814, ECO:0000269\|PubMed:28002403, ECO:0000269\|PubMed:34102106, ECO:0000269\|PubMed:34811483}.
P18887	XRCC1	S229	ochoa	DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1)	Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (PubMed:11163244, PubMed:28002403). Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity (PubMed:28002403, PubMed:34102106, PubMed:34811483). Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483). {ECO:0000269\|PubMed:11163244, ECO:0000269\|PubMed:14500814, ECO:0000269\|PubMed:28002403, ECO:0000269\|PubMed:34102106, ECO:0000269\|PubMed:34811483}.
P18887	XRCC1	S416	ochoa	DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1)	Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (PubMed:11163244, PubMed:28002403). Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity (PubMed:28002403, PubMed:34102106, PubMed:34811483). Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483). {ECO:0000269\|PubMed:11163244, ECO:0000269\|PubMed:14500814, ECO:0000269\|PubMed:28002403, ECO:0000269\|PubMed:34102106, ECO:0000269\|PubMed:34811483}.
P19174	PLCG1	S1227	ochoa	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) (PLC-148) (Phosphoinositide phospholipase C-gamma-1) (Phospholipase C-II) (PLC-II) (Phospholipase C-gamma-1) (PLC-gamma-1)	Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Plays a role in actin reorganization and cell migration (PubMed:17229814). Guanine nucleotide exchange factor that binds the GTPase DNM1 and catalyzes the dissociation of GDP, allowing a GTP molecule to bind in its place, therefore enhancing DNM1-dependent endocytosis (By similarity). {ECO:0000250\|UniProtKB:P10686, ECO:0000269\|PubMed:17229814, ECO:0000269\|PubMed:37422272}.
P19174	PLCG1	S1233	ochoa	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) (PLC-148) (Phosphoinositide phospholipase C-gamma-1) (Phospholipase C-II) (PLC-II) (Phospholipase C-gamma-1) (PLC-gamma-1)	Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Plays a role in actin reorganization and cell migration (PubMed:17229814). Guanine nucleotide exchange factor that binds the GTPase DNM1 and catalyzes the dissociation of GDP, allowing a GTP molecule to bind in its place, therefore enhancing DNM1-dependent endocytosis (By similarity). {ECO:0000250\|UniProtKB:P10686, ECO:0000269\|PubMed:17229814, ECO:0000269\|PubMed:37422272}.
P19634	SLC9A1	S605	ochoa	Sodium/hydrogen exchanger 1 (APNH) (Na(+)/H(+) antiporter, amiloride-sensitive) (Na(+)/H(+) exchanger 1) (NHE-1) (Solute carrier family 9 member 1)	Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (PubMed:11350981, PubMed:11532004, PubMed:14680478, PubMed:15035633, PubMed:15677483, PubMed:17073455, PubMed:17493937, PubMed:22020933, PubMed:27650500, PubMed:32130622, PubMed:7110335, PubMed:7603840). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival (PubMed:12947095, PubMed:15096511, PubMed:22020933, PubMed:8901634). In addition, can transport lithium Li(+) and also functions as a Na(+)/Li(+) antiporter (PubMed:7603840). SLC9A1 also functions in membrane anchoring and organization of scaffolding complexes that coordinate signaling inputs (PubMed:15096511). {ECO:0000250\|UniProtKB:P26431, ECO:0000269\|PubMed:11350981, ECO:0000269\|PubMed:11532004, ECO:0000269\|PubMed:12947095, ECO:0000269\|PubMed:14680478, ECO:0000269\|PubMed:15035633, ECO:0000269\|PubMed:15096511, ECO:0000269\|PubMed:15677483, ECO:0000269\|PubMed:17073455, ECO:0000269\|PubMed:17493937, ECO:0000269\|PubMed:22020933, ECO:0000269\|PubMed:27650500, ECO:0000269\|PubMed:32130622, ECO:0000269\|PubMed:7110335, ECO:0000269\|PubMed:7603840, ECO:0000269\|PubMed:8901634}.
P19634	SLC9A1	S729	ochoa\|psp	Sodium/hydrogen exchanger 1 (APNH) (Na(+)/H(+) antiporter, amiloride-sensitive) (Na(+)/H(+) exchanger 1) (NHE-1) (Solute carrier family 9 member 1)	Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (PubMed:11350981, PubMed:11532004, PubMed:14680478, PubMed:15035633, PubMed:15677483, PubMed:17073455, PubMed:17493937, PubMed:22020933, PubMed:27650500, PubMed:32130622, PubMed:7110335, PubMed:7603840). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival (PubMed:12947095, PubMed:15096511, PubMed:22020933, PubMed:8901634). In addition, can transport lithium Li(+) and also functions as a Na(+)/Li(+) antiporter (PubMed:7603840). SLC9A1 also functions in membrane anchoring and organization of scaffolding complexes that coordinate signaling inputs (PubMed:15096511). {ECO:0000250\|UniProtKB:P26431, ECO:0000269\|PubMed:11350981, ECO:0000269\|PubMed:11532004, ECO:0000269\|PubMed:12947095, ECO:0000269\|PubMed:14680478, ECO:0000269\|PubMed:15035633, ECO:0000269\|PubMed:15096511, ECO:0000269\|PubMed:15677483, ECO:0000269\|PubMed:17073455, ECO:0000269\|PubMed:17493937, ECO:0000269\|PubMed:22020933, ECO:0000269\|PubMed:27650500, ECO:0000269\|PubMed:32130622, ECO:0000269\|PubMed:7110335, ECO:0000269\|PubMed:7603840, ECO:0000269\|PubMed:8901634}.
P19793	RXRA	S27	psp	Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)	Receptor for retinoic acid that acts as a transcription factor (PubMed:10874028, PubMed:11162439, PubMed:11915042, PubMed:37478846). Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:16107141, PubMed:17761950, PubMed:18800767, PubMed:19167885, PubMed:28167758, PubMed:37478846). The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:17761950, PubMed:28167758). The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (PubMed:1310260). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (PubMed:20215566). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (PubMed:20215566, PubMed:37478846, PubMed:9267036). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (PubMed:10195690, PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (PubMed:29021580). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (PubMed:10195690). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). Acts as an enhancer of RARA binding to RARE DNA element (PubMed:28167758). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (PubMed:12145331, PubMed:15509776). Promotes myelin debris phagocytosis and remyelination by macrophages (PubMed:26463675). Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes (PubMed:25417649). Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (PubMed:30216632). {ECO:0000269\|PubMed:10195690, ECO:0000269\|PubMed:10874028, ECO:0000269\|PubMed:11162439, ECO:0000269\|PubMed:11915042, ECO:0000269\|PubMed:12145331, ECO:0000269\|PubMed:1310260, ECO:0000269\|PubMed:15509776, ECO:0000269\|PubMed:16107141, ECO:0000269\|PubMed:17761950, ECO:0000269\|PubMed:18800767, ECO:0000269\|PubMed:19167885, ECO:0000269\|PubMed:20215566, ECO:0000269\|PubMed:25417649, ECO:0000269\|PubMed:26463675, ECO:0000269\|PubMed:28167758, ECO:0000269\|PubMed:29021580, ECO:0000269\|PubMed:30216632, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:9267036}.
P19838	NFKB1	S899	ochoa	Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. {ECO:0000269\|PubMed:15485931, ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:2203531, ECO:0000269\|PubMed:2234062, ECO:0000269\|PubMed:7830764}.; FUNCTION: [Nuclear factor NF-kappa-B p105 subunit]: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B (PubMed:1423592). Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105 (PubMed:1423592). {ECO:0000269\|PubMed:1423592}.; FUNCTION: [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor (PubMed:1740106, PubMed:7830764). Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions (PubMed:1740106, PubMed:7830764). {ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:7830764}.
P20700	LMNB1	S308	ochoa	Lamin-B1	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28716252, PubMed:32910914). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:28716252, PubMed:32910914). {ECO:0000269\|PubMed:28716252, ECO:0000269\|PubMed:32910914}.
P20700	LMNB1	S401	ochoa	Lamin-B1	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28716252, PubMed:32910914). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:28716252, PubMed:32910914). {ECO:0000269\|PubMed:28716252, ECO:0000269\|PubMed:32910914}.
P20810	CAST	S243	ochoa	Calpastatin (Calpain inhibitor) (Sperm BS-17 component)	Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
P21333	FLNA	S972	ochoa	Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BTM8, ECO:0000269\|PubMed:22121117, ECO:0000269\|PubMed:25358863}.
P21333	FLNA	S2048	ochoa	Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BTM8, ECO:0000269\|PubMed:22121117, ECO:0000269\|PubMed:25358863}.
P21333	FLNA	S2158	ochoa	Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BTM8, ECO:0000269\|PubMed:22121117, ECO:0000269\|PubMed:25358863}.
P21333	FLNA	S2537	ochoa	Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BTM8, ECO:0000269\|PubMed:22121117, ECO:0000269\|PubMed:25358863}.
P21359	NF1	S882	ochoa	Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]	Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269\|PubMed:2121371, ECO:0000269\|PubMed:8417346}.
P21359	NF1	S2521	ochoa	Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]	Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269\|PubMed:2121371, ECO:0000269\|PubMed:8417346}.
P21453	S1PR1	S359	ochoa\|psp	Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Endothelial differentiation G-protein coupled receptor 1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1) (CD antigen CD363)	G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. {ECO:0000250, ECO:0000269\|PubMed:10982820, ECO:0000269\|PubMed:11230698, ECO:0000269\|PubMed:11583630, ECO:0000269\|PubMed:11604399, ECO:0000269\|PubMed:19286607, ECO:0000269\|PubMed:22344443, ECO:0000269\|PubMed:8626678, ECO:0000269\|PubMed:9488656}.
P21580	TNFAIP3	S459	ochoa	Tumor necrosis factor alpha-induced protein 3 (TNF alpha-induced protein 3) (EC 2.3.2.-) (EC 3.4.19.12) (OTU domain-containing protein 7C) (Putative DNA-binding protein A20) (Zinc finger protein A20) [Cleaved into: A20p50; A20p37]	Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of pro-inflammatory cytokines and IFN beta in LPS-tolerized macrophages. {ECO:0000269\|PubMed:14748687, ECO:0000269\|PubMed:15258597, ECO:0000269\|PubMed:16684768, ECO:0000269\|PubMed:17961127, ECO:0000269\|PubMed:18164316, ECO:0000269\|PubMed:18952128, ECO:0000269\|PubMed:19494296, ECO:0000269\|PubMed:22099304, ECO:0000269\|PubMed:23827681, ECO:0000269\|PubMed:8692885, ECO:0000269\|PubMed:9299557, ECO:0000269\|PubMed:9882303}.
P22059	OSBP	S244	ochoa	Oxysterol-binding protein 1	Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269\|PubMed:15746430, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18450749, ECO:0000269\|PubMed:24209621}.
P22059	OSBP	S385	ochoa	Oxysterol-binding protein 1	Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269\|PubMed:15746430, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18450749, ECO:0000269\|PubMed:24209621}.
P22314	UBA1	S816	ochoa	Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Protein A1S9) (Ubiquitin-activating enzyme E1)	Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1447181, PubMed:1606621, PubMed:33108101). Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:1447181). Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (PubMed:22456334). {ECO:0000269\|PubMed:1447181, ECO:0000269\|PubMed:1606621, ECO:0000269\|PubMed:22456334, ECO:0000269\|PubMed:33108101}.
P22670	RFX1	S123	ochoa	MHC class II regulatory factor RFX1 (Enhancer factor C) (EF-C) (Regulatory factor X 1) (RFX) (Transcription factor RFX1)	Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes. Also binds to an inverted repeat (ENH1) required for hepatitis B virus genes expression and to the most upstream element (alpha) of the RPL30 promoter.
P22670	RFX1	S126	ochoa	MHC class II regulatory factor RFX1 (Enhancer factor C) (EF-C) (Regulatory factor X 1) (RFX) (Transcription factor RFX1)	Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes. Also binds to an inverted repeat (ENH1) required for hepatitis B virus genes expression and to the most upstream element (alpha) of the RPL30 promoter.
P22681	CBL	S652	ochoa	E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)	E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250\|UniProtKB:P22682, ECO:0000269\|PubMed:10514377, ECO:0000269\|PubMed:11896602, ECO:0000269\|PubMed:14661060, ECO:0000269\|PubMed:14739300, ECO:0000269\|PubMed:15190072, ECO:0000269\|PubMed:17094949, ECO:0000269\|PubMed:17509076, ECO:0000269\|PubMed:17974561, ECO:0000269\|PubMed:18374639, ECO:0000269\|PubMed:19689429, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:28381567}.
P22681	CBL	S675	ochoa	E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)	E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250\|UniProtKB:P22682, ECO:0000269\|PubMed:10514377, ECO:0000269\|PubMed:11896602, ECO:0000269\|PubMed:14661060, ECO:0000269\|PubMed:14739300, ECO:0000269\|PubMed:15190072, ECO:0000269\|PubMed:17094949, ECO:0000269\|PubMed:17509076, ECO:0000269\|PubMed:17974561, ECO:0000269\|PubMed:18374639, ECO:0000269\|PubMed:19689429, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:28381567}.
P22681	CBL	S797	ochoa	E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)	E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250\|UniProtKB:P22682, ECO:0000269\|PubMed:10514377, ECO:0000269\|PubMed:11896602, ECO:0000269\|PubMed:14661060, ECO:0000269\|PubMed:14739300, ECO:0000269\|PubMed:15190072, ECO:0000269\|PubMed:17094949, ECO:0000269\|PubMed:17509076, ECO:0000269\|PubMed:17974561, ECO:0000269\|PubMed:18374639, ECO:0000269\|PubMed:19689429, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:28381567}.
P22681	CBL	S804	ochoa	E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)	E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250\|UniProtKB:P22682, ECO:0000269\|PubMed:10514377, ECO:0000269\|PubMed:11896602, ECO:0000269\|PubMed:14661060, ECO:0000269\|PubMed:14739300, ECO:0000269\|PubMed:15190072, ECO:0000269\|PubMed:17094949, ECO:0000269\|PubMed:17509076, ECO:0000269\|PubMed:17974561, ECO:0000269\|PubMed:18374639, ECO:0000269\|PubMed:19689429, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:28381567}.
P22760	AADAC	S129	ochoa	Arylacetamide deacetylase (EC 3.1.1.3)	Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. {ECO:0000269\|PubMed:17936933, ECO:0000269\|PubMed:19339378, ECO:0000269\|PubMed:22207054, ECO:0000269\|PubMed:22415931, ECO:0000269\|PubMed:23542347}.
P23497	SP100	S459	ochoa	Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa)	Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation. {ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:14647468, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000269\|PubMed:15767676, ECO:0000269\|PubMed:16177824, ECO:0000269\|PubMed:17245429, ECO:0000269\|PubMed:21274506, ECO:0000269\|PubMed:21880768}.
P23511	NFYA	S326	ochoa\|psp	Nuclear transcription factor Y subunit alpha (CAAT box DNA-binding protein subunit A) (Nuclear transcription factor Y subunit A) (NF-YA)	Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component BMAL1. {ECO:0000269\|PubMed:12741956}.
P23588	EIF4B	S317	ochoa	Eukaryotic translation initiation factor 4B (eIF-4B)	Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
P23677	ITPKA	S127	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P23677	ITPKA	S130	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P23677	ITPKA	S132	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P23677	ITPKA	S137	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P25054	APC	S1346	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S1510	psp	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S2146	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S2627	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S2772	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25116	F2R	S406	psp	Proteinase-activated receptor 1 (PAR-1) (Coagulation factor II receptor) (Thrombin receptor)	High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores (PubMed:1672265, PubMed:8136362). The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores (By similarity). In astrocytes, the calcium released into the cytosol allows the Ca(2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). May play a role in platelets activation and in vascular development (PubMed:10079109). Mediates up-regulation of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, triggered by coagulation factor Xa (F10) in cardiac fibroblasts and umbilical vein endothelial cells (PubMed:30568593, PubMed:34831181). {ECO:0000250\|UniProtKB:P26824, ECO:0000250\|UniProtKB:P30558, ECO:0000269\|PubMed:10079109, ECO:0000269\|PubMed:1672265, ECO:0000269\|PubMed:30568593, ECO:0000269\|PubMed:34831181, ECO:0000269\|PubMed:8136362}.
P26651	ZFP36	S66	psp	mRNA decay activator protein ZFP36 (G0/G1 switch regulatory protein 24) (Growth factor-inducible nuclear protein NUP475) (Tristetraprolin) (Zinc finger protein 36) (Zfp-36)	Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:10330172, PubMed:10751406, PubMed:11279239, PubMed:12115244, PubMed:12748283, PubMed:15187101, PubMed:15634918, PubMed:16702957, PubMed:17030620, PubMed:20221403, PubMed:20702587, PubMed:21775632, PubMed:23644599, PubMed:25815583, PubMed:27193233, PubMed:31439631, PubMed:9703499). Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:15687258, PubMed:23644599). Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation (PubMed:23644599). Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs (PubMed:11719186, PubMed:12748283, PubMed:15687258, PubMed:16364915). Self regulates by destabilizing its own mRNA (PubMed:15187101). Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA (PubMed:10330172, PubMed:10751406, PubMed:12115244, PubMed:15187101, PubMed:15634918, PubMed:16702957, PubMed:17030620, PubMed:19188452, PubMed:20221403, PubMed:20702587, PubMed:21775632, PubMed:25815583). Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages (By similarity). Also plays a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response (PubMed:18367721). Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia (PubMed:21775632). Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (By similarity). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (PubMed:20702587). Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA (By similarity). Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs (PubMed:18367721). Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs (PubMed:15766526). May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro (PubMed:16364915). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (PubMed:17369404). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing (By similarity). Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages (By similarity). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (By similarity). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis (PubMed:27182009). Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (PubMed:26926077). {ECO:0000250\|UniProtKB:P22893, ECO:0000269\|PubMed:10330172, ECO:0000269\|PubMed:10751406, ECO:0000269\|PubMed:11279239, ECO:0000269\|PubMed:11719186, ECO:0000269\|PubMed:12115244, ECO:0000269\|PubMed:12748283, ECO:0000269\|PubMed:15187101, ECO:0000269\|PubMed:15634918, ECO:0000269\|PubMed:15687258, ECO:0000269\|PubMed:15766526, ECO:0000269\|PubMed:16364915, ECO:0000269\|PubMed:16702957, ECO:0000269\|PubMed:17030620, ECO:0000269\|PubMed:17369404, ECO:0000269\|PubMed:18367721, ECO:0000269\|PubMed:19188452, ECO:0000269\|PubMed:20221403, ECO:0000269\|PubMed:20702587, ECO:0000269\|PubMed:21775632, ECO:0000269\|PubMed:23644599, ECO:0000269\|PubMed:25815583, ECO:0000269\|PubMed:26926077, ECO:0000269\|PubMed:27182009, ECO:0000269\|PubMed:27193233, ECO:0000269\|PubMed:31439631, ECO:0000269\|PubMed:9703499}.; FUNCTION: (Microbial infection) Negatively regulates HTLV-1 TAX-dependent transactivation of viral long terminal repeat (LTR) promoter. {ECO:0000269\|PubMed:14679154}.
P27448	MARK3	S383	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P27448	MARK3	S546	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P27694	RPA1	S396	ochoa	Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (Single-stranded DNA-binding protein) [Cleaved into: Replication protein A 70 kDa DNA-binding subunit, N-terminally processed]	As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (PubMed:17596542, PubMed:27723717, PubMed:27723720). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Also plays a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. Plays a role in telomere maintenance (PubMed:17959650, PubMed:34767620). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). RPA stimulates 5'-3' helicase activity of the BRIP1/FANCJ (PubMed:17596542). {ECO:0000269\|PubMed:12791985, ECO:0000269\|PubMed:17596542, ECO:0000269\|PubMed:17765923, ECO:0000269\|PubMed:17959650, ECO:0000269\|PubMed:19116208, ECO:0000269\|PubMed:19996105, ECO:0000269\|PubMed:24332808, ECO:0000269\|PubMed:27723717, ECO:0000269\|PubMed:27723720, ECO:0000269\|PubMed:34767620, ECO:0000269\|PubMed:7697716, ECO:0000269\|PubMed:7700386, ECO:0000269\|PubMed:9430682, ECO:0000269\|PubMed:9765279}.
P27816	MAP4	S163	ochoa	Microtubule-associated protein 4 (MAP-4)	Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269\|PubMed:10791892, ECO:0000269\|PubMed:34782749}.
P27816	MAP4	S793	ochoa	Microtubule-associated protein 4 (MAP-4)	Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269\|PubMed:10791892, ECO:0000269\|PubMed:34782749}.
P27987	ITPKB	S90	ochoa	Inositol-trisphosphate 3-kinase B (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase B) (IP3 3-kinase B) (IP3K B) (InsP 3-kinase B)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:11846419, ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:1654894}.
P27987	ITPKB	S92	ochoa	Inositol-trisphosphate 3-kinase B (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase B) (IP3 3-kinase B) (IP3K B) (InsP 3-kinase B)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:11846419, ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:1654894}.
P28066	PSMA5	S62	ochoa	Proteasome subunit alpha type-5 (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome subunit alpha-5) (alpha-5) (Proteasome zeta chain)	Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269\|PubMed:15244466, ECO:0000269\|PubMed:27176742, ECO:0000269\|PubMed:8610016}.
P28290	ITPRID2	S117	ochoa	Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2)	None
P28290	ITPRID2	S752	ochoa	Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2)	None
P28290	ITPRID2	S759	ochoa	Protein ITPRID2 (Cleavage signal-1 protein) (CS-1) (ITPR-interacting domain-containing protein 2) (Ki-ras-induced actin-interacting protein) (Sperm-specific antigen 2)	None
P28715	ERCC5	S318	ochoa	DNA excision repair protein ERCC-5 (EC 3.1.-.-) (DNA repair protein complementing XP-G cells) (XPG) (Xeroderma pigmentosum group G-complementing protein)	Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed:32522879, PubMed:32821917, PubMed:7651464, PubMed:8078765, PubMed:8090225, PubMed:8206890). Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed:32522879, PubMed:32821917, PubMed:8078765, PubMed:8090225). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed:32522879). Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed:9927729). Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed:16246722). Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed:16246722). Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722). Required for DNA replication fork maintenance and preservation of genomic stability (PubMed:26833090, PubMed:32522879). Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed:26833090). In TFIIH stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed:32522879). Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed:26833090). {ECO:0000269\|PubMed:16246722, ECO:0000269\|PubMed:26833090, ECO:0000269\|PubMed:31253769, ECO:0000269\|PubMed:32522879, ECO:0000269\|PubMed:32821917, ECO:0000269\|PubMed:7651464, ECO:0000269\|PubMed:8078765, ECO:0000269\|PubMed:8090225, ECO:0000269\|PubMed:8206890, ECO:0000269\|PubMed:9927729}.
P28715	ERCC5	S532	ochoa	DNA excision repair protein ERCC-5 (EC 3.1.-.-) (DNA repair protein complementing XP-G cells) (XPG) (Xeroderma pigmentosum group G-complementing protein)	Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed:32522879, PubMed:32821917, PubMed:7651464, PubMed:8078765, PubMed:8090225, PubMed:8206890). Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed:32522879, PubMed:32821917, PubMed:8078765, PubMed:8090225). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed:32522879). Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed:9927729). Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed:16246722). Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed:16246722). Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed:16246722). Required for DNA replication fork maintenance and preservation of genomic stability (PubMed:26833090, PubMed:32522879). Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed:26833090). In TFIIH stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed:32522879). Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed:26833090). {ECO:0000269\|PubMed:16246722, ECO:0000269\|PubMed:26833090, ECO:0000269\|PubMed:31253769, ECO:0000269\|PubMed:32522879, ECO:0000269\|PubMed:32821917, ECO:0000269\|PubMed:7651464, ECO:0000269\|PubMed:8078765, ECO:0000269\|PubMed:8090225, ECO:0000269\|PubMed:8206890, ECO:0000269\|PubMed:9927729}.
P29323	EPHB2	S782	ochoa	Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2]	Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. May be involved in the regulation of platelet activation and blood coagulation (PubMed:30213874). {ECO:0000269\|PubMed:15300251, ECO:0000269\|PubMed:30213874}.
P29558	RBMS1	S44	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29558	RBMS1	S49	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29558	RBMS1	S50	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29692	EEF1D	S70	ochoa	Elongation factor 1-delta (EF-1-delta) (Antigen NY-CO-4)	[Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
P29692	EEF1D	S71	ochoa	Elongation factor 1-delta (EF-1-delta) (Antigen NY-CO-4)	[Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
P30086	PEBP1	S60	ochoa	Phosphatidylethanolamine-binding protein 1 (PEBP-1) (HCNPpp) (Neuropolypeptide h3) (Prostatic-binding protein) (Raf kinase inhibitor protein) (RKIP) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)]	Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. {ECO:0000250, ECO:0000269\|PubMed:18294816}.; FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). {ECO:0000250}.
P30203	CD6	S568	psp	T-cell differentiation antigen CD6 (T12) (TP120) (CD antigen CD6) [Cleaved into: Soluble CD6]	Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166 (PubMed:15048703, PubMed:15294938, PubMed:16352806, PubMed:16914752, PubMed:24584089, PubMed:24945728). Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089). Functions as a costimulatory molecule; promotes T-cell activation and proliferation (PubMed:15294938, PubMed:16352806, PubMed:16914752). Contributes to the formation and maturation of the immunological synapse (PubMed:15294938, PubMed:16352806). Functions as a calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria (PubMed:17601777). LPS binding leads to the activation of signaling cascades and down-stream MAP kinases (PubMed:17601777). Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS (PubMed:17601777). {ECO:0000269\|PubMed:15048703, ECO:0000269\|PubMed:15294938, ECO:0000269\|PubMed:16352806, ECO:0000269\|PubMed:16914752, ECO:0000269\|PubMed:17601777, ECO:0000269\|PubMed:24584089, ECO:0000269\|PubMed:24945728}.
P30260	CDC27	S357	ochoa	Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (APC3) (CDC27 homolog) (CDC27Hs) (H-NUC)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
P30260	CDC27	S393	ochoa	Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (APC3) (CDC27 homolog) (CDC27Hs) (H-NUC)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
P30301	MIP	S235	psp	Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26)	Aquaporins form homotetrameric transmembrane channels, with each monomer independently mediating water transport across the plasma membrane along its osmotic gradient (PubMed:11001937, PubMed:24120416). Specifically expressed in lens fiber cells, this aquaporin is crucial for maintaining lens water homeostasis and transparency. Beyond water permeability, it also acts as a cell-to-cell adhesion molecule, forming thin junctions between lens fiber cells that are essential for maintaining the ordered structure and transparency of the lens (PubMed:24120416). {ECO:0000269\|PubMed:11001937, ECO:0000269\|PubMed:24120416}.
P30304	CDC25A	S82	psp	M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)	Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:12676925, PubMed:14559997, PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007). {ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:1836978, ECO:0000269\|PubMed:20360007}.
P30304	CDC25A	S88	psp	M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)	Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:12676925, PubMed:14559997, PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007). {ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:1836978, ECO:0000269\|PubMed:20360007}.
P30304	CDC25A	S267	ochoa	M-phase inducer phosphatase 1 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25A)	Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:12676925, PubMed:14559997, PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Also dephosphorylates CDK2 in complex with cyclin-E, in vitro (PubMed:20360007). {ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:1836978, ECO:0000269\|PubMed:20360007}.
P30414	NKTR	S204	ochoa	NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase)	PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). {ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:8421688}.
P30414	NKTR	S416	ochoa	NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase)	PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). {ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:8421688}.
P30414	NKTR	S814	ochoa	NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase)	PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). {ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:8421688}.
P30622	CLIP1	S158	ochoa	CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)	Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269\|PubMed:12433698, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:17889670}.
P30679	GNA15	S336	psp	Guanine nucleotide-binding protein subunit alpha-15 (G alpha-15) (G-protein subunit alpha-15) (Epididymis tissue protein Li 17E) (Guanine nucleotide-binding protein subunit alpha-16) (G alpha-16) (G-protein subunit alpha-16)	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
P31321	PRKAR1B	S77	ochoa	cAMP-dependent protein kinase type I-beta regulatory subunit	Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269\|PubMed:20819953}.
P31629	HIVEP2	S813	ochoa	Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2) (HIV-EP2) (MHC-binding protein 2) (MBP-2)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
P31629	HIVEP2	S819	ochoa	Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2) (HIV-EP2) (MHC-binding protein 2) (MBP-2)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
P31629	HIVEP2	S1622	ochoa	Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2) (HIV-EP2) (MHC-binding protein 2) (MBP-2)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
P33240	CSTF2	S524	ochoa	Cleavage stimulation factor subunit 2 (CF-1 64 kDa subunit) (Cleavage stimulation factor 64 kDa subunit) (CSTF 64 kDa subunit) (CstF-64)	One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs. {ECO:0000269\|PubMed:32816001, ECO:0000269\|PubMed:9199325}.
P33527	ABCC1	S921	ochoa\|psp	Multidrug resistance-associated protein 1 (EC 7.6.2.2) (ATP-binding cassette sub-family C member 1) (Glutathione-S-conjugate-translocating ATPase ABCC1) (EC 7.6.2.3) (Leukotriene C(4) transporter) (LTC4 transporter)	Mediates export of organic anions and drugs from the cytoplasm (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export (PubMed:9281595). Hydrolyzes ATP with low efficiency (PubMed:16230346). Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation (PubMed:17050692). Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthesizing cells (By similarity). Mediates ATP-dependent, GSH-independent cyclic GMP-AMP (cGAMP) export (PubMed:36070769). Thus, by limiting intracellular cGAMP concentrations negatively regulates the cGAS-STING pathway (PubMed:36070769). Exports S-geranylgeranyl-glutathione (GGG) in lymphoid cells and stromal compartments of lymphoid organs. ABCC1 (via extracellular transport) with GGT5 (via GGG catabolism) establish GGG gradients within lymphoid tissues to position P2RY8-positive lymphocytes at germinal centers in lymphoid follicles and restrict their chemotactic transmigration from blood vessels to the bone marrow parenchyma (By similarity). Mediates basolateral export of GSH-conjugated R- and S-prostaglandin A2 diastereomers in polarized epithelial cells (PubMed:9426231). {ECO:0000250\|UniProtKB:O35379, ECO:0000269\|PubMed:10064732, ECO:0000269\|PubMed:11114332, ECO:0000269\|PubMed:16230346, ECO:0000269\|PubMed:17050692, ECO:0000269\|PubMed:36070769, ECO:0000269\|PubMed:7961706, ECO:0000269\|PubMed:9281595, ECO:0000269\|PubMed:9426231}.
P33991	MCM4	S32	ochoa\|psp	DNA replication licensing factor MCM4 (EC 3.6.4.12) (CDC21 homolog) (P1-CDC21)	Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232, PubMed:9305914). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:16899510, PubMed:25661590, PubMed:32453425, PubMed:9305914). {ECO:0000269\|PubMed:16899510, ECO:0000269\|PubMed:25661590, ECO:0000269\|PubMed:32453425, ECO:0000269\|PubMed:34694004, ECO:0000269\|PubMed:34700328, ECO:0000269\|PubMed:35585232, ECO:0000269\|PubMed:9305914}.
P34932	HSPA4	S414	ochoa	Heat shock 70 kDa protein 4 (HSP70RY) (Heat shock 70-related protein APG-2) (Heat shock protein family H member 2)	None
P35222	CTNNB1	S29	ochoa\|psp	Catenin beta-1 (Beta-catenin)	Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250\|UniProtKB:Q02248, ECO:0000269\|PubMed:17524503, ECO:0000269\|PubMed:18077326, ECO:0000269\|PubMed:18086858, ECO:0000269\|PubMed:18957423, ECO:0000269\|PubMed:21262353, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22187462, ECO:0000269\|PubMed:22647378, ECO:0000269\|PubMed:22699938, ECO:0000269\|PubMed:29910125}.
P35222	CTNNB1	S681	ochoa	Catenin beta-1 (Beta-catenin)	Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250\|UniProtKB:Q02248, ECO:0000269\|PubMed:17524503, ECO:0000269\|PubMed:18077326, ECO:0000269\|PubMed:18086858, ECO:0000269\|PubMed:18957423, ECO:0000269\|PubMed:21262353, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22187462, ECO:0000269\|PubMed:22647378, ECO:0000269\|PubMed:22699938, ECO:0000269\|PubMed:29910125}.
P35269	GTF2F1	S391	ochoa	General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74)	TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269\|PubMed:10428810}.
P35269	GTF2F1	S442	ochoa	General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74)	TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269\|PubMed:10428810}.
P35348	ADRA1A	S407	psp	Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor) (Alpha-adrenergic receptor 1c)	This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269\|PubMed:18802028, ECO:0000269\|PubMed:22120526}.
P35348	ADRA1A	S413	psp	Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1A adrenoceptor) (Alpha-1C adrenergic receptor) (Alpha-adrenergic receptor 1c)	This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269\|PubMed:18802028, ECO:0000269\|PubMed:22120526}.
P35523	CLCN1	S892	psp	Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle)	Voltage-gated chloride channel involved in skeletal muscle excitability. Generates most of the plasma membrane chloride conductance in skeletal muscle fibers, stabilizes the resting membrane potential and contributes to the repolarization phase during action potential firing (PubMed:12456816, PubMed:16027167, PubMed:22521272, PubMed:22641783, PubMed:26007199, PubMed:26502825, PubMed:26510092, PubMed:7951242, PubMed:8112288, PubMed:8130334, PubMed:9122265, PubMed:9565403, PubMed:9736777). Forms a homodimeric channel where each subunit has its own ion conduction pathway. Conducts double-barreled currents controlled by two types of gates, two fast glutamate gates that control each subunit independently and a slow common gate that opens and shuts off both subunits simultaneously. Has a significant open probability at muscle resting potential and is further activated upon membrane depolarization (PubMed:10051520, PubMed:10962018, PubMed:29809153, PubMed:31022181). Permeable to small monovalent anions with ion selectivity for chloride > thiocyanate > bromide > nitrate > iodide (PubMed:9122265, PubMed:9565403). {ECO:0000269\|PubMed:10051520, ECO:0000269\|PubMed:10962018, ECO:0000269\|PubMed:12456816, ECO:0000269\|PubMed:16027167, ECO:0000269\|PubMed:22521272, ECO:0000269\|PubMed:22641783, ECO:0000269\|PubMed:26007199, ECO:0000269\|PubMed:26502825, ECO:0000269\|PubMed:26510092, ECO:0000269\|PubMed:29809153, ECO:0000269\|PubMed:31022181, ECO:0000269\|PubMed:7951242, ECO:0000269\|PubMed:8112288, ECO:0000269\|PubMed:8130334, ECO:0000269\|PubMed:9122265, ECO:0000269\|PubMed:9565403, ECO:0000269\|PubMed:9736777}.
P35568	IRS1	S1106	ochoa	Insulin receptor substrate 1 (IRS-1)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:7541045, PubMed:33991522, PubMed:38625937). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:19639489). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:11171109, PubMed:8265614). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:11171109, ECO:0000269\|PubMed:16878150, ECO:0000269\|PubMed:19639489, ECO:0000269\|PubMed:38625937, ECO:0000269\|PubMed:7541045, ECO:0000269\|PubMed:8265614}.
P35613	BSG	S368	ochoa	Basigin (5F7) (Collagenase stimulatory factor) (Extracellular matrix metalloproteinase inducer) (EMMPRIN) (Hepatoma-associated antigen) (HAb18G) (Leukocyte activation antigen M6) (OK blood group antigen) (Tumor cell-derived collagenase stimulatory factor) (TCSF) (CD antigen CD147)	[Isoform 1]: Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors (PubMed:25957687). In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors (PubMed:25957687). May act as a potent stimulator of IL6 secretion in multiple cell lines that include monocytes (PubMed:21620857). {ECO:0000250\|UniProtKB:P18572, ECO:0000269\|PubMed:21620857, ECO:0000269\|PubMed:25957687}.; FUNCTION: [Isoform 1]: (Microbial infection) Erythrocyte receptor for P.falciparum RH5 which is essential for erythrocyte invasion by the merozoite stage of P.falciparum isolates 3D7 and Dd2. {ECO:0000269\|PubMed:22080952}.; FUNCTION: [Isoform 2]: Signaling receptor for cyclophilins, essential for PPIA/CYPA and PPIB/CYPB-dependent signaling related to chemotaxis and adhesion of immune cells (PubMed:11688976, PubMed:11943775). Plays an important role in targeting monocarboxylate transporters SLC16A1/GLUT1, SLC16A11 and SLC16A12 to the plasma membrane (PubMed:17127621, PubMed:21778275, PubMed:28666119). Acts as a coreceptor for vascular endothelial growth factor receptor 2 (KDR/VEGFR2) in endothelial cells enhancing its VEGFA-mediated activation and downstream signaling (PubMed:25825981). Promotes angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA (isoform VEGF-165 and VEGF-121) and KDR/VEGFR2 in endothelial cells (PubMed:19837976). Plays a key role in regulating tumor growth, invasion, metastasis and neoangiogenesis by stimulating the production and release of extracellular matrix metalloproteinases and KDR/VEGFR2 by both tumor cells and stromal cells (fibroblasts and endothelial cells) (PubMed:11992541, PubMed:12553375, PubMed:15833850). {ECO:0000269\|PubMed:11688976, ECO:0000269\|PubMed:11943775, ECO:0000269\|PubMed:11992541, ECO:0000269\|PubMed:12553375, ECO:0000269\|PubMed:15833850, ECO:0000269\|PubMed:17127621, ECO:0000269\|PubMed:19837976, ECO:0000269\|PubMed:21778275, ECO:0000269\|PubMed:25825981, ECO:0000269\|PubMed:28666119}.; FUNCTION: [Isoform 2]: (Microbial infection) Erythrocyte receptor for P.falciparum RH5 which is essential for erythrocyte invasion by the merozoite stage of P.falciparum isolates 3D7, Dd2, 7G8 and HB3 (PubMed:22080952, PubMed:26195724). Binding of P.falciparum RH5 results in BSG dimerization which triggers an increase in intracellular Ca(2+) in the erythrocyte (PubMed:28409866). This essential step leads to a rearrangement of the erythrocyte cytoskeleton required for the merozoite invasion (PubMed:28409866). {ECO:0000269\|PubMed:22080952, ECO:0000269\|PubMed:26195724, ECO:0000269\|PubMed:28409866}.; FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate human SARS coronavirus (SARS-CoV-1) infection via its interaction with virus-associated PPIA/CYPA. {ECO:0000269\|PubMed:15688292}.; FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate HIV-1 infection via its interaction with virus-associated PPIA/CYPA. {ECO:0000269\|PubMed:11353871}.; FUNCTION: [Isoform 2]: (Microbial infection) First described as a receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), it is not required for SARS-CoV-2 infection. {ECO:0000269\|PubMed:33432067, ECO:0000303\|PubMed:32307653}.; FUNCTION: [Isoform 2]: (Microbial infection) Acts as a receptor for measles virus. {ECO:0000269\|PubMed:20147391}.; FUNCTION: [Isoform 2]: (Microbial infection) Promotes entry of pentamer-expressing human cytomegalovirus (HCMV) into epithelial and endothelial cells. {ECO:0000269\|PubMed:29739904}.
P35711	SOX5	S126	ochoa	Transcription factor SOX-5	Transcription factor involved in chondrocytes differentiation and cartilage formation. Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes, such as COL2A1 and AGC1. Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes. Together with SOX6, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts. Binds to the proximal promoter region of the myelin protein MPZ gene. {ECO:0000250\|UniProtKB:P35710}.
P35716	SOX11	S284	ochoa	Transcription factor SOX-11	Transcription factor that acts as a transcriptional activator (PubMed:24886874, PubMed:26543203). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity). {ECO:0000250\|UniProtKB:Q7M6Y2, ECO:0000269\|PubMed:24886874, ECO:0000269\|PubMed:26543203}.
P35749	MYH11	S643	ochoa	Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC)	Muscle contraction.
P36507	MAP2K2	S222	ochoa\|psp	Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)	Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). {ECO:0000250\|UniProtKB:Q63932, ECO:0000269\|PubMed:29433126}.
P37275	ZEB1	S319	ochoa	Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8)	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2 transcription via binding to the E-box in the upstream enhancer region (By similarity). {ECO:0000250\|UniProtKB:Q64318, ECO:0000269\|PubMed:19935649, ECO:0000269\|PubMed:20175752, ECO:0000269\|PubMed:20418909}.
P37275	ZEB1	S679	ochoa	Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8)	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2 transcription via binding to the E-box in the upstream enhancer region (By similarity). {ECO:0000250\|UniProtKB:Q64318, ECO:0000269\|PubMed:19935649, ECO:0000269\|PubMed:20175752, ECO:0000269\|PubMed:20418909}.
P37275	ZEB1	S704	ochoa	Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8)	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2 transcription via binding to the E-box in the upstream enhancer region (By similarity). {ECO:0000250\|UniProtKB:Q64318, ECO:0000269\|PubMed:19935649, ECO:0000269\|PubMed:20175752, ECO:0000269\|PubMed:20418909}.
P38159	RBMX	S293	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38159	RBMX	S314	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38159	RBMX	S329	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38159	RBMX	S332	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38159	RBMX	S336	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38398	BRCA1	S1466	ochoa	Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)	E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269\|PubMed:10500182, ECO:0000269\|PubMed:10724175, ECO:0000269\|PubMed:11836499, ECO:0000269\|PubMed:12183412, ECO:0000269\|PubMed:12887909, ECO:0000269\|PubMed:12890688, ECO:0000269\|PubMed:14976165, ECO:0000269\|PubMed:16326698, ECO:0000269\|PubMed:16818604, ECO:0000269\|PubMed:17525340, ECO:0000269\|PubMed:18056443, ECO:0000269\|PubMed:19261748, ECO:0000269\|PubMed:19369211, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:20351172}.
P38398	BRCA1	S1486	ochoa	Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)	E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269\|PubMed:10500182, ECO:0000269\|PubMed:10724175, ECO:0000269\|PubMed:11836499, ECO:0000269\|PubMed:12183412, ECO:0000269\|PubMed:12887909, ECO:0000269\|PubMed:12890688, ECO:0000269\|PubMed:14976165, ECO:0000269\|PubMed:16326698, ECO:0000269\|PubMed:16818604, ECO:0000269\|PubMed:17525340, ECO:0000269\|PubMed:18056443, ECO:0000269\|PubMed:19261748, ECO:0000269\|PubMed:19369211, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:20351172}.
P38398	BRCA1	S1503	ochoa	Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)	E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269\|PubMed:10500182, ECO:0000269\|PubMed:10724175, ECO:0000269\|PubMed:11836499, ECO:0000269\|PubMed:12183412, ECO:0000269\|PubMed:12887909, ECO:0000269\|PubMed:12890688, ECO:0000269\|PubMed:14976165, ECO:0000269\|PubMed:16326698, ECO:0000269\|PubMed:16818604, ECO:0000269\|PubMed:17525340, ECO:0000269\|PubMed:18056443, ECO:0000269\|PubMed:19261748, ECO:0000269\|PubMed:19369211, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:20351172}.
P41162	ETV3	S139	ochoa	ETS translocation variant 3 (ETS domain transcriptional repressor PE1) (PE-1) (Mitogenic Ets transcriptional suppressor)	Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. {ECO:0000269\|PubMed:12007404}.
P41235	HNF4A	S148	ochoa	Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)	Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes (PubMed:30597922). Activates the transcription of CYP2C38 (By similarity). Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells (PubMed:30530698). {ECO:0000250\|UniProtKB:P49698, ECO:0000269\|PubMed:30530698, ECO:0000269\|PubMed:30597922}.
P42166	TMPO	S301	ochoa	Lamina-associated polypeptide 2, isoform alpha (Thymopoietin isoform alpha) (TP alpha) (Thymopoietin-related peptide isoform alpha) (TPRP isoform alpha) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)]	May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
P42166	TMPO	S354	ochoa	Lamina-associated polypeptide 2, isoform alpha (Thymopoietin isoform alpha) (TP alpha) (Thymopoietin-related peptide isoform alpha) (TPRP isoform alpha) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)]	May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
P42331	ARHGAP25	S401	ochoa	Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.
P42331	ARHGAP25	S517	ochoa	Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.
P42345	MTOR	S2454	ochoa	Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin and FKBP12 target 1) (Rapamycin target protein 1) (Tyrosine-protein kinase mTOR) (EC 2.7.10.2)	Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:29236692, PubMed:31112131, PubMed:31601708, PubMed:32561715, PubMed:34519269, PubMed:37751742). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed:15268862, PubMed:15467718, PubMed:17517883, PubMed:18372248, PubMed:18497260, PubMed:18925875, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704, PubMed:30171069, PubMed:29236692, PubMed:37751742). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862, PubMed:15467718, PubMed:18497260, PubMed:18925875, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704, PubMed:29424687, PubMed:29567957, PubMed:35926713). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:29236692, PubMed:31112131, PubMed:34519269). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed:24403073, PubMed:29236692). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:12087098, PubMed:12150925, PubMed:18925875, PubMed:29150432, PubMed:29236692). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed:23429703, PubMed:23429704). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation (PubMed:36691768). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (PubMed:23426360). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1 (PubMed:32561715). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed:32561715). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed:23524951, PubMed:25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:24403073, PubMed:31695197). The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670, PubMed:36697823). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670). The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization (PubMed:34289345). MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15467718, PubMed:24670654, PubMed:29424687, PubMed:29567957, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:15268862, PubMed:15467718, PubMed:21376236, PubMed:24670654, PubMed:29424687, PubMed:29567957, PubMed:35926713). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:21376236, PubMed:24670654, PubMed:29424687, PubMed:29567957). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo (PubMed:26584640). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity). {ECO:0000250\|UniProtKB:Q9JLN9, ECO:0000269\|PubMed:12087098, ECO:0000269\|PubMed:12150925, ECO:0000269\|PubMed:12150926, ECO:0000269\|PubMed:12231510, ECO:0000269\|PubMed:12718876, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15545625, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:17517883, ECO:0000269\|PubMed:18372248, ECO:0000269\|PubMed:18497260, ECO:0000269\|PubMed:18762023, ECO:0000269\|PubMed:18925875, ECO:0000269\|PubMed:20516213, ECO:0000269\|PubMed:20537536, ECO:0000269\|PubMed:21376236, ECO:0000269\|PubMed:21576368, ECO:0000269\|PubMed:21659604, ECO:0000269\|PubMed:22343943, ECO:0000269\|PubMed:22576015, ECO:0000269\|PubMed:22692423, ECO:0000269\|PubMed:23426360, ECO:0000269\|PubMed:23429703, ECO:0000269\|PubMed:23429704, ECO:0000269\|PubMed:23524951, ECO:0000269\|PubMed:24403073, ECO:0000269\|PubMed:24448649, ECO:0000269\|PubMed:24670654, ECO:0000269\|PubMed:25438055, ECO:0000269\|PubMed:25799227, ECO:0000269\|PubMed:26018084, ECO:0000269\|PubMed:26584640, ECO:0000269\|PubMed:29150432, ECO:0000269\|PubMed:29236692, ECO:0000269\|PubMed:29424687, ECO:0000269\|PubMed:29567957, ECO:0000269\|PubMed:30171069, ECO:0000269\|PubMed:30704899, ECO:0000269\|PubMed:31112131, ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31695197, ECO:0000269\|PubMed:32561715, ECO:0000269\|PubMed:32612235, ECO:0000269\|PubMed:34289345, ECO:0000269\|PubMed:34519269, ECO:0000269\|PubMed:35926713, ECO:0000269\|PubMed:36608670, ECO:0000269\|PubMed:36691768, ECO:0000269\|PubMed:36697823, ECO:0000269\|PubMed:37751742}.
P42356	PI4KA	S262	ochoa	Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67) (Phosphatidylinositol 4-Kinase III alpha)	Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000269\|PubMed:10101268, ECO:0000269\|PubMed:23229899}.
P42356	PI4KA	S265	ochoa	Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67) (Phosphatidylinositol 4-Kinase III alpha)	Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000269\|PubMed:10101268, ECO:0000269\|PubMed:23229899}.
P42566	EPS15	S113	ochoa	Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)	Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:16903783, ECO:0000269\|PubMed:18362181, ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170}.
P42566	EPS15	S330	ochoa	Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)	Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:16903783, ECO:0000269\|PubMed:18362181, ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170}.
P42566	EPS15	S675	ochoa	Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)	Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:16903783, ECO:0000269\|PubMed:18362181, ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170}.
P42566	EPS15	S681	ochoa	Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)	Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:16903783, ECO:0000269\|PubMed:18362181, ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170}.
P42568	MLLT3	S294	ochoa	Protein AF-9 (ALL1-fused gene from chromosome 9 protein) (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein) (YEATS domain-containing protein 3)	Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated (PubMed:25417107, PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25417107, PubMed:27105114, PubMed:27545619). Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114). Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3 (PubMed:25417107, PubMed:27105114, PubMed:30385749). In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones (PubMed:27105114, PubMed:27545619). Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me) (PubMed:25417107). Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than conferring, HSC stemness (PubMed:31776511). Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L (PubMed:31776511). {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:25417107, ECO:0000269\|PubMed:27105114, ECO:0000269\|PubMed:27545619, ECO:0000269\|PubMed:30374167, ECO:0000269\|PubMed:30385749, ECO:0000269\|PubMed:31776511}.
P42684	ABL2	S208	ochoa	Tyrosine-protein kinase ABL2 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 2) (Abelson tyrosine-protein kinase 2) (Abelson-related gene protein) (Tyrosine-protein kinase ARG)	Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 also acts as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). {ECO:0000250\|UniProtKB:Q4JIM5, ECO:0000269\|PubMed:15735735, ECO:0000269\|PubMed:15886098, ECO:0000269\|PubMed:16678104, ECO:0000269\|PubMed:17306540, ECO:0000269\|PubMed:18945674}.
P42694	HELZ	S1620	ochoa	Probable helicase with zinc finger domain (EC 3.6.4.-) (Down-regulated in human cancers protein)	May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo.
P42694	HELZ	S1744	ochoa	Probable helicase with zinc finger domain (EC 3.6.4.-) (Down-regulated in human cancers protein)	May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo.
P42694	HELZ	S1771	ochoa	Probable helicase with zinc finger domain (EC 3.6.4.-) (Down-regulated in human cancers protein)	May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo.
P42695	NCAPD3	S523	ochoa	Condensin-2 complex subunit D3 (Non-SMC condensin II complex subunit D3) (hCAP-D3)	Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis (PubMed:14532007). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Specifically required for decatenation of centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). {ECO:0000269\|PubMed:14532007, ECO:0000269\|PubMed:27737959}.
P42702	LIFR	S1050	ochoa	Leukemia inhibitory factor receptor (LIF receptor) (LIF-R) (CD antigen CD118)	Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.
P42858	HTT	S1870	ochoa\|psp	Huntingtin (Huntington disease protein) (HD protein) [Cleaved into: Huntingtin, myristoylated N-terminal fragment]	[Huntingtin]: May play a role in microtubule-mediated transport or vesicle function.; FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the formation of autophagic vesicles. {ECO:0000269\|PubMed:24459296}.
P43243	MATR3	S77	ochoa	Matrin-3	May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:11525732, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32245947}.
P43243	MATR3	S80	ochoa	Matrin-3	May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:11525732, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32245947}.
P43243	MATR3	S604	ochoa	Matrin-3	May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:11525732, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32245947}.
P43354	NR4A2	S256	ochoa	Nuclear receptor subfamily 4 group A member 2 (Immediate-early response protein NOT) (Orphan nuclear receptor NURR1) (Transcriptionally-inducible nuclear receptor)	Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development (PubMed:15716272, PubMed:17184956). It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity). {ECO:0000250\|UniProtKB:Q06219, ECO:0000269\|PubMed:15716272, ECO:0000269\|PubMed:17184956}.
P45985	MAP2K4	S257	ochoa\|psp	Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1) (Stress-activated protein kinase kinase 1) (SAPK kinase 1) (SAPKK-1) (SAPKK1) (c-Jun N-terminal kinase kinase 1) (JNKK)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to pro-inflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269\|PubMed:7716521}.
P46013	MKI67	S131	ochoa	Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67)	Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250\|UniProtKB:E9PVX6, ECO:0000269\|PubMed:10878551, ECO:0000269\|PubMed:24867636, ECO:0000269\|PubMed:27362226, ECO:0000269\|PubMed:28935370, ECO:0000269\|PubMed:32879492, ECO:0000269\|PubMed:35513709, ECO:0000269\|PubMed:39153474}.
P46013	MKI67	S713	ochoa	Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67)	Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250\|UniProtKB:E9PVX6, ECO:0000269\|PubMed:10878551, ECO:0000269\|PubMed:24867636, ECO:0000269\|PubMed:27362226, ECO:0000269\|PubMed:28935370, ECO:0000269\|PubMed:32879492, ECO:0000269\|PubMed:35513709, ECO:0000269\|PubMed:39153474}.
P46019	PHKA2	S1049	ochoa	Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit)	Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
P46019	PHKA2	S1050	ochoa	Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit)	Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
P46020	PHKA1	S978	ochoa	Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (Phosphorylase kinase alpha M subunit)	Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
P46379	BAG6	S106	ochoa	Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe)	ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (PubMed:26565908). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250\|UniProtKB:Q9Z1R2, ECO:0000269\|PubMed:20516149, ECO:0000269\|PubMed:20676083, ECO:0000269\|PubMed:21636303, ECO:0000269\|PubMed:21743475, ECO:0000269\|PubMed:23129660, ECO:0000269\|PubMed:24981174, ECO:0000269\|PubMed:25179605, ECO:0000269\|PubMed:26565908, ECO:0000269\|PubMed:26692333, ECO:0000269\|PubMed:27193484, ECO:0000269\|PubMed:28104892}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity (PubMed:17403783). When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). {ECO:0000269\|PubMed:17403783, ECO:0000269\|PubMed:18765639}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000269\|PubMed:18055229, ECO:0000269\|PubMed:18852879}.; FUNCTION: Mediates ricin-induced apoptosis. {ECO:0000269\|PubMed:14960581}.
P46821	MAP1B	S1211	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1330	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1345	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1406	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1421	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1646	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1785	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1803	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46934	NEDD4	S739	ochoa	E3 ubiquitin-protein ligase NEDD4 (EC 2.3.2.26) (Cell proliferation-inducing gene 53 protein) (HECT-type E3 ubiquitin transferase NEDD4) (Neural precursor cell expressed developmentally down-regulated protein 4) (NEDD-4)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:19920177, PubMed:21399620, PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes (By similarity). Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes (PubMed:21765395). Promotes ubiquitination of RAPGEF2 (PubMed:11598133). According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD (By similarity). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (By similarity). Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (PubMed:20086093). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Ubiquitinates DAZAP2, leading to its proteasomal degradation (PubMed:11342538). Ubiquitinates POLR2A (PubMed:19920177). Functions as a platform to recruit USP13 to form an NEDD4-USP13 deubiquitination complex that plays a critical role in cleaving the 'Lys-48'-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes (PubMed:32101753). {ECO:0000250\|UniProtKB:P46935, ECO:0000269\|PubMed:11342538, ECO:0000269\|PubMed:11598133, ECO:0000269\|PubMed:17218260, ECO:0000269\|PubMed:18562292, ECO:0000269\|PubMed:21399620, ECO:0000269\|PubMed:21765395, ECO:0000269\|PubMed:23644597, ECO:0000269\|PubMed:25631046, ECO:0000269\|PubMed:32101753}.; FUNCTION: (Microbial infection) Involved in the ubiquitination of Ebola virus protein VP40 which plays a role in viral budding. {ECO:0000269\|PubMed:12559917, ECO:0000269\|PubMed:18305167}.
P46934	NEDD4	S743	ochoa	E3 ubiquitin-protein ligase NEDD4 (EC 2.3.2.26) (Cell proliferation-inducing gene 53 protein) (HECT-type E3 ubiquitin transferase NEDD4) (Neural precursor cell expressed developmentally down-regulated protein 4) (NEDD-4)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:19920177, PubMed:21399620, PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes (By similarity). Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes (PubMed:21765395). Promotes ubiquitination of RAPGEF2 (PubMed:11598133). According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD (By similarity). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (By similarity). Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (PubMed:20086093). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Ubiquitinates DAZAP2, leading to its proteasomal degradation (PubMed:11342538). Ubiquitinates POLR2A (PubMed:19920177). Functions as a platform to recruit USP13 to form an NEDD4-USP13 deubiquitination complex that plays a critical role in cleaving the 'Lys-48'-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes (PubMed:32101753). {ECO:0000250\|UniProtKB:P46935, ECO:0000269\|PubMed:11342538, ECO:0000269\|PubMed:11598133, ECO:0000269\|PubMed:17218260, ECO:0000269\|PubMed:18562292, ECO:0000269\|PubMed:21399620, ECO:0000269\|PubMed:21765395, ECO:0000269\|PubMed:23644597, ECO:0000269\|PubMed:25631046, ECO:0000269\|PubMed:32101753}.; FUNCTION: (Microbial infection) Involved in the ubiquitination of Ebola virus protein VP40 which plays a role in viral budding. {ECO:0000269\|PubMed:12559917, ECO:0000269\|PubMed:18305167}.
P46937	YAP1	S109	ochoa\|psp	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P46937	YAP1	S388	ochoa\|psp	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P46937	YAP1	S403	ochoa\|psp	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P46937	YAP1	S406	ochoa	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P46939	UTRN	S833	ochoa	Utrophin (Dystrophin-related protein 1) (DRP-1)	May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}.
P46939	UTRN	S2219	ochoa	Utrophin (Dystrophin-related protein 1) (DRP-1)	May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}.
P47712	PLA2G4A	S441	ochoa	Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)]	Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:18451993, PubMed:27642067, PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:8619991, PubMed:9425121). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:9425121). In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891). Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891). {ECO:0000250\|UniProtKB:P47713, ECO:0000269\|PubMed:10358058, ECO:0000269\|PubMed:12672805, ECO:0000269\|PubMed:14709560, ECO:0000269\|PubMed:16617059, ECO:0000269\|PubMed:17472963, ECO:0000269\|PubMed:18451993, ECO:0000269\|PubMed:27642067, ECO:0000269\|PubMed:7794891, ECO:0000269\|PubMed:8619991, ECO:0000269\|PubMed:8702602, ECO:0000269\|PubMed:9425121}.
P47736	RAP1GAP	S490	psp	Rap1 GTPase-activating protein 1 (Rap1GAP) (Rap1GAP1)	GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269\|PubMed:15141215}.
P47974	ZFP36L2	S265	ochoa	mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (EGF-response factor 2) (ERF-2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2)	Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:14981510, PubMed:25106868, PubMed:34611029). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:25106868). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (PubMed:25106868). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:14981510, PubMed:20506496, PubMed:25106868). Promotes ARE-containing mRNA decay of the low-density lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (PubMed:25106868). Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Plays a role in mature peripheral neuron integrity by promoting ARE-containing mRNA decay of the transcriptional repressor REST mRNA. Plays a role in ovulation and oocyte meiotic maturation by promoting ARE-mediated mRNA decay of the luteinizing hormone receptor LHCGR mRNA. Acts as a negative regulator of erythroid cell differentiation: promotes glucocorticoid-induced self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. In association with ZFP36L1 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination process and functional immune cell formation. Together with ZFP36L1 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA. {ECO:0000250\|UniProtKB:P23949, ECO:0000269\|PubMed:14981510, ECO:0000269\|PubMed:20506496, ECO:0000269\|PubMed:25106868, ECO:0000269\|PubMed:34611029}.
P48444	ARCN1	S195	ochoa	Coatomer subunit delta (Archain) (Delta-coat protein) (Delta-COP)	Component of the coatomer, a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.
P48634	PRRC2A	S166	ochoa	Protein PRRC2A (HLA-B-associated transcript 2) (Large proline-rich protein BAT2) (Proline-rich and coiled-coil-containing protein 2A) (Protein G2)	May play a role in the regulation of pre-mRNA splicing. {ECO:0000269\|PubMed:14667819}.
P48634	PRRC2A	S204	ochoa	Protein PRRC2A (HLA-B-associated transcript 2) (Large proline-rich protein BAT2) (Proline-rich and coiled-coil-containing protein 2A) (Protein G2)	May play a role in the regulation of pre-mRNA splicing. {ECO:0000269\|PubMed:14667819}.
P48634	PRRC2A	S765	ochoa	Protein PRRC2A (HLA-B-associated transcript 2) (Large proline-rich protein BAT2) (Proline-rich and coiled-coil-containing protein 2A) (Protein G2)	May play a role in the regulation of pre-mRNA splicing. {ECO:0000269\|PubMed:14667819}.
P48681	NES	S358	ochoa	Nestin	Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.
P48681	NES	S465	ochoa	Nestin	Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.
P48681	NES	S1451	ochoa	Nestin	Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.
P48681	NES	S1502	ochoa	Nestin	Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.
P49005	POLD2	S257	ochoa	DNA polymerase delta subunit 2 (DNA polymerase delta subunit p50)	Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex (PubMed:17317665, PubMed:22801543, PubMed:24449906). As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:12403614, PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200). Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the DNA polymerase zeta complex (PubMed:24449906). Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the DNA polymerase zeta complex compared to the minimal zeta complex, consisting of only REV3L and REV7 (PubMed:24449906). {ECO:0000269\|PubMed:12403614, ECO:0000269\|PubMed:16510448, ECO:0000269\|PubMed:19074196, ECO:0000269\|PubMed:20227374, ECO:0000269\|PubMed:20334433, ECO:0000269\|PubMed:24035200, ECO:0000269\|PubMed:24310611, ECO:0000269\|PubMed:24449906}.
P49023	PXN	S90	ochoa	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	S91	ochoa	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	S109	ochoa	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	S143	ochoa	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	S250	ochoa\|psp	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49685	GPR15	S335	ochoa	G-protein coupled receptor 15 (Brother of Bonzo) (BoB)	G protein-coupled receptor that plays an important role in immune homeostasis (PubMed:33758080, PubMed:38918398). Acts via its natural ligand GPR15LG, a chemokine-like polypeptide strongly expressed in gastrointestinal tissues. GPR15-GPR15LG signaling axis regulates intestinal homeostasis and inflammation through the migration of immune cells (PubMed:33758080, PubMed:38918398). Controls thereby the specific homing of T-cells, particularly FOXP3+ regulatory T-cells (Tregs), to the large intestine lamina propria (By similarity). Also required for skin localization of thymus-derived dendritic epidermal T-cells (By similarity). Plays an important role in mediating cytoprotective function as well as angiogenesis of thrombomodulin (By similarity). Mechanistically, preferentially signals through the Gi/o pathway to inhibit adenylate cyclase activity and activate a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores (PubMed:35510660). {ECO:0000250\|UniProtKB:Q0VDU3, ECO:0000269\|PubMed:33758080, ECO:0000269\|PubMed:35510660, ECO:0000269\|PubMed:38918398}.; FUNCTION: (Microbial infection) Acts as an alternative coreceptor with CD4 for HIV-1 infection. {ECO:0000269\|PubMed:9791028}.
P49736	MCM2	S32	ochoa	DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28)	Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677). {ECO:0000269\|PubMed:26196677, ECO:0000269\|PubMed:32453425, ECO:0000269\|PubMed:34694004, ECO:0000269\|PubMed:34700328, ECO:0000269\|PubMed:35585232, ECO:0000269\|PubMed:8175912}.
P49756	RBM25	S683	ochoa	RNA-binding protein 25 (Arg/Glu/Asp-rich protein of 120 kDa) (RED120) (Protein S164) (RNA-binding motif protein 25) (RNA-binding region-containing protein 7)	RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure. {ECO:0000269\|PubMed:18663000, ECO:0000269\|PubMed:21859973}.
P49757	NUMB	S247	ochoa	Protein numb homolog (h-Numb) (Protein S171)	Regulates clathrin-mediated receptor endocytosis (PubMed:18657069). Plays a role in the process of neurogenesis (By similarity). Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate (By similarity). Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity (By similarity). May also mediate local repair of brain ventricular wall damage (By similarity). {ECO:0000250\|UniProtKB:Q9QZS3, ECO:0000269\|PubMed:18657069}.
P49790	NUP153	S188	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S209	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S225	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S240	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S246	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S320	ochoa\|psp	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S522	ochoa\|psp	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49792	RANBP2	S773	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S796	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S1456	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S2462	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S2526	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S2561	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S2568	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49796	RGS3	S401	ochoa	Regulator of G-protein signaling 3 (RGP3) (RGS3)	Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. {ECO:0000269\|PubMed:10749886, ECO:0000269\|PubMed:11294858, ECO:0000269\|PubMed:8602223, ECO:0000269\|PubMed:9858594}.
P49815	TSC2	S1371	ochoa\|psp	Tuberin (Tuberous sclerosis 2 protein)	Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:35772404). Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12820960, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:33436626). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:35772404). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 (By similarity). {ECO:0000250\|UniProtKB:P49816, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12820960, ECO:0000269\|PubMed:12842888, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:22819219, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:33436626, ECO:0000269\|PubMed:35772404}.
P49916	LIG3	S216	ochoa	DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)	Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269\|PubMed:10207110, ECO:0000269\|PubMed:24674627}.
P49916	LIG3	S236	ochoa	DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)	Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269\|PubMed:10207110, ECO:0000269\|PubMed:24674627}.
P49916	LIG3	S853	ochoa	DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)	Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269\|PubMed:10207110, ECO:0000269\|PubMed:24674627}.
P49916	LIG3	S854	ochoa	DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)	Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269\|PubMed:10207110, ECO:0000269\|PubMed:24674627}.
P49959	MRE11	S275	ochoa	Double-strand break repair protein MRE11 (EC 3.1.-.-) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)	Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:11741547, PubMed:14657032, PubMed:22078559, PubMed:23080121, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:28867292, PubMed:29670289, PubMed:30464262, PubMed:30612738, PubMed:31353207, PubMed:37696958, PubMed:38128537, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:24316220, PubMed:28867292, PubMed:31353207, PubMed:38128537). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:24316220, PubMed:27889449, PubMed:28867292, PubMed:36050397, PubMed:38128537). Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:11741547, PubMed:22078559, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:29670289, PubMed:31353207, PubMed:36563124, PubMed:9590181, PubMed:9651580, PubMed:9705271). After DSBs, MRE11 is loaded onto DSBs sites and cleaves DNA by cooperating with RBBP8/CtIP to initiate end resection (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:24316220). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3' long-range resection, which is required for single-strand invasion and recombination (PubMed:24316220, PubMed:28867292). RBBP8/CtIP specifically promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 endonuclease activity is also enhanced by AGER/RAGE (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:14657032, PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). The MRN complex is involved in the activation of the cGAS-STING pathway induced by DNA damage during tumorigenesis: the MRN complex acts by displacing CGAS from nucleosome sequestration, thereby activating it (By similarity). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888). {ECO:0000250\|UniProtKB:Q61216, ECO:0000269\|PubMed:10888888, ECO:0000269\|PubMed:11741547, ECO:0000269\|PubMed:14657032, ECO:0000269\|PubMed:15064416, ECO:0000269\|PubMed:15790808, ECO:0000269\|PubMed:16622404, ECO:0000269\|PubMed:22078559, ECO:0000269\|PubMed:23080121, ECO:0000269\|PubMed:24316220, ECO:0000269\|PubMed:26240375, ECO:0000269\|PubMed:27814491, ECO:0000269\|PubMed:27889449, ECO:0000269\|PubMed:28867292, ECO:0000269\|PubMed:29670289, ECO:0000269\|PubMed:30464262, ECO:0000269\|PubMed:30612738, ECO:0000269\|PubMed:30787182, ECO:0000269\|PubMed:31353207, ECO:0000269\|PubMed:31537797, ECO:0000269\|PubMed:36050397, ECO:0000269\|PubMed:36563124, ECO:0000269\|PubMed:37696958, ECO:0000269\|PubMed:38128537, ECO:0000269\|PubMed:9590181, ECO:0000269\|PubMed:9651580, ECO:0000269\|PubMed:9705271}.; FUNCTION: MRE11 contains two DNA-binding domains (DBDs), enabling it to bind both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). {ECO:0000305}.
P50402	EMD	S58	ochoa	Emerin	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:32923640}.
P50402	EMD	Y59	psp	Emerin	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:32923640}.
P50402	EMD	S60	ochoa	Emerin	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:32923640}.
P50443	SLC26A2	S22	ochoa	Sulfate transporter (Diastrophic dysplasia protein) (Solute carrier family 26 member 2)	Sulfate transporter which mediates sulfate uptake into chondrocytes in order to maintain adequate sulfation of proteoglycans which is needed for cartilage development (PubMed:11448940, PubMed:15294877, PubMed:20219950, PubMed:7923357). Mediates electroneutral anion exchange of sulfate ions for oxalate ions and of sulfate and oxalate ions for chloride ions (PubMed:20219950). Mediates exchange of sulfate and oxalate ions for hydroxyl ions and of chloride ions for bromide, iodide and nitrate ions (By similarity). The coupling of sulfate transport to both hydroxyl and chloride ions likely serves to ensure transport at both acidic pH when most sulfate uptake is mediated by sulfate-hydroxide exchange and alkaline pH when most sulfate uptake is mediated by sulfate-chloride exchange (By similarity). Essential for chondrocyte proliferation, differentiation and cell size expansion (By similarity). {ECO:0000250\|UniProtKB:Q62273, ECO:0000269\|PubMed:11448940, ECO:0000269\|PubMed:15294877, ECO:0000269\|PubMed:20219950, ECO:0000269\|PubMed:7923357}.
P50548	ERF	S137	ochoa	ETS domain-containing transcription factor ERF (Ets2 repressor factor) (PE-2)	Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). {ECO:0000250}.
P50548	ERF	S167	ochoa	ETS domain-containing transcription factor ERF (Ets2 repressor factor) (PE-2)	Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). {ECO:0000250}.
P50552	VASP	S329	ochoa	Vasodilator-stimulated phosphoprotein (VASP)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. {ECO:0000269\|PubMed:10087267, ECO:0000269\|PubMed:10438535, ECO:0000269\|PubMed:15939738, ECO:0000269\|PubMed:17082196, ECO:0000269\|PubMed:18559661}.
P50750	CDK9	S353	ochoa\|psp	Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)	Protein kinase involved in the regulation of transcription (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094, PubMed:29335245). Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:16427012, PubMed:20930849, PubMed:28426094, PubMed:30134174). This complex is inactive when in the 7SK snRNP complex form (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR and the negative elongation factors DSIF and NELFE (PubMed:10912001, PubMed:11112772, PubMed:12037670, PubMed:16427012, PubMed:20081228, PubMed:20980437, PubMed:21127351, PubMed:9857195). Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling) (PubMed:17956865, PubMed:18362169). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis (PubMed:10393184, PubMed:11112772). P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export (PubMed:15564463, PubMed:19575011, PubMed:19844166). Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing (PubMed:15564463, PubMed:19575011, PubMed:19844166). The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro (PubMed:21127351). Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage (PubMed:20493174). In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6 (PubMed:20493174). Promotes cardiac myocyte enlargement (PubMed:20081228). RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription (PubMed:21127351). AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect (PubMed:10912001, PubMed:11112772, PubMed:9857195). The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (PubMed:12037670). Catalyzes phosphorylation of KAT5, promoting KAT5 recruitment to chromatin and histone acetyltransferase activity (PubMed:29335245). {ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:10574912, ECO:0000269\|PubMed:10757782, ECO:0000269\|PubMed:10912001, ECO:0000269\|PubMed:11112772, ECO:0000269\|PubMed:11145967, ECO:0000269\|PubMed:11575923, ECO:0000269\|PubMed:11809800, ECO:0000269\|PubMed:11884399, ECO:0000269\|PubMed:12037670, ECO:0000269\|PubMed:14701750, ECO:0000269\|PubMed:15564463, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:16427012, ECO:0000269\|PubMed:17956865, ECO:0000269\|PubMed:18362169, ECO:0000269\|PubMed:19575011, ECO:0000269\|PubMed:19844166, ECO:0000269\|PubMed:20081228, ECO:0000269\|PubMed:20493174, ECO:0000269\|PubMed:20930849, ECO:0000269\|PubMed:20980437, ECO:0000269\|PubMed:21127351, ECO:0000269\|PubMed:28426094, ECO:0000269\|PubMed:29335245, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:9857195}.
P50851	LRBA	S1237	ochoa	Lipopolysaccharide-responsive and beige-like anchor protein (Beige-like protein) (CDC4-like protein)	Involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules (By similarity). Involved in phagophore growth during mitophagy by regulating ATG9A trafficking to mitochondria (PubMed:33773106). {ECO:0000250\|UniProtKB:Q9ESE1, ECO:0000269\|PubMed:33773106}.
P50851	LRBA	S1767	ochoa	Lipopolysaccharide-responsive and beige-like anchor protein (Beige-like protein) (CDC4-like protein)	Involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules (By similarity). Involved in phagophore growth during mitophagy by regulating ATG9A trafficking to mitochondria (PubMed:33773106). {ECO:0000250\|UniProtKB:Q9ESE1, ECO:0000269\|PubMed:33773106}.
P51003	PAPOLA	S660	ochoa	Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha)	Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000269\|PubMed:19224921}.
P51116	FXR2	S453	ochoa	RNA-binding protein FXR2 (FXR2P) (FMR1 autosomal homolog 2)	mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for adult hippocampal neurogenesis (By similarity). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity). Acts as a regulator of adult hippocampal neurogenesis by regulating translation and/or stability of NOG mRNA, thereby preventing NOG protein expression in the dentate gyrus (By similarity). {ECO:0000250\|UniProtKB:Q61584, ECO:0000250\|UniProtKB:Q9WVR4}.
P51116	FXR2	S622	ochoa	RNA-binding protein FXR2 (FXR2P) (FMR1 autosomal homolog 2)	mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for adult hippocampal neurogenesis (By similarity). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity). Acts as a regulator of adult hippocampal neurogenesis by regulating translation and/or stability of NOG mRNA, thereby preventing NOG protein expression in the dentate gyrus (By similarity). {ECO:0000250\|UniProtKB:Q61584, ECO:0000250\|UniProtKB:Q9WVR4}.
P51587	BRCA2	S76	ochoa\|psp	Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein)	Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180). {ECO:0000269\|PubMed:15115758, ECO:0000269\|PubMed:15199141, ECO:0000269\|PubMed:15671039, ECO:0000269\|PubMed:18317453, ECO:0000269\|PubMed:20729832, ECO:0000269\|PubMed:20729858, ECO:0000269\|PubMed:20729859, ECO:0000269\|PubMed:21084279, ECO:0000269\|PubMed:21719596, ECO:0000269\|PubMed:24485656, ECO:0000269\|PubMed:24896180}.
P51617	IRAK1	S376	ochoa\|psp	Interleukin-1 receptor-associated kinase 1 (IRAK-1) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. {ECO:0000269\|PubMed:11397809, ECO:0000269\|PubMed:12860405, ECO:0000269\|PubMed:14684752, ECO:0000269\|PubMed:15084582, ECO:0000269\|PubMed:15465816, ECO:0000269\|PubMed:15767370, ECO:0000269\|PubMed:17997719, ECO:0000269\|PubMed:20400509}.
P51812	RPS6KA3	S375	ochoa	Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1 (PubMed:16213824, PubMed:16223362, PubMed:17360704, PubMed:9770464). In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes (PubMed:10436156, PubMed:9770464). In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:16223362). Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:8250835). Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex (PubMed:17360704). In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:18508509, PubMed:18813292). Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway (PubMed:18722121). Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:16213824). Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:18508509, PubMed:18813292). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (By similarity). In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3 (By similarity). Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1 (By similarity). Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630). Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity (By similarity). {ECO:0000250\|UniProtKB:P18654, ECO:0000269\|PubMed:10436156, ECO:0000269\|PubMed:16213824, ECO:0000269\|PubMed:16223362, ECO:0000269\|PubMed:17360704, ECO:0000269\|PubMed:18722121, ECO:0000269\|PubMed:26158630, ECO:0000269\|PubMed:8250835, ECO:0000269\|PubMed:9770464, ECO:0000303\|PubMed:18508509, ECO:0000303\|PubMed:18813292}.
P51826	AFF3	S884	ochoa	AF4/FMR2 family member 3 (Lymphoid nuclear protein related to AF4) (Protein LAF-4)	Putative transcription activator that may function in lymphoid development and oncogenesis. Binds, in vitro, to double-stranded DNA.
P51965	UBE2E1	S17	ochoa	Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1)	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. Catalyzes monoubiquitination of other proteins in both an E3-dependent and E3-independent manner (PubMed:27237050). {ECO:0000269\|PubMed:16428300, ECO:0000269\|PubMed:20061386, ECO:0000269\|PubMed:27237050}.
P51965	UBE2E1	S18	ochoa	Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1)	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. Catalyzes monoubiquitination of other proteins in both an E3-dependent and E3-independent manner (PubMed:27237050). {ECO:0000269\|PubMed:16428300, ECO:0000269\|PubMed:20061386, ECO:0000269\|PubMed:27237050}.
P52333	JAK3	S789	ochoa	Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) (L-JAK)	Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A and STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion. {ECO:0000269\|PubMed:11909529, ECO:0000269\|PubMed:20440074, ECO:0000269\|PubMed:7662955, ECO:0000269\|PubMed:8022485}.
P52594	AGFG1	S153	ochoa	Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)	Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269\|PubMed:10613896, ECO:0000269\|PubMed:14701878, ECO:0000269\|PubMed:15749819}.
P52594	AGFG1	S365	ochoa	Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)	Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269\|PubMed:10613896, ECO:0000269\|PubMed:14701878, ECO:0000269\|PubMed:15749819}.
P52594	AGFG1	S368	ochoa	Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)	Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269\|PubMed:10613896, ECO:0000269\|PubMed:14701878, ECO:0000269\|PubMed:15749819}.
P52594	AGFG1	S371	ochoa	Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)	Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269\|PubMed:10613896, ECO:0000269\|PubMed:14701878, ECO:0000269\|PubMed:15749819}.
P52701	MSH6	S285	ochoa	DNA mismatch repair protein Msh6 (hMSH6) (G/T mismatch-binding protein) (GTBP) (GTMBP) (MutS protein homolog 6) (MutS-alpha 160 kDa subunit) (p160)	Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. {ECO:0000269\|PubMed:10078208, ECO:0000269\|PubMed:10660545, ECO:0000269\|PubMed:15064730, ECO:0000269\|PubMed:21120944, ECO:0000269\|PubMed:23622243, ECO:0000269\|PubMed:9564049, ECO:0000269\|PubMed:9822679, ECO:0000269\|PubMed:9822680}.
P52799	EFNB2	S284	ochoa	Ephrin-B2 (EPH-related receptor tyrosine kinase ligand 5) (LERK-5) (HTK ligand) (HTK-L)	Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons. {ECO:0000269\|PubMed:12734395}.; FUNCTION: (Microbial infection) Acts as a receptor for Hendra virus and Nipah virus. {ECO:0000269\|PubMed:15998730, ECO:0000269\|PubMed:16007075, ECO:0000269\|PubMed:16477309, ECO:0000269\|PubMed:17376907}.
P52948	NUP98	S1034	ochoa	Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)]	Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:33097660}.; FUNCTION: (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed:23523133). {ECO:0000269\|PubMed:23523133}.
P53355	DAPK1	S319	ochoa	Death-associated protein kinase 1 (DAP kinase 1) (EC 2.7.11.1)	Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition.; FUNCTION: Isoform 2 cannot induce apoptosis but can induce membrane blebbing.
P53567	CEBPG	S62	ochoa	CCAAT/enhancer-binding protein gamma (C/EBP gamma)	Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. {ECO:0000250\|UniProtKB:P26801, ECO:0000250\|UniProtKB:P53568, ECO:0000269\|PubMed:7665092}.
P53621	COPA	S179	ochoa	Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin]	The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.
P53667	LIMK1	S302	ochoa	LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11832213, PubMed:12807904, PubMed:15660133, PubMed:16230460, PubMed:18028908, PubMed:22328514, PubMed:23633677). Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop (PubMed:10436159). LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly (PubMed:18028908). Stimulates axonal outgrowth and may be involved in brain development (PubMed:18028908). {ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:11832213, ECO:0000269\|PubMed:12807904, ECO:0000269\|PubMed:15660133, ECO:0000269\|PubMed:16230460, ECO:0000269\|PubMed:18028908, ECO:0000269\|PubMed:22328514, ECO:0000269\|PubMed:23633677}.; FUNCTION: [Isoform 3]: Has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1). {ECO:0000269\|PubMed:10196227}.
P53814	SMTN	S382	ochoa	Smoothelin	Structural protein of the cytoskeleton.
P53814	SMTN	S383	ochoa	Smoothelin	Structural protein of the cytoskeleton.
P53814	SMTN	S529	ochoa	Smoothelin	Structural protein of the cytoskeleton.
P53999	SUB1	S17	ochoa	Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269\|PubMed:16605275, ECO:0000269\|PubMed:16689930, ECO:0000269\|PubMed:7628453, ECO:0000269\|PubMed:8062391, ECO:0000269\|PubMed:8062392, ECO:0000269\|PubMed:9360603, ECO:0000269\|PubMed:9482861}.
P53999	SUB1	S19	ochoa	Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269\|PubMed:16605275, ECO:0000269\|PubMed:16689930, ECO:0000269\|PubMed:7628453, ECO:0000269\|PubMed:8062391, ECO:0000269\|PubMed:8062392, ECO:0000269\|PubMed:9360603, ECO:0000269\|PubMed:9482861}.
P53999	SUB1	S56	ochoa	Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269\|PubMed:16605275, ECO:0000269\|PubMed:16689930, ECO:0000269\|PubMed:7628453, ECO:0000269\|PubMed:8062391, ECO:0000269\|PubMed:8062392, ECO:0000269\|PubMed:9360603, ECO:0000269\|PubMed:9482861}.
P53999	SUB1	S58	ochoa	Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269\|PubMed:16605275, ECO:0000269\|PubMed:16689930, ECO:0000269\|PubMed:7628453, ECO:0000269\|PubMed:8062391, ECO:0000269\|PubMed:8062392, ECO:0000269\|PubMed:9360603, ECO:0000269\|PubMed:9482861}.
P54132	BLM	S149	ochoa	RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein) (DNA 3'-5' helicase BLM) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3)	ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity). {ECO:0000250\|UniProtKB:O88700, ECO:0000269\|PubMed:12019152, ECO:0000269\|PubMed:18426915, ECO:0000269\|PubMed:20639533, ECO:0000269\|PubMed:21325134, ECO:0000269\|PubMed:23509288, ECO:0000269\|PubMed:24257077, ECO:0000269\|PubMed:24816114, ECO:0000269\|PubMed:25901030, ECO:0000269\|PubMed:34606619, ECO:0000269\|PubMed:9388193, ECO:0000269\|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269\|PubMed:32690953}.
P54132	BLM	S1296	ochoa\|psp	RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein) (DNA 3'-5' helicase BLM) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3)	ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity). {ECO:0000250\|UniProtKB:O88700, ECO:0000269\|PubMed:12019152, ECO:0000269\|PubMed:18426915, ECO:0000269\|PubMed:20639533, ECO:0000269\|PubMed:21325134, ECO:0000269\|PubMed:23509288, ECO:0000269\|PubMed:24257077, ECO:0000269\|PubMed:24816114, ECO:0000269\|PubMed:25901030, ECO:0000269\|PubMed:34606619, ECO:0000269\|PubMed:9388193, ECO:0000269\|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269\|PubMed:32690953}.
P54132	BLM	S1302	ochoa	RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein) (DNA 3'-5' helicase BLM) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3)	ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity). {ECO:0000250\|UniProtKB:O88700, ECO:0000269\|PubMed:12019152, ECO:0000269\|PubMed:18426915, ECO:0000269\|PubMed:20639533, ECO:0000269\|PubMed:21325134, ECO:0000269\|PubMed:23509288, ECO:0000269\|PubMed:24257077, ECO:0000269\|PubMed:24816114, ECO:0000269\|PubMed:25901030, ECO:0000269\|PubMed:34606619, ECO:0000269\|PubMed:9388193, ECO:0000269\|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269\|PubMed:32690953}.
P54198	HIRA	S549	ochoa	Protein HIRA (TUP1-like enhancer of split protein 1)	Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269\|PubMed:12370293, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527}.
P54198	HIRA	S557	ochoa	Protein HIRA (TUP1-like enhancer of split protein 1)	Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269\|PubMed:12370293, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527}.
P54259	ATN1	S107	ochoa	Atrophin-1 (Dentatorubral-pallidoluysian atrophy protein)	Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats. {ECO:0000250\|UniProtKB:O35126, ECO:0000269\|PubMed:10085113, ECO:0000269\|PubMed:10973986}.
P54725	RAD23A	S144	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P54725	RAD23A	S146	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P54727	RAD23B	S166	ochoa	UV excision repair protein RAD23 homolog B (HR23B) (hHR23B) (XP-C repair-complementing complex 58 kDa protein) (p58)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
P54727	RAD23B	S172	ochoa	UV excision repair protein RAD23 homolog B (HR23B) (hHR23B) (XP-C repair-complementing complex 58 kDa protein) (p58)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
P54760	EPHB4	S776	ochoa	Ephrin type-B receptor 4 (EC 2.7.10.1) (Hepatoma transmembrane kinase) (Tyrosine-protein kinase TYRO11)	Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. {ECO:0000269\|PubMed:12734395, ECO:0000269\|PubMed:16424904, ECO:0000269\|PubMed:27400125, ECO:0000269\|PubMed:30578106}.
P55196	AFDN	S557	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55196	AFDN	S1315	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55196	AFDN	S1317	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55197	MLLT10	S370	ochoa	Protein AF-10 (ALL1-fused gene from chromosome 10 protein)	Probably involved in transcriptional regulation. In vitro or as fusion protein with KMT2A/MLL1 has transactivation activity. Binds to cruciform DNA. In cells, binding to unmodified histone H3 regulates DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2) and gene activation (PubMed:26439302). {ECO:0000269\|PubMed:17868029, ECO:0000269\|PubMed:26439302}.
P55197	MLLT10	S686	ochoa	Protein AF-10 (ALL1-fused gene from chromosome 10 protein)	Probably involved in transcriptional regulation. In vitro or as fusion protein with KMT2A/MLL1 has transactivation activity. Binds to cruciform DNA. In cells, binding to unmodified histone H3 regulates DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2) and gene activation (PubMed:26439302). {ECO:0000269\|PubMed:17868029, ECO:0000269\|PubMed:26439302}.
P55198	MLLT6	S435	ochoa	Protein AF-17 (ALL1-fused gene from chromosome 17 protein)	None
P55201	BRPF1	S866	ochoa	Peregrin (Bromodomain and PHD finger-containing protein 1) (Protein Br140)	Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (PubMed:16387653, PubMed:24065767, PubMed:27939640). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (PubMed:24065767). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation (PubMed:27939640). Positively regulates the transcription of RUNX1 and RUNX2 (PubMed:18794358). {ECO:0000269\|PubMed:16387653, ECO:0000269\|PubMed:18794358, ECO:0000269\|PubMed:24065767, ECO:0000269\|PubMed:27939640}.
P55265	ADAR	S611	ochoa	Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)	Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:12618436, PubMed:7565688, PubMed:7972084). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269\|PubMed:12618436, ECO:0000269\|PubMed:15556947, ECO:0000269\|PubMed:15858013, ECO:0000269\|PubMed:16120648, ECO:0000269\|PubMed:16475990, ECO:0000269\|PubMed:17079286, ECO:0000269\|PubMed:19605474, ECO:0000269\|PubMed:19651874, ECO:0000269\|PubMed:19710021, ECO:0000269\|PubMed:19908260, ECO:0000269\|PubMed:21289159, ECO:0000269\|PubMed:22278222, ECO:0000269\|PubMed:7565688, ECO:0000269\|PubMed:7972084}.
P55265	ADAR	S614	ochoa	Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)	Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:12618436, PubMed:7565688, PubMed:7972084). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269\|PubMed:12618436, ECO:0000269\|PubMed:15556947, ECO:0000269\|PubMed:15858013, ECO:0000269\|PubMed:16120648, ECO:0000269\|PubMed:16475990, ECO:0000269\|PubMed:17079286, ECO:0000269\|PubMed:19605474, ECO:0000269\|PubMed:19651874, ECO:0000269\|PubMed:19710021, ECO:0000269\|PubMed:19908260, ECO:0000269\|PubMed:21289159, ECO:0000269\|PubMed:22278222, ECO:0000269\|PubMed:7565688, ECO:0000269\|PubMed:7972084}.
P55317	FOXA1	S304	ochoa	Hepatocyte nuclear factor 3-alpha (HNF-3-alpha) (HNF-3A) (Forkhead box protein A1) (Transcription factor 3A) (TCF-3A)	Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promoter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis. {ECO:0000250, ECO:0000269\|PubMed:16087863, ECO:0000269\|PubMed:16331276, ECO:0000269\|PubMed:18358809, ECO:0000269\|PubMed:19127412, ECO:0000269\|PubMed:19917725}.
P55347	PKNOX1	S47	ochoa	Homeobox protein PKNOX1 (Homeobox protein PREP-1) (PBX/knotted homeobox 1)	Activates transcription in the presence of PBX1A and HOXA1. {ECO:0000250\|UniProtKB:O70477}.
P56524	HDAC4	S215	ochoa	Histone deacetylase 4 (HD4) (EC 3.5.1.98)	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256). {ECO:0000269\|PubMed:10523670, ECO:0000269\|PubMed:24413532, ECO:0000269\|PubMed:27708256}.
P56693	SOX10	S30	ochoa\|psp	Transcription factor SOX-10	Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (PubMed:21965087). Transcriptional activator of MBP, via binding to the gene promoter (By similarity). {ECO:0000250\|UniProtKB:O55170, ECO:0000250\|UniProtKB:Q04888, ECO:0000269\|PubMed:21965087}.
P56945	BCAR1	S437	ochoa	Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12432078, PubMed:12832404). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). {ECO:0000250\|UniProtKB:Q61140, ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:12832404, ECO:0000269\|PubMed:17038317}.
P56945	BCAR1	S645	ochoa	Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12432078, PubMed:12832404). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). {ECO:0000250\|UniProtKB:Q61140, ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:12832404, ECO:0000269\|PubMed:17038317}.
P57060	RWDD2B	S178	ochoa	RWD domain-containing protein 2B	None
P57078	RIPK4	S430	ochoa	Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-delta-interacting protein kinase)	Serine/threonine protein kinase (By similarity). Required for embryonic skin development and correct skin homeostasis in adults, via phosphorylation of PKP1 and subsequent promotion of keratinocyte differentiation and cell adhesion (By similarity). It is a direct transcriptional target of TP63 (PubMed:22197488). Plays a role in NF-kappa-B activation (PubMed:12446564). {ECO:0000250\|UniProtKB:Q9ERK0, ECO:0000269\|PubMed:12446564, ECO:0000269\|PubMed:22197488}.
P60709	ACTB	S239	ochoa	Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]	Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250\|UniProtKB:Q6QAQ1, ECO:0000269\|PubMed:25255767, ECO:0000269\|PubMed:29581253, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:38609661, ECO:0000269\|PubMed:39321809}.
P60709	ACTB	S344	ochoa	Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]	Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250\|UniProtKB:Q6QAQ1, ECO:0000269\|PubMed:25255767, ECO:0000269\|PubMed:29581253, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:38609661, ECO:0000269\|PubMed:39321809}.
P60709	ACTB	S350	ochoa	Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]	Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250\|UniProtKB:Q6QAQ1, ECO:0000269\|PubMed:25255767, ECO:0000269\|PubMed:29581253, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:38609661, ECO:0000269\|PubMed:39321809}.
P61073	CXCR4	S325	ochoa\|psp	C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (FB22) (Fusin) (HM89) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Lipopolysaccharide-associated protein 3) (LAP-3) (LPS-associated protein 3) (NPYRL) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)	Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:18799424, PubMed:24912431, PubMed:28978524). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). {ECO:0000250\|UniProtKB:P70658, ECO:0000269\|PubMed:10074102, ECO:0000269\|PubMed:10452968, ECO:0000269\|PubMed:10644702, ECO:0000269\|PubMed:10825158, ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:17197449, ECO:0000269\|PubMed:18799424, ECO:0000269\|PubMed:20048153, ECO:0000269\|PubMed:20228059, ECO:0000269\|PubMed:20505072, ECO:0000269\|PubMed:24912431, ECO:0000269\|PubMed:28978524, ECO:0000269\|PubMed:8752280, ECO:0000269\|PubMed:8752281}.; FUNCTION: (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:10074122, PubMed:10756055, PubMed:8849450, PubMed:8929542, PubMed:9427609). {ECO:0000269\|PubMed:10074122, ECO:0000269\|PubMed:10756055, ECO:0000269\|PubMed:8849450, ECO:0000269\|PubMed:8929542, ECO:0000269\|PubMed:9427609}.
P61073	CXCR4	S330	psp	C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (FB22) (Fusin) (HM89) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Lipopolysaccharide-associated protein 3) (LAP-3) (LPS-associated protein 3) (NPYRL) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)	Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:18799424, PubMed:24912431, PubMed:28978524). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). {ECO:0000250\|UniProtKB:P70658, ECO:0000269\|PubMed:10074102, ECO:0000269\|PubMed:10452968, ECO:0000269\|PubMed:10644702, ECO:0000269\|PubMed:10825158, ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:17197449, ECO:0000269\|PubMed:18799424, ECO:0000269\|PubMed:20048153, ECO:0000269\|PubMed:20228059, ECO:0000269\|PubMed:20505072, ECO:0000269\|PubMed:24912431, ECO:0000269\|PubMed:28978524, ECO:0000269\|PubMed:8752280, ECO:0000269\|PubMed:8752281}.; FUNCTION: (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:10074122, PubMed:10756055, PubMed:8849450, PubMed:8929542, PubMed:9427609). {ECO:0000269\|PubMed:10074122, ECO:0000269\|PubMed:10756055, ECO:0000269\|PubMed:8849450, ECO:0000269\|PubMed:8929542, ECO:0000269\|PubMed:9427609}.
P61978	HNRNPK	S81	ochoa	Heterogeneous nuclear ribonucleoprotein K (hnRNP K) (Transformation up-regulated nuclear protein) (TUNP)	One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). {ECO:0000250, ECO:0000269\|PubMed:16360036, ECO:0000269\|PubMed:20673990, ECO:0000269\|PubMed:22825850, ECO:0000269\|PubMed:33174841}.
P61978	HNRNPK	S127	ochoa	Heterogeneous nuclear ribonucleoprotein K (hnRNP K) (Transformation up-regulated nuclear protein) (TUNP)	One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). {ECO:0000250, ECO:0000269\|PubMed:16360036, ECO:0000269\|PubMed:20673990, ECO:0000269\|PubMed:22825850, ECO:0000269\|PubMed:33174841}.
P62736	ACTA2	S241	ochoa	Actin, aortic smooth muscle (EC 3.6.4.-) (Alpha-actin-2) (Cell growth-inhibiting gene 46 protein) [Cleaved into: Actin, aortic smooth muscle, intermediate form]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P62995	TRA2B	S22	ochoa	Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:9546399}.
P62995	TRA2B	S26	ochoa	Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:9546399}.
P63104	YWHAZ	S64	ochoa\|psp	14-3-3 protein zeta/delta (Protein kinase C inhibitor protein 1) (KCIP-1)	Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:14578935, PubMed:15071501, PubMed:15644438, PubMed:16376338, PubMed:16959763, PubMed:31024343, PubMed:9360956). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35662396). Binding generally results in the modulation of the activity of the binding partner (PubMed:35662396). Promotes cytosolic retention and inactivation of TFEB transcription factor by binding to phosphorylated TFEB (PubMed:35662396). Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (PubMed:16959763). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250\|UniProtKB:O55043, ECO:0000269\|PubMed:14578935, ECO:0000269\|PubMed:15071501, ECO:0000269\|PubMed:15644438, ECO:0000269\|PubMed:16376338, ECO:0000269\|PubMed:16959763, ECO:0000269\|PubMed:31024343, ECO:0000269\|PubMed:35662396, ECO:0000269\|PubMed:9360956}.
P63261	ACTG1	S239	ochoa	Actin, cytoplasmic 2 (EC 3.6.4.-) (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity). {ECO:0000250\|UniProtKB:P63260, ECO:0000305\|PubMed:29581253}.
P63261	ACTG1	S344	ochoa	Actin, cytoplasmic 2 (EC 3.6.4.-) (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity). {ECO:0000250\|UniProtKB:P63260, ECO:0000305\|PubMed:29581253}.
P63261	ACTG1	S350	ochoa	Actin, cytoplasmic 2 (EC 3.6.4.-) (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity). {ECO:0000250\|UniProtKB:P63260, ECO:0000305\|PubMed:29581253}.
P63267	ACTG2	S240	ochoa	Actin, gamma-enteric smooth muscle (EC 3.6.4.-) (Alpha-actin-3) (Gamma-2-actin) (Smooth muscle gamma-actin) [Cleaved into: Actin, gamma-enteric smooth muscle, intermediate form]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P68032	ACTC1	S241	ochoa	Actin, alpha cardiac muscle 1 (EC 3.6.4.-) (Alpha-cardiac actin) [Cleaved into: Actin, alpha cardiac muscle 1, intermediate form]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P68133	ACTA1	S241	ochoa	Actin, alpha skeletal muscle (EC 3.6.4.-) (Alpha-actin-1) [Cleaved into: Actin, alpha skeletal muscle, intermediate form]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P68363	TUBA1B	S54	ochoa	Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]	Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). {ECO:0000269\|PubMed:34996871, ECO:0000269\|PubMed:38305685, ECO:0000269\|PubMed:38609661}.
P78310	CXADR	S306	ochoa	Coxsackievirus and adenovirus receptor (CAR) (hCAR) (CVB3-binding protein) (Coxsackievirus B-adenovirus receptor) (HCVADR)	Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. {ECO:0000269\|PubMed:11734628, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:15800062, ECO:0000269\|PubMed:19064666, ECO:0000269\|PubMed:9096397}.; FUNCTION: (Microbial infection) Acts as a receptor for adenovirus type C. {ECO:0000269\|PubMed:10567268, ECO:0000269\|PubMed:10666333, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:9733828}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus B1 to B6. {ECO:0000269\|PubMed:10814575, ECO:0000269\|PubMed:14978041}.
P78310	CXADR	S314	ochoa	Coxsackievirus and adenovirus receptor (CAR) (hCAR) (CVB3-binding protein) (Coxsackievirus B-adenovirus receptor) (HCVADR)	Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. {ECO:0000269\|PubMed:11734628, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:15800062, ECO:0000269\|PubMed:19064666, ECO:0000269\|PubMed:9096397}.; FUNCTION: (Microbial infection) Acts as a receptor for adenovirus type C. {ECO:0000269\|PubMed:10567268, ECO:0000269\|PubMed:10666333, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:9733828}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus B1 to B6. {ECO:0000269\|PubMed:10814575, ECO:0000269\|PubMed:14978041}.
P78317	RNF4	S101	ochoa	E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Small nuclear ring finger protein) (Protein SNURF)	E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:18408734, PubMed:19307308, PubMed:35013556). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:18408734, PubMed:19307308, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (PubMed:20212317). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (PubMed:19779455, PubMed:20026589). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (PubMed:12885770). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (PubMed:35013556). {ECO:0000269\|PubMed:12885770, ECO:0000269\|PubMed:18408734, ECO:0000269\|PubMed:19307308, ECO:0000269\|PubMed:19779455, ECO:0000269\|PubMed:20026589, ECO:0000269\|PubMed:20212317, ECO:0000269\|PubMed:20943951, ECO:0000269\|PubMed:35013556}.
P78504	JAG1	S1107	ochoa	Protein jagged-1 (Jagged1) (hJ1) (CD antigen CD339)	Ligand for multiple Notch receptors and involved in the mediation of Notch signaling (PubMed:18660822, PubMed:20437614). May be involved in cell-fate decisions during hematopoiesis (PubMed:9462510). Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation (By similarity). Enhances fibroblast growth factor-induced angiogenesis (in vitro). {ECO:0000250, ECO:0000269\|PubMed:18660822, ECO:0000269\|PubMed:20437614, ECO:0000269\|PubMed:9462510}.
P78524	DENND2B	S545	ochoa	DENN domain-containing protein 2B (HeLa tumor suppression 1) (Suppression of tumorigenicity 5 protein)	[Isoform 1]: May be involved in cytoskeletal organization and tumorogenicity. Seems to be involved in a signaling transduction pathway leading to activation of MAPK1/ERK2. Plays a role in EGFR trafficking from recycling endosomes back to the cell membrane (PubMed:29030480). {ECO:0000269\|PubMed:29030480, ECO:0000269\|PubMed:9632734}.; FUNCTION: [Isoform 2]: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269\|PubMed:20937701}.; FUNCTION: [Isoform 3]: May block ERK2 activation stimulated by ABL1 (Probable). May alter cell morphology and cell growth (Probable). {ECO:0000305\|PubMed:10229203, ECO:0000305\|PubMed:9632734}.
P78527	PRKDC	S2029	psp	DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (DNPK1) (Ser-473 kinase) (S473K) (p460)	Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326, PubMed:33854234). Acts as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:10026262, PubMed:10467406, PubMed:11889123, PubMed:12509254, PubMed:14599745, PubMed:14612514, PubMed:14704337, PubMed:15177042, PubMed:1597196, PubMed:16397295, PubMed:18644470, PubMed:2247066, PubMed:2507541, PubMed:26237645, PubMed:26666690, PubMed:28712728, PubMed:29478807, PubMed:30247612, PubMed:8407951, PubMed:8464713, PubMed:9139719, PubMed:9362500). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of 'Ser-473' of protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), promoting their activation (PubMed:15262962). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603). {ECO:0000250\|UniProtKB:P97313, ECO:0000269\|PubMed:10026262, ECO:0000269\|PubMed:10467406, ECO:0000269\|PubMed:11889123, ECO:0000269\|PubMed:11955432, ECO:0000269\|PubMed:12509254, ECO:0000269\|PubMed:12649176, ECO:0000269\|PubMed:14599745, ECO:0000269\|PubMed:14612514, ECO:0000269\|PubMed:14627815, ECO:0000269\|PubMed:14704337, ECO:0000269\|PubMed:14734805, ECO:0000269\|PubMed:15177042, ECO:0000269\|PubMed:15262962, ECO:0000269\|PubMed:15574326, ECO:0000269\|PubMed:1597196, ECO:0000269\|PubMed:16046194, ECO:0000269\|PubMed:16397295, ECO:0000269\|PubMed:18644470, ECO:0000269\|PubMed:2247066, ECO:0000269\|PubMed:2507541, ECO:0000269\|PubMed:26237645, ECO:0000269\|PubMed:26666690, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:29478807, ECO:0000269\|PubMed:30247612, ECO:0000269\|PubMed:32103174, ECO:0000269\|PubMed:33273464, ECO:0000269\|PubMed:33854234, ECO:0000269\|PubMed:34352203, ECO:0000269\|PubMed:35460603, ECO:0000269\|PubMed:8407951, ECO:0000269\|PubMed:8464713, ECO:0000269\|PubMed:9139719, ECO:0000269\|PubMed:9362500, ECO:0000269\|PubMed:9363941, ECO:0000269\|PubMed:9679063}.
P78527	PRKDC	S3021	ochoa	DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (DNPK1) (Ser-473 kinase) (S473K) (p460)	Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326, PubMed:33854234). Acts as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:15574326). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:10026262, PubMed:10467406, PubMed:11889123, PubMed:12509254, PubMed:14599745, PubMed:14612514, PubMed:14704337, PubMed:15177042, PubMed:1597196, PubMed:16397295, PubMed:18644470, PubMed:2247066, PubMed:2507541, PubMed:26237645, PubMed:26666690, PubMed:28712728, PubMed:29478807, PubMed:30247612, PubMed:8407951, PubMed:8464713, PubMed:9139719, PubMed:9362500). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of 'Ser-473' of protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), promoting their activation (PubMed:15262962). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603). {ECO:0000250\|UniProtKB:P97313, ECO:0000269\|PubMed:10026262, ECO:0000269\|PubMed:10467406, ECO:0000269\|PubMed:11889123, ECO:0000269\|PubMed:11955432, ECO:0000269\|PubMed:12509254, ECO:0000269\|PubMed:12649176, ECO:0000269\|PubMed:14599745, ECO:0000269\|PubMed:14612514, ECO:0000269\|PubMed:14627815, ECO:0000269\|PubMed:14704337, ECO:0000269\|PubMed:14734805, ECO:0000269\|PubMed:15177042, ECO:0000269\|PubMed:15262962, ECO:0000269\|PubMed:15574326, ECO:0000269\|PubMed:1597196, ECO:0000269\|PubMed:16046194, ECO:0000269\|PubMed:16397295, ECO:0000269\|PubMed:18644470, ECO:0000269\|PubMed:2247066, ECO:0000269\|PubMed:2507541, ECO:0000269\|PubMed:26237645, ECO:0000269\|PubMed:26666690, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:29478807, ECO:0000269\|PubMed:30247612, ECO:0000269\|PubMed:32103174, ECO:0000269\|PubMed:33273464, ECO:0000269\|PubMed:33854234, ECO:0000269\|PubMed:34352203, ECO:0000269\|PubMed:35460603, ECO:0000269\|PubMed:8407951, ECO:0000269\|PubMed:8464713, ECO:0000269\|PubMed:9139719, ECO:0000269\|PubMed:9362500, ECO:0000269\|PubMed:9363941, ECO:0000269\|PubMed:9679063}.
P78559	MAP1A	S1152	ochoa	Microtubule-associated protein 1A (MAP-1A) (Proliferation-related protein p80) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]	Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
P78559	MAP1A	S1196	ochoa	Microtubule-associated protein 1A (MAP-1A) (Proliferation-related protein p80) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]	Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
P78559	MAP1A	S1209	ochoa	Microtubule-associated protein 1A (MAP-1A) (Proliferation-related protein p80) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]	Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
P80723	BASP1	S183	ochoa	Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein) (Neuronal axonal membrane protein NAP-22)	None
P82094	TMF1	S336	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P82094	TMF1	S344	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P82094	TMF1	S933	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P82979	SARNP	S168	ochoa	SAP domain-containing ribonucleoprotein (Cytokine-induced protein of 29 kDa) (Nuclear protein Hcc-1) (Proliferation-associated cytokine-inducible protein CIP29)	Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15338056, PubMed:17196963, PubMed:20844015). The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15338056, PubMed:17196963, PubMed:20844015). Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). {ECO:0000269\|PubMed:15338056, ECO:0000269\|PubMed:17196963, ECO:0000269\|PubMed:20844015, ECO:0000269\|PubMed:37578863}.
P85037	FOXK1	S249	ochoa	Forkhead box protein K1 (Myocyte nuclear factor) (MNF)	Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis, muscle cell differentiation and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (PubMed:17670796). Together with FOXK2, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity). Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity). Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity). Involved in mTORC1-mediated metabolic reprogramming: in response to mTORC1 signaling, translocates into the nucleus and regulates the expression of genes associated with glycolysis and downstream anabolic pathways, such as HIF1A, thereby regulating glucose metabolism (By similarity). Together with FOXK2, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). Acts as a transcriptional regulator of the myogenic progenitor cell population in skeletal muscle (By similarity). Binds to the upstream enhancer region (CCAC box) of myoglobin (MB) gene, regulating the myogenic progenitor cell population (By similarity). Promotes muscle progenitor cell proliferation by repressing the transcriptional activity of FOXO4, thereby inhibiting myogenic differentiation (By similarity). Involved in remodeling processes of adult muscles that occur in response to physiological stimuli (By similarity). Required to correct temporal orchestration of molecular and cellular events necessary for muscle repair (By similarity). Represses myogenic differentiation by inhibiting MEFC activity (By similarity). Positively regulates Wnt/beta-catenin signaling by translocating DVL into the nucleus (PubMed:25805136). Reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression (PubMed:25852164). Accessory component of the polycomb repressive deubiquitinase (PR-DUB) complex; recruits the PR-DUB complex to specific FOXK1-bound genes (PubMed:24634419, PubMed:30664650). {ECO:0000250\|UniProtKB:P42128, ECO:0000269\|PubMed:17670796, ECO:0000269\|PubMed:24634419, ECO:0000269\|PubMed:25805136, ECO:0000269\|PubMed:25852164, ECO:0000269\|PubMed:30664650}.
P85299	PRR5	S288	ochoa	Proline-rich protein 5 (Protein observed with Rictor-1) (Protor-1)	Associated subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals (PubMed:17461779, PubMed:17599906, PubMed:29424687). mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive (PubMed:17461779, PubMed:17599906, PubMed:29424687). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:17461779, PubMed:17599906, PubMed:29424687). PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling (PubMed:17599906). May act as a tumor suppressor in breast cancer (PubMed:15718101). {ECO:0000269\|PubMed:15718101, ECO:0000269\|PubMed:17461779, ECO:0000269\|PubMed:17599906, ECO:0000269\|PubMed:29424687}.
P98082	DAB2	S332	ochoa	Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)	Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269\|PubMed:11387212, ECO:0000269\|PubMed:12805222, ECO:0000269\|PubMed:16267015, ECO:0000269\|PubMed:16984970, ECO:0000269\|PubMed:19306879, ECO:0000269\|PubMed:21995445, ECO:0000269\|PubMed:22323290, ECO:0000269\|PubMed:22491013}.
P98082	DAB2	S407	ochoa	Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)	Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269\|PubMed:11387212, ECO:0000269\|PubMed:12805222, ECO:0000269\|PubMed:16267015, ECO:0000269\|PubMed:16984970, ECO:0000269\|PubMed:19306879, ECO:0000269\|PubMed:21995445, ECO:0000269\|PubMed:22323290, ECO:0000269\|PubMed:22491013}.
P98082	DAB2	S729	ochoa	Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)	Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269\|PubMed:11387212, ECO:0000269\|PubMed:12805222, ECO:0000269\|PubMed:16267015, ECO:0000269\|PubMed:16984970, ECO:0000269\|PubMed:19306879, ECO:0000269\|PubMed:21995445, ECO:0000269\|PubMed:22323290, ECO:0000269\|PubMed:22491013}.
P98172	EFNB1	S287	ochoa	Ephrin-B1 (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)]	Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:7973638, PubMed:8070404). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:7973638, PubMed:8070404). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:7973638, PubMed:8070404). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity). {ECO:0000250\|UniProtKB:P52795, ECO:0000269\|PubMed:7973638, ECO:0000269\|PubMed:8070404}.
P98177	FOXO4	S268	psp	Forkhead box protein O4 (Fork head domain transcription factor AFX1)	Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269\|PubMed:10217147, ECO:0000269\|PubMed:10783894, ECO:0000269\|PubMed:12761217, ECO:0000269\|PubMed:15126506, ECO:0000269\|PubMed:16054032, ECO:0000269\|PubMed:16964248, ECO:0000269\|PubMed:20874444, ECO:0000269\|PubMed:22972301}.
P98198	ATP8B2	S1175	ochoa	Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2)	Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. May contribute to the maintenance of membrane lipid asymmetry. {ECO:0000269\|PubMed:25315773}.
P98198	ATP8B2	S1187	ochoa	Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2)	Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. May contribute to the maintenance of membrane lipid asymmetry. {ECO:0000269\|PubMed:25315773}.
Q00403	GTF2B	S76	ochoa	Transcription initiation factor IIB (EC 2.3.1.48) (General transcription factor TFIIB) (S300-II)	General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA (PubMed:12931194, PubMed:1517211, PubMed:1876184, PubMed:1946368, PubMed:27193682, PubMed:3029109, PubMed:3818643, PubMed:7601352, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:9420329). Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex (PubMed:8413225, PubMed:8504927, PubMed:8515820, PubMed:8516311, PubMed:8516312). Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle (PubMed:7601352). Associates with chromatin to core promoter-specific regions (PubMed:12931194, PubMed:24441171). Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element (PubMed:10619841, PubMed:16230532, PubMed:7675079, PubMed:9420329). Modulates transcription start site selection (PubMed:10318856). Also exhibits autoacetyltransferase activity that contributes to the activated transcription (PubMed:12931194). {ECO:0000269\|PubMed:10318856, ECO:0000269\|PubMed:10619841, ECO:0000269\|PubMed:12931194, ECO:0000269\|PubMed:1517211, ECO:0000269\|PubMed:16230532, ECO:0000269\|PubMed:1876184, ECO:0000269\|PubMed:1946368, ECO:0000269\|PubMed:24441171, ECO:0000269\|PubMed:27193682, ECO:0000269\|PubMed:3029109, ECO:0000269\|PubMed:3818643, ECO:0000269\|PubMed:7601352, ECO:0000269\|PubMed:7675079, ECO:0000269\|PubMed:8413225, ECO:0000269\|PubMed:8504927, ECO:0000269\|PubMed:8515820, ECO:0000269\|PubMed:8516311, ECO:0000269\|PubMed:8516312, ECO:0000269\|PubMed:9420329}.
Q00536	CDK16	S95	ochoa\|psp	Cyclin-dependent kinase 16 (EC 2.7.11.22) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1)	Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250, ECO:0000269\|PubMed:22184064, ECO:0000269\|PubMed:22796189, ECO:0000269\|PubMed:22798068}.
Q00587	CDC42EP1	S25	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q00587	CDC42EP1	S71	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q00587	CDC42EP1	S77	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q00587	CDC42EP1	S152	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q00587	CDC42EP1	S153	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q00613	HSF1	S320	ochoa\|psp	Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)	Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). {ECO:0000269\|PubMed:10359787, ECO:0000269\|PubMed:11447121, ECO:0000269\|PubMed:11583998, ECO:0000269\|PubMed:12659875, ECO:0000269\|PubMed:12917326, ECO:0000269\|PubMed:14707147, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:16278218, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18451878, ECO:0000269\|PubMed:1871105, ECO:0000269\|PubMed:18794143, ECO:0000269\|PubMed:1986252, ECO:0000269\|PubMed:25963659, ECO:0000269\|PubMed:26359349, ECO:0000269\|PubMed:26727489, ECO:0000269\|PubMed:26754925, ECO:0000269\|PubMed:34723967, ECO:0000269\|PubMed:7623826, ECO:0000269\|PubMed:7760831, ECO:0000269\|PubMed:7935471, ECO:0000269\|PubMed:8455624, ECO:0000269\|PubMed:8940068, ECO:0000269\|PubMed:8946918, ECO:0000269\|PubMed:9121459, ECO:0000269\|PubMed:9341107, ECO:0000269\|PubMed:9499401, ECO:0000269\|PubMed:9535852, ECO:0000269\|PubMed:9727490}.; FUNCTION: (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {ECO:0000269\|PubMed:27189267}.
Q00613	HSF1	S326	ochoa\|psp	Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)	Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). {ECO:0000269\|PubMed:10359787, ECO:0000269\|PubMed:11447121, ECO:0000269\|PubMed:11583998, ECO:0000269\|PubMed:12659875, ECO:0000269\|PubMed:12917326, ECO:0000269\|PubMed:14707147, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:16278218, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18451878, ECO:0000269\|PubMed:1871105, ECO:0000269\|PubMed:18794143, ECO:0000269\|PubMed:1986252, ECO:0000269\|PubMed:25963659, ECO:0000269\|PubMed:26359349, ECO:0000269\|PubMed:26727489, ECO:0000269\|PubMed:26754925, ECO:0000269\|PubMed:34723967, ECO:0000269\|PubMed:7623826, ECO:0000269\|PubMed:7760831, ECO:0000269\|PubMed:7935471, ECO:0000269\|PubMed:8455624, ECO:0000269\|PubMed:8940068, ECO:0000269\|PubMed:8946918, ECO:0000269\|PubMed:9121459, ECO:0000269\|PubMed:9341107, ECO:0000269\|PubMed:9499401, ECO:0000269\|PubMed:9535852, ECO:0000269\|PubMed:9727490}.; FUNCTION: (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {ECO:0000269\|PubMed:27189267}.
Q00613	HSF1	S344	ochoa\|psp	Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)	Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). {ECO:0000269\|PubMed:10359787, ECO:0000269\|PubMed:11447121, ECO:0000269\|PubMed:11583998, ECO:0000269\|PubMed:12659875, ECO:0000269\|PubMed:12917326, ECO:0000269\|PubMed:14707147, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:16278218, ECO:0000269\|PubMed:17897941, ECO:0000269\|PubMed:18451878, ECO:0000269\|PubMed:1871105, ECO:0000269\|PubMed:18794143, ECO:0000269\|PubMed:1986252, ECO:0000269\|PubMed:25963659, ECO:0000269\|PubMed:26359349, ECO:0000269\|PubMed:26727489, ECO:0000269\|PubMed:26754925, ECO:0000269\|PubMed:34723967, ECO:0000269\|PubMed:7623826, ECO:0000269\|PubMed:7760831, ECO:0000269\|PubMed:7935471, ECO:0000269\|PubMed:8455624, ECO:0000269\|PubMed:8940068, ECO:0000269\|PubMed:8946918, ECO:0000269\|PubMed:9121459, ECO:0000269\|PubMed:9341107, ECO:0000269\|PubMed:9499401, ECO:0000269\|PubMed:9535852, ECO:0000269\|PubMed:9727490}.; FUNCTION: (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {ECO:0000269\|PubMed:27189267}.
Q00653	NFKB2	S713	psp	Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. {ECO:0000269\|PubMed:7925301}.
Q00653	NFKB2	S717	psp	Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. {ECO:0000269\|PubMed:7925301}.
Q01082	SPTBN1	S2128	ochoa	Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin) (Fodrin beta chain) (Spectrin, non-erythroid beta chain 1)	Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function. {ECO:0000269\|PubMed:34211179}.
Q01082	SPTBN1	S2314	ochoa	Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin) (Fodrin beta chain) (Spectrin, non-erythroid beta chain 1)	Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function. {ECO:0000269\|PubMed:34211179}.
Q01167	FOXK2	S205	ochoa	Forkhead box protein K2 (G/T-mismatch specific binding protein) (nGTBP) (Interleukin enhancer-binding factor 1)	Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (PubMed:22083952, PubMed:25451922). Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity). Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity). Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity). Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription (PubMed:22083952). Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence (PubMed:20097901). Binds to NFAT-like motifs (purine-rich) in the IL2 promoter (PubMed:1339390). Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus (PubMed:25805136). Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements (PubMed:1909027). Accessory component of the polycomb repressive deubiquitinase (PR-DUB) complex; recruits the PR-DUB complex to specific FOXK2-bound genes (PubMed:24634419, PubMed:30664650). {ECO:0000250\|UniProtKB:Q3UCQ1, ECO:0000269\|PubMed:1339390, ECO:0000269\|PubMed:1909027, ECO:0000269\|PubMed:20097901, ECO:0000269\|PubMed:22083952, ECO:0000269\|PubMed:24634419, ECO:0000269\|PubMed:25451922, ECO:0000269\|PubMed:25805136, ECO:0000269\|PubMed:30664650}.
Q01484	ANK2	S904	ochoa	Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) (Non-erythroid ankyrin)	Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:12571597). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity). {ECO:0000250\|UniProtKB:Q8C8R3, ECO:0000269\|PubMed:12571597}.
Q01831	XPC	S507	ochoa	DNA repair protein complementing XP-C cells (Xeroderma pigmentosum group C-complementing protein) (p125)	Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19609301, PubMed:19941824, PubMed:20028083, PubMed:20649465, PubMed:20798892, PubMed:9734359). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083). {ECO:0000269\|PubMed:10734143, ECO:0000269\|PubMed:10873465, ECO:0000269\|PubMed:12509299, ECO:0000269\|PubMed:12547395, ECO:0000269\|PubMed:19609301, ECO:0000269\|PubMed:19941824, ECO:0000269\|PubMed:20028083, ECO:0000269\|PubMed:20649465, ECO:0000269\|PubMed:20798892, ECO:0000269\|PubMed:9734359}.; FUNCTION: In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT) (PubMed:29973595, PubMed:31527837). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes (PubMed:31527837). {ECO:0000269\|PubMed:29973595, ECO:0000269\|PubMed:31527837}.
Q01974	ROR2	S870	ochoa	Tyrosine-protein kinase transmembrane receptor ROR2 (EC 2.7.10.1) (Neurotrophic tyrosine kinase, receptor-related 2)	Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation (PubMed:17717073). In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443). {ECO:0000250\|UniProtKB:Q9Z138, ECO:0000269\|PubMed:17717073, ECO:0000269\|PubMed:25029443}.
Q02241	KIF23	S692	ochoa	Kinesin-like protein KIF23 (Kinesin-like protein 5) (Mitotic kinesin-like protein 1)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. {ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:22522702, ECO:0000269\|PubMed:23570799}.
Q02446	SP4	S46	ochoa	Transcription factor Sp4 (SPR-1)	Binds to GT and GC boxes promoters elements. Probable transcriptional activator.
Q02446	SP4	S130	ochoa	Transcription factor Sp4 (SPR-1)	Binds to GT and GC boxes promoters elements. Probable transcriptional activator.
Q02446	SP4	S134	ochoa	Transcription factor Sp4 (SPR-1)	Binds to GT and GC boxes promoters elements. Probable transcriptional activator.
Q02750	MAP2K1	S218	ochoa\|psp	Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (MKK1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. {ECO:0000269\|PubMed:14737111, ECO:0000269\|PubMed:17101779, ECO:0000269\|PubMed:29433126}.
Q02952	AKAP12	S651	ochoa	A-kinase anchor protein 12 (AKAP-12) (A-kinase anchor protein 250 kDa) (AKAP 250) (Gravin) (Myasthenia gravis autoantigen)	Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Q02952	AKAP12	S749	ochoa	A-kinase anchor protein 12 (AKAP-12) (A-kinase anchor protein 250 kDa) (AKAP 250) (Gravin) (Myasthenia gravis autoantigen)	Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Q03001	DST	S7422	ochoa	Dystonin (230 kDa bullous pemphigoid antigen) (230/240 kDa bullous pemphigoid antigen) (Bullous pemphigoid antigen 1) (BPA) (Bullous pemphigoid antigen) (Dystonia musculorum protein) (Hemidesmosomal plaque protein)	Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity). {ECO:0000250\|UniProtKB:Q91ZU6}.; FUNCTION: [Isoform 3]: Plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; FUNCTION: [Isoform 6]: Required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269\|PubMed:10428034, ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:19403692}.; FUNCTION: [Isoform 7]: Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.
Q03060	CREM	S277	psp	cAMP-responsive element modulator (Inducible cAMP early repressor) (ICER)	Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Plays a role in spermatogenesis and is involved in spermatid maturation (PubMed:10373550). {ECO:0000269\|PubMed:10373550}.; FUNCTION: [Isoform 6]: May play a role in the regulation of the circadian clock: acts as a transcriptional repressor of the core circadian component PER1 by directly binding to cAMP response elements in its promoter. {ECO:0000250}.
Q03111	MLLT1	S325	ochoa	Protein ENL (YEATS domain-containing protein 1)	Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948). Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated (PubMed:27105114). Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20) (PubMed:27105114). {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:27105114}.; FUNCTION: Acts as a key chromatin reader in acute myeloid leukemia by recognizing and binding to acetylated histones via its YEATS domain, thereby regulating oncogenic gene transcription. {ECO:0000269\|PubMed:28241139, ECO:0000269\|PubMed:28241141}.
Q03164	KMT2A	S187	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S197	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S487	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S2872	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S3521	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03188	CENPC	S176	ochoa	Centromere protein C (CENP-C) (Centromere autoantigen C) (Centromere protein C 1) (CENP-C 1) (Interphase centromere complex protein 7)	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269\|PubMed:19482874, ECO:0000269\|PubMed:21529714}.
Q03252	LMNB2	S415	ochoa	Lamin-B2	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:33033404). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:33033404). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:33033404). {ECO:0000269\|PubMed:33033404}.
Q03252	LMNB2	S426	ochoa	Lamin-B2	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:33033404). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:33033404). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:33033404). {ECO:0000269\|PubMed:33033404}.
Q03252	LMNB2	S559	ochoa	Lamin-B2	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:33033404). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:33033404). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:33033404). {ECO:0000269\|PubMed:33033404}.
Q04637	EIF4G1	S204	ochoa	Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220)	Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). {ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29987188}.
Q04637	EIF4G1	S1098	ochoa	Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220)	Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). {ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29987188}.
Q04656	ATP7A	S1430	ochoa	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S1466	ochoa\|psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S1469	ochoa\|psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04725	TLE2	S313	ochoa	Transducin-like enhancer protein 2 (Enhancer of split groucho-like protein 2) (ESG2)	Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250}.
Q04726	TLE3	S203	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04726	TLE3	S211	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04726	TLE3	S292	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04726	TLE3	S295	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04726	TLE3	S299	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04727	TLE4	S301	ochoa	Transducin-like enhancer protein 4 (Grg-4) (Groucho-related protein 4)	Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Essential for the transcriptional repressor activity of SIX3 during retina and lens development and for SIX3 transcriptional auto-repression (By similarity). Involved in transcriptional repression of GNRHR and enhances MSX1-mediated transcriptional repression of CGA/alpha-GSU (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:Q62441}.
Q05397	PTK2	S580	ochoa	Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)	Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:10655584, ECO:0000269\|PubMed:11331870, ECO:0000269\|PubMed:11980671, ECO:0000269\|PubMed:15166238, ECO:0000269\|PubMed:15561106, ECO:0000269\|PubMed:15895076, ECO:0000269\|PubMed:16919435, ECO:0000269\|PubMed:16927379, ECO:0000269\|PubMed:17395594, ECO:0000269\|PubMed:17431114, ECO:0000269\|PubMed:17968709, ECO:0000269\|PubMed:18006843, ECO:0000269\|PubMed:18206965, ECO:0000269\|PubMed:18256281, ECO:0000269\|PubMed:18292575, ECO:0000269\|PubMed:18497331, ECO:0000269\|PubMed:18677107, ECO:0000269\|PubMed:19138410, ECO:0000269\|PubMed:19147981, ECO:0000269\|PubMed:19224453, ECO:0000269\|PubMed:20332118, ECO:0000269\|PubMed:20495381, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:9360983}.; FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:20109444}.
Q05397	PTK2	S708	ochoa	Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)	Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:10655584, ECO:0000269\|PubMed:11331870, ECO:0000269\|PubMed:11980671, ECO:0000269\|PubMed:15166238, ECO:0000269\|PubMed:15561106, ECO:0000269\|PubMed:15895076, ECO:0000269\|PubMed:16919435, ECO:0000269\|PubMed:16927379, ECO:0000269\|PubMed:17395594, ECO:0000269\|PubMed:17431114, ECO:0000269\|PubMed:17968709, ECO:0000269\|PubMed:18006843, ECO:0000269\|PubMed:18206965, ECO:0000269\|PubMed:18256281, ECO:0000269\|PubMed:18292575, ECO:0000269\|PubMed:18497331, ECO:0000269\|PubMed:18677107, ECO:0000269\|PubMed:19138410, ECO:0000269\|PubMed:19147981, ECO:0000269\|PubMed:19224453, ECO:0000269\|PubMed:20332118, ECO:0000269\|PubMed:20495381, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:9360983}.; FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:20109444}.
Q05397	PTK2	S893	ochoa	Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)	Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:10655584, ECO:0000269\|PubMed:11331870, ECO:0000269\|PubMed:11980671, ECO:0000269\|PubMed:15166238, ECO:0000269\|PubMed:15561106, ECO:0000269\|PubMed:15895076, ECO:0000269\|PubMed:16919435, ECO:0000269\|PubMed:16927379, ECO:0000269\|PubMed:17395594, ECO:0000269\|PubMed:17431114, ECO:0000269\|PubMed:17968709, ECO:0000269\|PubMed:18006843, ECO:0000269\|PubMed:18206965, ECO:0000269\|PubMed:18256281, ECO:0000269\|PubMed:18292575, ECO:0000269\|PubMed:18497331, ECO:0000269\|PubMed:18677107, ECO:0000269\|PubMed:19138410, ECO:0000269\|PubMed:19147981, ECO:0000269\|PubMed:19224453, ECO:0000269\|PubMed:20332118, ECO:0000269\|PubMed:20495381, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:9360983}.; FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269\|PubMed:20109444}.
Q06413	MEF2C	S228	ochoa	Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C)	Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). Isoforms that lack the repressor domain are more active than isoform 1. {ECO:0000250\|UniProtKB:Q8CFN5, ECO:0000269\|PubMed:11904443, ECO:0000269\|PubMed:15340086, ECO:0000269\|PubMed:15831463, ECO:0000269\|PubMed:15834131, ECO:0000269\|PubMed:9069290, ECO:0000269\|PubMed:9384584}.
Q06455	RUNX1T1	S417	ochoa	Protein CBFA2T1 (Cyclin-D-related protein) (Eight twenty one protein) (Protein ETO) (Protein MTG8) (Zinc finger MYND domain-containing protein 2)	Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:10688654, PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). Can repress transactivation mediated by TCF12 (PubMed:16803958). Acts as a negative regulator of adipogenesis (By similarity). The AML1-MTG8/ETO fusion protein frequently found in leukemic cells is involved in leukemogenesis and contributes to hematopoietic stem/progenitor cell self-renewal (PubMed:23812588). {ECO:0000250\|UniProtKB:Q61909, ECO:0000269\|PubMed:10688654, ECO:0000269\|PubMed:10973986, ECO:0000269\|PubMed:16803958, ECO:0000269\|PubMed:23251453, ECO:0000269\|PubMed:23812588, ECO:0000303\|PubMed:12559562, ECO:0000303\|PubMed:15203199}.
Q07157	TJP1	S290	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S300	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S303	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S326	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S340	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S834	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S837	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S933	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07666	KHDRBS1	S18	ochoa	KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)	Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity). {ECO:0000250\|UniProtKB:Q60749, ECO:0000269\|PubMed:15021911, ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:20186123, ECO:0000269\|PubMed:20610388, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:26080397, ECO:0000269\|PubMed:26758068}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269\|PubMed:9013542}.
Q07666	KHDRBS1	S20	ochoa	KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)	Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity). {ECO:0000250\|UniProtKB:Q60749, ECO:0000269\|PubMed:15021911, ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:20186123, ECO:0000269\|PubMed:20610388, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:26080397, ECO:0000269\|PubMed:26758068}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269\|PubMed:9013542}.
Q07666	KHDRBS1	S24	ochoa	KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)	Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity). {ECO:0000250\|UniProtKB:Q60749, ECO:0000269\|PubMed:15021911, ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:20186123, ECO:0000269\|PubMed:20610388, ECO:0000269\|PubMed:22253824, ECO:0000269\|PubMed:26080397, ECO:0000269\|PubMed:26758068}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269\|PubMed:9013542}.
Q07954	LRP1	S4523	ochoa\|psp	Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]	Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor (PubMed:1702392, PubMed:26142438). Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178). May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:12888553). Also acts as a receptor for IGFBP3 to mediate cell growth inhibition (PubMed:9252371). {ECO:0000250\|UniProtKB:Q91ZX7, ECO:0000269\|PubMed:11907044, ECO:0000269\|PubMed:12713657, ECO:0000269\|PubMed:12888553, ECO:0000269\|PubMed:1702392, ECO:0000269\|PubMed:26142438, ECO:0000269\|PubMed:32296178, ECO:0000269\|PubMed:9252371}.; FUNCTION: (Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A. {ECO:0000269\|PubMed:1618748}.
Q08050	FOXM1	S505	ochoa	Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells)	Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (PubMed:19160488, PubMed:20360045). Plays a role in the control of cell proliferation (PubMed:19160488). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promotes transcription of PHB2 (PubMed:33754036). {ECO:0000269\|PubMed:17101782, ECO:0000269\|PubMed:19160488, ECO:0000269\|PubMed:20360045, ECO:0000269\|PubMed:33754036}.
Q08050	FOXM1	S710	ochoa	Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells)	Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (PubMed:19160488, PubMed:20360045). Plays a role in the control of cell proliferation (PubMed:19160488). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promotes transcription of PHB2 (PubMed:33754036). {ECO:0000269\|PubMed:17101782, ECO:0000269\|PubMed:19160488, ECO:0000269\|PubMed:20360045, ECO:0000269\|PubMed:33754036}.
Q08170	SRSF4	S450	ochoa	Serine/arginine-rich splicing factor 4 (Pre-mRNA-splicing factor SRP75) (SRP001LB) (Splicing factor, arginine/serine-rich 4)	Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:15009664}.
Q08211	DHX9	S1032	ochoa	ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (DExH-box helicase 9) (Leukophysin) (LKP) (Nuclear DNA helicase II) (NDH II) (RNA helicase A)	Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing (PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:24990949, PubMed:25062910, PubMed:28221134, PubMed:9111062, PubMed:37467750). Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:10198287, PubMed:9111062). Also binds to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1 (PubMed:11038348, PubMed:11149922, PubMed:11416126, PubMed:15355351, PubMed:28221134, PubMed:9323138, PubMed:9662397). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). Also acts as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA (PubMed:10924507, PubMed:11402034, PubMed:9162007). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process (PubMed:17531811). Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (PubMed:11687588). {ECO:0000250\|UniProtKB:O70133, ECO:0000269\|PubMed:10198287, ECO:0000269\|PubMed:10924507, ECO:0000269\|PubMed:11038348, ECO:0000269\|PubMed:11149922, ECO:0000269\|PubMed:11402034, ECO:0000269\|PubMed:11416126, ECO:0000269\|PubMed:11687588, ECO:0000269\|PubMed:12711669, ECO:0000269\|PubMed:15355351, ECO:0000269\|PubMed:1537828, ECO:0000269\|PubMed:16680162, ECO:0000269\|PubMed:17531811, ECO:0000269\|PubMed:19029303, ECO:0000269\|PubMed:20669935, ECO:0000269\|PubMed:21247876, ECO:0000269\|PubMed:21561811, ECO:0000269\|PubMed:22190748, ECO:0000269\|PubMed:24049074, ECO:0000269\|PubMed:24990949, ECO:0000269\|PubMed:25062910, ECO:0000269\|PubMed:28221134, ECO:0000269\|PubMed:28355180, ECO:0000269\|PubMed:28636595, ECO:0000269\|PubMed:37467750, ECO:0000269\|PubMed:9111062, ECO:0000269\|PubMed:9162007, ECO:0000269\|PubMed:9323138, ECO:0000269\|PubMed:9662397}.; FUNCTION: (Microbial infection) Plays a role in HIV-1 replication and virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by facilitating the binding of RNA polymerase II holoenzyme to the proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation response element (TAR)-containing mRNAs (PubMed:11096080, PubMed:9892698). Involved also in HIV-1 mRNA splicing and transport (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-1 double-stranded RNA region of the primer binding site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 incorporation into virions and virion infectivity (PubMed:27107641). Also plays a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in plasmacytoid dendritic cells (pDCs), and hence induce antiviral innate immune responses (PubMed:20696886, PubMed:21957149). Binds (via the OB-fold region) to viral single-stranded DNA unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886). {ECO:0000269\|PubMed:11096080, ECO:0000269\|PubMed:16680162, ECO:0000269\|PubMed:19229320, ECO:0000269\|PubMed:20696886, ECO:0000269\|PubMed:21957149, ECO:0000269\|PubMed:25149208, ECO:0000269\|PubMed:27107641, ECO:0000269\|PubMed:9892698}.
Q08378	GOLGA3	S22	ochoa	Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160)	Golgi auto-antigen; probably involved in maintaining Golgi structure.
Q08378	GOLGA3	S278	ochoa	Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160)	Golgi auto-antigen; probably involved in maintaining Golgi structure.
Q08499	PDE4D	S380	ochoa	3',5'-cyclic-AMP phosphodiesterase 4D (EC 3.1.4.53) (DPDE3) (PDE43) (cAMP-specific phosphodiesterase 4D)	Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269\|PubMed:15260978, ECO:0000269\|PubMed:15576036, ECO:0000269\|PubMed:9371713}.
Q08999	RBL2	S971	ochoa	Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Q08999	RBL2	S972	ochoa	Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Q08AD1	CAMSAP2	S439	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S980	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S1293	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S1319	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q09666	AHNAK	S115	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S216	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5737	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5745	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5752	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5790	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5857	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5860	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5863	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5870	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q0JRZ9	FCHO2	S514	ochoa	F-BAR domain only protein 2	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269\|PubMed:17540576, ECO:0000269\|PubMed:20448150, ECO:0000269\|PubMed:21762413, ECO:0000269\|PubMed:22323290}.
Q0JRZ9	FCHO2	S515	ochoa	F-BAR domain only protein 2	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269\|PubMed:17540576, ECO:0000269\|PubMed:20448150, ECO:0000269\|PubMed:21762413, ECO:0000269\|PubMed:22323290}.
Q0JRZ9	FCHO2	S517	ochoa	F-BAR domain only protein 2	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269\|PubMed:17540576, ECO:0000269\|PubMed:20448150, ECO:0000269\|PubMed:21762413, ECO:0000269\|PubMed:22323290}.
Q12778	FOXO1	S325	ochoa\|psp	Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)	Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). {ECO:0000250\|UniProtKB:A4L7N3, ECO:0000250\|UniProtKB:G3V7R4, ECO:0000250\|UniProtKB:Q9R1E0, ECO:0000269\|PubMed:10358076, ECO:0000269\|PubMed:12228231, ECO:0000269\|PubMed:15220471, ECO:0000269\|PubMed:15890677, ECO:0000269\|PubMed:17024043, ECO:0000269\|PubMed:18356527, ECO:0000269\|PubMed:19221179, ECO:0000269\|PubMed:19483080, ECO:0000269\|PubMed:20543840, ECO:0000269\|PubMed:21245099, ECO:0000269\|PubMed:31063815}.
Q12789	GTF3C1	S754	ochoa	General transcription factor 3C polypeptide 1 (TF3C-alpha) (TFIIIC box B-binding subunit) (Transcription factor IIIC 220 kDa subunit) (TFIIIC 220 kDa subunit) (TFIIIC220) (Transcription factor IIIC subunit alpha)	Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.
Q12789	GTF3C1	S757	ochoa	General transcription factor 3C polypeptide 1 (TF3C-alpha) (TFIIIC box B-binding subunit) (Transcription factor IIIC 220 kDa subunit) (TFIIIC 220 kDa subunit) (TFIIIC220) (Transcription factor IIIC subunit alpha)	Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.
Q12797	ASPH	S20	ochoa	Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase)	[Isoform 1]: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269\|PubMed:11773073}.; FUNCTION: [Isoform 8]: Membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269\|PubMed:22586105}.
Q12797	ASPH	S22	ochoa	Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase)	[Isoform 1]: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269\|PubMed:11773073}.; FUNCTION: [Isoform 8]: Membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269\|PubMed:22586105}.
Q12802	AKAP13	S1513	ochoa	A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)	Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:24993829, PubMed:25186459). May also activate other Rho family members (PubMed:11546812). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:21224381, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (PubMed:11579095, PubMed:9627117). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (PubMed:11546812). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q394, ECO:0000269\|PubMed:11546812, ECO:0000269\|PubMed:11579095, ECO:0000269\|PubMed:17537920, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:23716597, ECO:0000269\|PubMed:24993829, ECO:0000269\|PubMed:25186459, ECO:0000269\|PubMed:9627117, ECO:0000269\|PubMed:9891067}.
Q12802	AKAP13	S1904	ochoa	A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)	Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:24993829, PubMed:25186459). May also activate other Rho family members (PubMed:11546812). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:21224381, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (PubMed:11579095, PubMed:9627117). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (PubMed:11546812). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q394, ECO:0000269\|PubMed:11546812, ECO:0000269\|PubMed:11579095, ECO:0000269\|PubMed:17537920, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:23716597, ECO:0000269\|PubMed:24993829, ECO:0000269\|PubMed:25186459, ECO:0000269\|PubMed:9627117, ECO:0000269\|PubMed:9891067}.
Q12802	AKAP13	S1906	ochoa	A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)	Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:24993829, PubMed:25186459). May also activate other Rho family members (PubMed:11546812). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:21224381, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (PubMed:11579095, PubMed:9627117). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (PubMed:11546812). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q394, ECO:0000269\|PubMed:11546812, ECO:0000269\|PubMed:11579095, ECO:0000269\|PubMed:17537920, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:23716597, ECO:0000269\|PubMed:24993829, ECO:0000269\|PubMed:25186459, ECO:0000269\|PubMed:9627117, ECO:0000269\|PubMed:9891067}.
Q12802	AKAP13	S2726	ochoa	A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)	Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:24993829, PubMed:25186459). May also activate other Rho family members (PubMed:11546812). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:21224381, PubMed:23716597). Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity (PubMed:23090968). Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (PubMed:11579095, PubMed:9627117). Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438). Functions as a scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (PubMed:11546812). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q394, ECO:0000269\|PubMed:11546812, ECO:0000269\|PubMed:11579095, ECO:0000269\|PubMed:17537920, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:23716597, ECO:0000269\|PubMed:24993829, ECO:0000269\|PubMed:25186459, ECO:0000269\|PubMed:9627117, ECO:0000269\|PubMed:9891067}.
Q12830	BPTF	S202	ochoa	Nucleosome-remodeling factor subunit BPTF (Bromodomain and PHD finger-containing transcription factor) (Fetal Alz-50 clone 1 protein) (Fetal Alzheimer antigen)	Regulatory subunit of the ATP-dependent NURF-1 and NURF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:14609955, PubMed:28801535). The NURF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NURF-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NURF-1 ISWI chromatin-remodeling complex, binds to the promoters of En1 and En2 to positively regulate their expression and promote brain development (PubMed:14609955). Histone-binding protein which binds to H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of active genes (PubMed:16728976, PubMed:16728978). Binds to histone H3 tails dimethylated on 'Lys-4' (H3K4Me2) to a lesser extent (PubMed:16728976, PubMed:16728978, PubMed:18042461). May also regulate transcription through direct binding to DNA or transcription factors (PubMed:10575013). {ECO:0000269\|PubMed:10575013, ECO:0000269\|PubMed:14609955, ECO:0000269\|PubMed:16728976, ECO:0000269\|PubMed:16728978, ECO:0000269\|PubMed:18042461, ECO:0000269\|PubMed:28801535}.
Q12872	SFSWAP	S610	ochoa	Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog)	Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:8940107}.
Q12888	TP53BP1	S316	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S360	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S518	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S898	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S900	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1034	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1208	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1322	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1368	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12929	EPS8	S667	ochoa\|psp	Epidermal growth factor receptor kinase substrate 8	Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes. {ECO:0000269\|PubMed:15558031, ECO:0000269\|PubMed:17115031}.
Q12948	FOXC1	S527	ochoa	Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3)	DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development (PubMed:11782474, PubMed:14506133, PubMed:14578375, PubMed:15277473, PubMed:15299087, PubMed:15684392, PubMed:16449236, PubMed:16492674, PubMed:17210863, PubMed:19279310, PubMed:19793056, PubMed:25786029, PubMed:27804176, PubMed:27907090). Acts either as a transcriptional activator or repressor (PubMed:11782474). Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes (PubMed:11782474, PubMed:12533514, PubMed:14506133, PubMed:19793056, PubMed:27804176, PubMed:7957066). Upon DNA-binding, promotes DNA bending (PubMed:14506133, PubMed:7957066). Acts as a transcriptional coactivator (PubMed:26565916). Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification (By similarity). Also acts as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells (PubMed:26565916). Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye (PubMed:17993506). Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity (By similarity). Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals (PubMed:12408963). Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion (PubMed:20406990, PubMed:22991501). Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation (PubMed:27907090). Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). May function as a tumor suppressor (PubMed:12408963). {ECO:0000250\|UniProtKB:Q61572, ECO:0000269\|PubMed:11782474, ECO:0000269\|PubMed:12408963, ECO:0000269\|PubMed:12533514, ECO:0000269\|PubMed:14506133, ECO:0000269\|PubMed:14578375, ECO:0000269\|PubMed:15277473, ECO:0000269\|PubMed:15299087, ECO:0000269\|PubMed:15684392, ECO:0000269\|PubMed:16449236, ECO:0000269\|PubMed:16492674, ECO:0000269\|PubMed:17210863, ECO:0000269\|PubMed:17993506, ECO:0000269\|PubMed:19279310, ECO:0000269\|PubMed:19793056, ECO:0000269\|PubMed:20406990, ECO:0000269\|PubMed:22991501, ECO:0000269\|PubMed:25786029, ECO:0000269\|PubMed:26565916, ECO:0000269\|PubMed:27804176, ECO:0000269\|PubMed:27907090, ECO:0000269\|PubMed:7957066}.
Q12959	DLG1	S573	ochoa	Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97) (hDlg)	Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). May also play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. During long-term depression in hippocampal neurons, it recruits ADAM10 to the plasma membrane (PubMed:23676497). {ECO:0000250\|UniProtKB:A0A8C0TYJ0, ECO:0000250\|UniProtKB:Q811D0, ECO:0000269\|PubMed:10656683, ECO:0000269\|PubMed:12445884, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15263016, ECO:0000269\|PubMed:19213956, ECO:0000269\|PubMed:20605917, ECO:0000269\|PubMed:23676497}.
Q12968	NFATC3	S186	psp	Nuclear factor of activated T-cells, cytoplasmic 3 (NF-ATc3) (NFATc3) (NFATx) (T-cell transcription factor NFAT4) (NF-AT4) (NF-AT4c)	Acts as a regulator of transcriptional activation. Binds to the TNFSF11/RANKL promoter region and promotes TNFSF11 transcription (By similarity). Binding to the TNFSF11 promoter region is increased by high levels of Ca(2+) which induce NFATC3 expression and may lead to regulation of TNFSF11 expression in osteoblasts (By similarity). Plays a role in promoting mesenteric arterial wall remodeling in response to the intermittent hypoxia-induced increase in EDN1 and ROCK signaling (By similarity). As a result NFATC3 colocalizes with F-actin filaments, translocates to the nucleus and promotes transcription of the smooth muscle hypertrophy and differentiation marker ACTA2 (By similarity). Promotes lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes (By similarity). Following JAK/STAT signaling activation and as part of a complex with NFATC4 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity). In conjunction with NFATC4, involved in embryonic heart development via maintenance of cardiomyocyte survival, proliferation and differentiation (By similarity). Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 (PubMed:18815128). Required for thymocyte maturation during DN3 to DN4 transition and during positive selection (By similarity). Positively regulates macrophage-derived polymicrobial clearance, via binding to the promoter region and promoting transcription of NOS2 resulting in subsequent generation of nitric oxide (By similarity). Involved in Ca(2+)-mediated transcriptional responses upon Ca(2+) influx via ORAI1 CRAC channels. {ECO:0000250\|UniProtKB:A0A0G2JTY4, ECO:0000250\|UniProtKB:P97305, ECO:0000269\|PubMed:18815128, ECO:0000269\|PubMed:32415068}.
Q12968	NFATC3	S372	ochoa	Nuclear factor of activated T-cells, cytoplasmic 3 (NF-ATc3) (NFATc3) (NFATx) (T-cell transcription factor NFAT4) (NF-AT4) (NF-AT4c)	Acts as a regulator of transcriptional activation. Binds to the TNFSF11/RANKL promoter region and promotes TNFSF11 transcription (By similarity). Binding to the TNFSF11 promoter region is increased by high levels of Ca(2+) which induce NFATC3 expression and may lead to regulation of TNFSF11 expression in osteoblasts (By similarity). Plays a role in promoting mesenteric arterial wall remodeling in response to the intermittent hypoxia-induced increase in EDN1 and ROCK signaling (By similarity). As a result NFATC3 colocalizes with F-actin filaments, translocates to the nucleus and promotes transcription of the smooth muscle hypertrophy and differentiation marker ACTA2 (By similarity). Promotes lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes (By similarity). Following JAK/STAT signaling activation and as part of a complex with NFATC4 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity). In conjunction with NFATC4, involved in embryonic heart development via maintenance of cardiomyocyte survival, proliferation and differentiation (By similarity). Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 (PubMed:18815128). Required for thymocyte maturation during DN3 to DN4 transition and during positive selection (By similarity). Positively regulates macrophage-derived polymicrobial clearance, via binding to the promoter region and promoting transcription of NOS2 resulting in subsequent generation of nitric oxide (By similarity). Involved in Ca(2+)-mediated transcriptional responses upon Ca(2+) influx via ORAI1 CRAC channels. {ECO:0000250\|UniProtKB:A0A0G2JTY4, ECO:0000250\|UniProtKB:P97305, ECO:0000269\|PubMed:18815128, ECO:0000269\|PubMed:32415068}.
Q13029	PRDM2	S427	ochoa	PR domain zinc finger protein 2 (EC 2.1.1.355) (GATA-3-binding protein G3B) (Lysine N-methyltransferase 8) (MTB-ZF) (MTE-binding protein) (PR domain-containing protein 2) (Retinoblastoma protein-interacting zinc finger protein) (Zinc finger protein RIZ)	S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene. {ECO:0000269\|PubMed:14633678}.
Q13085	ACACA	S56	ochoa	Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (Acetyl-Coenzyme A carboxylase alpha) (ACC-alpha)	Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis (PubMed:20457939, PubMed:20952656, PubMed:29899443). This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:20457939, PubMed:20952656, PubMed:29899443). {ECO:0000269\|PubMed:20457939, ECO:0000269\|PubMed:20952656, ECO:0000269\|PubMed:29899443}.
Q13107	USP4	S598	ochoa	Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Ubiquitous nuclear protein homolog)	Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins (PubMed:16316627, PubMed:16339847, PubMed:16472766, PubMed:20595234, PubMed:22347420, PubMed:25404403, PubMed:28604766, PubMed:30514904). Deubiquitinates PDPK1 (PubMed:22347420). Deubiquitinates TRIM21 (PubMed:16316627). Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface (PubMed:16339847). Deubiquitinates HAS2 (PubMed:28604766). Deubiquitinates RHEB in response to EGF signaling, promoting mTORC1 signaling (PubMed:30514904). May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3 (PubMed:20595234). This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP (PubMed:20595234). May also play a role in the regulation of quality control in the ER (PubMed:16339847). {ECO:0000269\|PubMed:16316627, ECO:0000269\|PubMed:16339847, ECO:0000269\|PubMed:16472766, ECO:0000269\|PubMed:20595234, ECO:0000269\|PubMed:22347420, ECO:0000269\|PubMed:25404403, ECO:0000269\|PubMed:28604766, ECO:0000269\|PubMed:30514904}.
Q13112	CHAF1B	S464	ochoa	Chromatin assembly factor 1 subunit B (CAF-1 subunit B) (Chromatin assembly factor I p60 subunit) (CAF-I 60 kDa subunit) (CAF-I p60) (M-phase phosphoprotein 7)	Acts as a component of the histone chaperone complex chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto DNA during replication and repair. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. {ECO:0000269\|PubMed:9813080}.
Q13127	REST	S1030	psp	RE1-silencing transcription factor (Neural-restrictive silencer factor) (X2 box repressor)	Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (PubMed:11741002, PubMed:11779185, PubMed:12399542, PubMed:26551668, PubMed:7697725, PubMed:7871435, PubMed:8568247). Restricts the expression of neuronal genes by associating with two distinct corepressors, SIN3A and RCOR1, which in turn recruit histone deacetylase to the promoters of REST-regulated genes (PubMed:10449787, PubMed:10734093). Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier (By similarity). Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression (PubMed:19061646). Represses the expression of SRRM4 in non-neural cells to prevent the activation of neural-specific splicing events and to prevent production of REST isoform 3 (By similarity). Repressor activity may be inhibited by forming heterodimers with isoform 3, thereby preventing binding to NRSE or binding to corepressors and leading to derepression of target genes (PubMed:11779185). Also maintains repression of neuronal genes in neural stem cells, and allows transcription and differentiation into neurons by dissociation from RE1/NRSE sites of target genes (By similarity). Thereby is involved in maintaining the quiescent state of adult neural stem cells and preventing premature differentiation into mature neurons (PubMed:21258371). Plays a role in the developmental switch in synaptic NMDA receptor composition during postnatal development, by repressing GRIN2B expression and thereby altering NMDA receptor properties from containing primarily GRIN2B to primarily GRIN2A subunits (By similarity). Acts as a regulator of osteoblast differentiation (By similarity). Key repressor of gene expression in hypoxia; represses genes in hypoxia by direct binding to an RE1/NRSE site on their promoter regions (PubMed:27531581). May also function in stress resistance in the brain during aging; possibly by regulating expression of genes involved in cell death and in the stress response (PubMed:24670762). Repressor of gene expression in the hippocampus after ischemia by directly binding to RE1/NRSE sites and recruiting SIN3A and RCOR1 to promoters of target genes, thereby promoting changes in chromatin modifications and ischemia-induced cell death (By similarity). After ischemia, might play a role in repression of miR-132 expression in hippocampal neurons, thereby leading to neuronal cell death (By similarity). Negatively regulates the expression of SRRM3 in breast cancer cell lines (PubMed:26053433). {ECO:0000250\|UniProtKB:O54963, ECO:0000250\|UniProtKB:Q8VIG1, ECO:0000269\|PubMed:10449787, ECO:0000269\|PubMed:10734093, ECO:0000269\|PubMed:11741002, ECO:0000269\|PubMed:11779185, ECO:0000269\|PubMed:12399542, ECO:0000269\|PubMed:19061646, ECO:0000269\|PubMed:21258371, ECO:0000269\|PubMed:24670762, ECO:0000269\|PubMed:26053433, ECO:0000269\|PubMed:26551668, ECO:0000269\|PubMed:27531581, ECO:0000269\|PubMed:7697725, ECO:0000269\|PubMed:7871435, ECO:0000269\|PubMed:8568247}.; FUNCTION: [Isoform 3]: Binds to the 3' region of the neuron-restrictive silencer element (NRSE), with lower affinity than full-length REST isoform 1 (By similarity). Exhibits weaker repressor activity compared to isoform 1 (PubMed:11779185). May negatively regulate the repressor activity of isoform 1 by binding to isoform 1, thereby preventing its binding to NRSE and leading to derepression of target genes (PubMed:11779185). However, in another study, does not appear to be implicated in repressor activity of a NRSE motif-containing reporter construct nor in inhibitory activity on the isoform 1 transcriptional repressor activity (PubMed:11741002). Post-transcriptional inactivation of REST by SRRM4-dependent alternative splicing into isoform 3 is required in mechanosensory hair cells in the inner ear for derepression of neuronal genes and hearing (By similarity). {ECO:0000250\|UniProtKB:Q8VIG1, ECO:0000269\|PubMed:11741002, ECO:0000269\|PubMed:11779185}.
Q13131	PRKAA1	S523	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13131	PRKAA1	S530	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13136	PPFIA1	S693	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13136	PPFIA1	S793	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13163	MAP2K5	S148	ochoa	Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)	Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250\|UniProtKB:Q62862, ECO:0000269\|PubMed:7759517, ECO:0000269\|PubMed:9384584}.
Q13177	PAK2	S42	ochoa	Serine/threonine-protein kinase PAK 2 (EC 2.7.11.1) (Gamma-PAK) (PAK65) (S6/H4 kinase) (p21-activated kinase 2) (PAK-2) (p58) [Cleaved into: PAK-2p27 (p27); PAK-2p34 (p34) (C-t-PAK2)]	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:12853446, PubMed:16617111, PubMed:19273597, PubMed:19923322, PubMed:33693784, PubMed:7744004, PubMed:9171063). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:12853446, PubMed:16617111, PubMed:9171063). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964). {ECO:0000269\|PubMed:12853446, ECO:0000269\|PubMed:15234964, ECO:0000269\|PubMed:16617111, ECO:0000269\|PubMed:19273597, ECO:0000269\|PubMed:19923322, ECO:0000269\|PubMed:21177766, ECO:0000269\|PubMed:21317288, ECO:0000269\|PubMed:21555521, ECO:0000269\|PubMed:21724829, ECO:0000269\|PubMed:27889207, ECO:0000269\|PubMed:33693784, ECO:0000269\|PubMed:7744004, ECO:0000269\|PubMed:9171063}.
Q13177	PAK2	S64	ochoa\|psp	Serine/threonine-protein kinase PAK 2 (EC 2.7.11.1) (Gamma-PAK) (PAK65) (S6/H4 kinase) (p21-activated kinase 2) (PAK-2) (p58) [Cleaved into: PAK-2p27 (p27); PAK-2p34 (p34) (C-t-PAK2)]	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:12853446, PubMed:16617111, PubMed:19273597, PubMed:19923322, PubMed:33693784, PubMed:7744004, PubMed:9171063). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:12853446, PubMed:16617111, PubMed:9171063). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964). {ECO:0000269\|PubMed:12853446, ECO:0000269\|PubMed:15234964, ECO:0000269\|PubMed:16617111, ECO:0000269\|PubMed:19273597, ECO:0000269\|PubMed:19923322, ECO:0000269\|PubMed:21177766, ECO:0000269\|PubMed:21317288, ECO:0000269\|PubMed:21555521, ECO:0000269\|PubMed:21724829, ECO:0000269\|PubMed:27889207, ECO:0000269\|PubMed:33693784, ECO:0000269\|PubMed:7744004, ECO:0000269\|PubMed:9171063}.
Q13242	SRSF9	S193	ochoa	Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:10196175, ECO:0000269\|PubMed:11875052, ECO:0000269\|PubMed:12024014, ECO:0000269\|PubMed:12604611, ECO:0000269\|PubMed:15009090, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:15695522, ECO:0000269\|PubMed:7556075}.
Q13242	SRSF9	S195	ochoa	Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:10196175, ECO:0000269\|PubMed:11875052, ECO:0000269\|PubMed:12024014, ECO:0000269\|PubMed:12604611, ECO:0000269\|PubMed:15009090, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:15695522, ECO:0000269\|PubMed:7556075}.
Q13247	SRSF6	S303	ochoa	Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6)	Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269\|PubMed:12549914, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:22767602, ECO:0000269\|PubMed:24440982}.
Q13263	TRIM28	S459	ochoa	Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)	Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250\|UniProtKB:Q62318, ECO:0000269\|PubMed:10347202, ECO:0000269\|PubMed:11959841, ECO:0000269\|PubMed:15882967, ECO:0000269\|PubMed:16107876, ECO:0000269\|PubMed:16862143, ECO:0000269\|PubMed:17079232, ECO:0000269\|PubMed:17178852, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:17942393, ECO:0000269\|PubMed:18060868, ECO:0000269\|PubMed:18082607, ECO:0000269\|PubMed:20424263, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:20864041, ECO:0000269\|PubMed:21940674, ECO:0000269\|PubMed:23543754, ECO:0000269\|PubMed:23665872, ECO:0000269\|PubMed:24623306, ECO:0000269\|PubMed:27029610, ECO:0000269\|PubMed:8769649, ECO:0000269\|PubMed:9016654}.; FUNCTION: (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1. {ECO:0000269\|PubMed:24741090}.
Q13263	TRIM28	S466	ochoa	Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)	Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250\|UniProtKB:Q62318, ECO:0000269\|PubMed:10347202, ECO:0000269\|PubMed:11959841, ECO:0000269\|PubMed:15882967, ECO:0000269\|PubMed:16107876, ECO:0000269\|PubMed:16862143, ECO:0000269\|PubMed:17079232, ECO:0000269\|PubMed:17178852, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:17942393, ECO:0000269\|PubMed:18060868, ECO:0000269\|PubMed:18082607, ECO:0000269\|PubMed:20424263, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:20864041, ECO:0000269\|PubMed:21940674, ECO:0000269\|PubMed:23543754, ECO:0000269\|PubMed:23665872, ECO:0000269\|PubMed:24623306, ECO:0000269\|PubMed:27029610, ECO:0000269\|PubMed:8769649, ECO:0000269\|PubMed:9016654}.; FUNCTION: (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1. {ECO:0000269\|PubMed:24741090}.
Q13263	TRIM28	S479	ochoa	Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)	Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250\|UniProtKB:Q62318, ECO:0000269\|PubMed:10347202, ECO:0000269\|PubMed:11959841, ECO:0000269\|PubMed:15882967, ECO:0000269\|PubMed:16107876, ECO:0000269\|PubMed:16862143, ECO:0000269\|PubMed:17079232, ECO:0000269\|PubMed:17178852, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:17942393, ECO:0000269\|PubMed:18060868, ECO:0000269\|PubMed:18082607, ECO:0000269\|PubMed:20424263, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:20864041, ECO:0000269\|PubMed:21940674, ECO:0000269\|PubMed:23543754, ECO:0000269\|PubMed:23665872, ECO:0000269\|PubMed:24623306, ECO:0000269\|PubMed:27029610, ECO:0000269\|PubMed:8769649, ECO:0000269\|PubMed:9016654}.; FUNCTION: (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1. {ECO:0000269\|PubMed:24741090}.
Q13263	TRIM28	S600	ochoa	Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)	Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250\|UniProtKB:Q62318, ECO:0000269\|PubMed:10347202, ECO:0000269\|PubMed:11959841, ECO:0000269\|PubMed:15882967, ECO:0000269\|PubMed:16107876, ECO:0000269\|PubMed:16862143, ECO:0000269\|PubMed:17079232, ECO:0000269\|PubMed:17178852, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:17942393, ECO:0000269\|PubMed:18060868, ECO:0000269\|PubMed:18082607, ECO:0000269\|PubMed:20424263, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:20864041, ECO:0000269\|PubMed:21940674, ECO:0000269\|PubMed:23543754, ECO:0000269\|PubMed:23665872, ECO:0000269\|PubMed:24623306, ECO:0000269\|PubMed:27029610, ECO:0000269\|PubMed:8769649, ECO:0000269\|PubMed:9016654}.; FUNCTION: (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1. {ECO:0000269\|PubMed:24741090}.
Q13283	G3BP1	S256	ochoa	Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)	Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210). Plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36279435, PubMed:37379838). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:36279435, PubMed:36692217). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278). Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends (PubMed:9889278). Plays an essential role in innate immunity by promoting CGAS and RIGI activity (PubMed:30510222, PubMed:30804210). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (PubMed:30510222). Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles (PubMed:34779554). Also enhances RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (PubMed:30804210). May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). {ECO:0000269\|PubMed:11604510, ECO:0000269\|PubMed:12642610, ECO:0000269\|PubMed:20180778, ECO:0000269\|PubMed:23279204, ECO:0000269\|PubMed:27022092, ECO:0000269\|PubMed:30510222, ECO:0000269\|PubMed:30804210, ECO:0000269\|PubMed:32302570, ECO:0000269\|PubMed:32302571, ECO:0000269\|PubMed:32302572, ECO:0000269\|PubMed:34739333, ECO:0000269\|PubMed:34779554, ECO:0000269\|PubMed:35977029, ECO:0000269\|PubMed:36183834, ECO:0000269\|PubMed:36279435, ECO:0000269\|PubMed:36692217, ECO:0000269\|PubMed:37379838, ECO:0000269\|PubMed:9889278}.
Q13303	KCNAB2	S20	ochoa	Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (hKvbeta2)	Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits (PubMed:11825900, PubMed:7649300). The beta-2/KCNAB2 cytoplasmic subunit promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:11825900, PubMed:7649300). Promotes the inactivation of Kv1.4/KCNA4 and Kv1.5/KCNA5 alpha subunit-containing channels (PubMed:11825900, PubMed:7649300). Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH-dependent reduction of a wide range of aldehyde and ketone substrates (By similarity). Substrate specificity includes methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro, no physiological substrate identified yet) (By similarity). The binding of oxidized and reduced nucleotide alters Kv channel gating and may contribute to dynamic fine tuning of cell excitability (By similarity). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). {ECO:0000250\|UniProtKB:P62482, ECO:0000250\|UniProtKB:P62483, ECO:0000269\|PubMed:11825900, ECO:0000269\|PubMed:7649300}.
Q13416	ORC2	S145	ochoa	Origin recognition complex subunit 2	Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3. {ECO:0000269\|PubMed:22427655, ECO:0000269\|PubMed:22935713}.
Q13425	SNTB2	S239	ochoa	Beta-2-syntrophin (59 kDa dystrophin-associated protein A1 basic component 2) (Syntrophin-3) (SNT3) (Syntrophin-like) (SNTL)	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.
Q13425	SNTB2	S393	ochoa	Beta-2-syntrophin (59 kDa dystrophin-associated protein A1 basic component 2) (Syntrophin-3) (SNT3) (Syntrophin-like) (SNTL)	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.
Q13428	TCOF1	S484	ochoa	Treacle protein (Treacher Collins syndrome protein)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269\|PubMed:12777385, ECO:0000269\|PubMed:26399832}.
Q13428	TCOF1	S701	ochoa	Treacle protein (Treacher Collins syndrome protein)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269\|PubMed:12777385, ECO:0000269\|PubMed:26399832}.
Q13428	TCOF1	S1233	ochoa	Treacle protein (Treacher Collins syndrome protein)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269\|PubMed:12777385, ECO:0000269\|PubMed:26399832}.
Q13459	MYO9B	S1267	ochoa	Unconventional myosin-IXb (Unconventional myosin-9b)	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:26529257, PubMed:9490638). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269\|PubMed:26529257, ECO:0000269\|PubMed:9490638}.
Q13459	MYO9B	S1329	ochoa	Unconventional myosin-IXb (Unconventional myosin-9b)	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:26529257, PubMed:9490638). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269\|PubMed:26529257, ECO:0000269\|PubMed:9490638}.
Q13459	MYO9B	S1331	ochoa	Unconventional myosin-IXb (Unconventional myosin-9b)	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:26529257, PubMed:9490638). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269\|PubMed:26529257, ECO:0000269\|PubMed:9490638}.
Q13464	ROCK1	S1108	ochoa	Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)	Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250\|UniProtKB:P70335, ECO:0000250\|UniProtKB:Q8MIT6, ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:10652353, ECO:0000269\|PubMed:11018042, ECO:0000269\|PubMed:11283607, ECO:0000269\|PubMed:17158456, ECO:0000269\|PubMed:18573880, ECO:0000269\|PubMed:18694941, ECO:0000269\|PubMed:19036714, ECO:0000269\|PubMed:19131646, ECO:0000269\|PubMed:19181962, ECO:0000269\|PubMed:19997641, ECO:0000269\|PubMed:21072057, ECO:0000269\|PubMed:23093407, ECO:0000269\|PubMed:23355470, ECO:0000269\|PubMed:8617235, ECO:0000269\|PubMed:9722579}.
Q13469	NFATC2	S801	ochoa	Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)	Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF (PubMed:15790681). Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (PubMed:21871017). Is involved in the negative regulation of chondrogenesis (PubMed:35789258). Recruited by AKAP5 to ORAI1 pore-forming subunit of CRAC channels in Ca(2+) signaling microdomains where store-operated Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT-dependent transcriptional responses. {ECO:0000250\|UniProtKB:Q60591, ECO:0000269\|PubMed:15790681, ECO:0000269\|PubMed:21871017, ECO:0000269\|PubMed:35789258}.
Q13469	NFATC2	S814	ochoa	Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)	Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF (PubMed:15790681). Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (PubMed:21871017). Is involved in the negative regulation of chondrogenesis (PubMed:35789258). Recruited by AKAP5 to ORAI1 pore-forming subunit of CRAC channels in Ca(2+) signaling microdomains where store-operated Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT-dependent transcriptional responses. {ECO:0000250\|UniProtKB:Q60591, ECO:0000269\|PubMed:15790681, ECO:0000269\|PubMed:21871017, ECO:0000269\|PubMed:35789258}.
Q13470	TNK1	S508	ochoa	Non-receptor tyrosine-protein kinase TNK1 (EC 2.7.10.2) (CD38 negative kinase 1)	Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction. {ECO:0000269\|PubMed:10873601, ECO:0000269\|PubMed:18974114}.
Q13480	GAB1	S651	ochoa	GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1)	Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway (PubMed:29408807). {ECO:0000269\|PubMed:29408807}.
Q13490	BIRC2	S146	ochoa	Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)	Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. {ECO:0000269\|PubMed:15665297, ECO:0000269\|PubMed:18082613, ECO:0000269\|PubMed:21145488, ECO:0000269\|PubMed:21653699, ECO:0000269\|PubMed:21931591, ECO:0000269\|PubMed:23453969}.
Q13492	PICALM	S359	ochoa	Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein)	Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly (PubMed:10436022, PubMed:16262731, PubMed:27574975). Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature (PubMed:25898166). In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8 (PubMed:21808019, PubMed:22118466, PubMed:23741335). In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors (PubMed:25241929). Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF) (PubMed:24067654, PubMed:25241929). {ECO:0000269\|PubMed:10436022, ECO:0000269\|PubMed:16262731, ECO:0000269\|PubMed:21808019, ECO:0000269\|PubMed:22118466, ECO:0000269\|PubMed:23741335, ECO:0000269\|PubMed:24067654, ECO:0000269\|PubMed:25241929, ECO:0000269\|PubMed:25898166, ECO:0000269\|PubMed:27574975}.
Q13501	SQSTM1	S176	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S182	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S282	ochoa\|psp	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S283	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S349	ochoa\|psp	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S355	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13506	NAB1	S180	ochoa	NGFI-A-binding protein 1 (EGR-1-binding protein 1) (Transcriptional regulatory protein p54)	Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. {ECO:0000250}.
Q13523	PRP4K	S578	ochoa	Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 kinase) (PRP4 pre-mRNA-processing factor 4 homolog)	Serine/threonine kinase involved in spliceosomal assembly as well as mitosis and signaling regulation (PubMed:10799319, PubMed:12077342, PubMed:17513757, PubMed:17998396). Connects chromatin mediated regulation of transcription and pre-mRNA splicing (PubMed:12077342). During spliceosomal assembly, interacts with and phosphorylates PRPF6 and PRPF31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), to facilitate the formation of the spliceosome B complex. Plays a role in regulating transcription and the spindle assembly checkpoint (SAC) (PubMed:20118938). Associates with U5 snRNP and NCOR1 deacetylase complexes which may allow a coordination of pre-mRNA splicing with chromatin remodeling events involved in transcriptional regulation (PubMed:12077342). Associates and probably phosphorylates SMARCA4 and NCOR1 (PubMed:12077342). Phosphorylates SRSF1 (PubMed:11418604). Associates with kinetochores during mitosis and is necessary for recruitment and maintenance of the checkpoint proteins such as MAD1L1 and MAD12L1 at the kinetochores (PubMed:17998396). Phosphorylates and regulates the activity of the transcription factors such as ELK1 and KLF13 (PubMed:10799319, PubMed:17513757). Phosphorylates nuclear YAP1 and WWTR1/TAZ which induces nuclear exclusion and regulates Hippo signaling pathway, involved in tissue growth control (PubMed:29695716). {ECO:0000269\|PubMed:10799319, ECO:0000269\|PubMed:11418604, ECO:0000269\|PubMed:12077342, ECO:0000269\|PubMed:17513757, ECO:0000269\|PubMed:17998396, ECO:0000269\|PubMed:20118938, ECO:0000269\|PubMed:29695716}.
Q13526	PIN1	S38	ochoa	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1)	Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (PubMed:23623683, PubMed:27561354). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells (PubMed:29686383). Catalyzes cis-trans isomerization of phosphorylated phosphoglycerate kinase PGK1 under hypoxic conditions to promote its binding to the TOM complex and targeting to the mitochondrion (PubMed:26942675). {ECO:0000269\|PubMed:15664191, ECO:0000269\|PubMed:16644721, ECO:0000269\|PubMed:17828269, ECO:0000269\|PubMed:21497122, ECO:0000269\|PubMed:22033920, ECO:0000269\|PubMed:22608923, ECO:0000269\|PubMed:23623683, ECO:0000269\|PubMed:26942675, ECO:0000269\|PubMed:27561354, ECO:0000269\|PubMed:29686383}.
Q13563	PKD2	S801	ochoa\|psp	Polycystin-2 (PC2) (Autosomal dominant polycystic kidney disease type II protein) (Polycystic kidney disease 2 protein) (Polycystwin) (R48321) (Transient receptor potential cation channel subfamily P member 2)	Forms a nonselective cation channel (PubMed:11854751, PubMed:11991947, PubMed:15692563, PubMed:26269590, PubMed:27071085, PubMed:31441214, PubMed:39009345). Can function as a homotetrameric ion channel or can form heteromer with PKD1 (PubMed:31441214, PubMed:33164752). Displays distinct function depending on its subcellular localization and regulation by its binding partners (PubMed:11854751, PubMed:11991947, PubMed:27214281, PubMed:29899465). In primary cilium functions as a cation channel, with a preference for monovalent cations over divalent cations that allows K(+), Na(+) and Ca(2+) influx, with low selectivity for Ca(2+) (PubMed:27071085). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). In the endoplasmic reticulum, likely functions as a K(+) channel to facilitate Ca(2+) release (By similarity). The heterotetrameric PKD1/PKD2 channel has higher Ca(2+) permeability than homomeric PKD2 channel and acts as a primarily Ca(2+)-permeable channel (PubMed:31441214). Interacts with and acts as a regulator of a number of other channels, such as TRPV4, TRPC1, IP3R, RYR2, ultimately further affecting intracellular signaling, to modulate intracellular Ca(2+) signaling (PubMed:11854751, PubMed:11991947, PubMed:27214281, PubMed:29899465). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). In cardiomyocytes, PKD2 modulates Ca(2+) release from stimulated RYR2 receptors through direct association (By similarity). Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning (By similarity). Acts as a regulator of cilium length together with PKD1 (By similarity). Mediates systemic blood pressure and contributes to the myogenic response in cerebral arteries though vasoconstriction (By similarity). {ECO:0000250\|UniProtKB:O35245, ECO:0000269\|PubMed:11854751, ECO:0000269\|PubMed:11991947, ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:18695040, ECO:0000269\|PubMed:26269590, ECO:0000269\|PubMed:27071085, ECO:0000269\|PubMed:27214281, ECO:0000269\|PubMed:29899465, ECO:0000269\|PubMed:31441214, ECO:0000269\|PubMed:33164752, ECO:0000269\|PubMed:39009345}.
Q13563	PKD2	S835	ochoa	Polycystin-2 (PC2) (Autosomal dominant polycystic kidney disease type II protein) (Polycystic kidney disease 2 protein) (Polycystwin) (R48321) (Transient receptor potential cation channel subfamily P member 2)	Forms a nonselective cation channel (PubMed:11854751, PubMed:11991947, PubMed:15692563, PubMed:26269590, PubMed:27071085, PubMed:31441214, PubMed:39009345). Can function as a homotetrameric ion channel or can form heteromer with PKD1 (PubMed:31441214, PubMed:33164752). Displays distinct function depending on its subcellular localization and regulation by its binding partners (PubMed:11854751, PubMed:11991947, PubMed:27214281, PubMed:29899465). In primary cilium functions as a cation channel, with a preference for monovalent cations over divalent cations that allows K(+), Na(+) and Ca(2+) influx, with low selectivity for Ca(2+) (PubMed:27071085). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). In the endoplasmic reticulum, likely functions as a K(+) channel to facilitate Ca(2+) release (By similarity). The heterotetrameric PKD1/PKD2 channel has higher Ca(2+) permeability than homomeric PKD2 channel and acts as a primarily Ca(2+)-permeable channel (PubMed:31441214). Interacts with and acts as a regulator of a number of other channels, such as TRPV4, TRPC1, IP3R, RYR2, ultimately further affecting intracellular signaling, to modulate intracellular Ca(2+) signaling (PubMed:11854751, PubMed:11991947, PubMed:27214281, PubMed:29899465). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). In cardiomyocytes, PKD2 modulates Ca(2+) release from stimulated RYR2 receptors through direct association (By similarity). Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning (By similarity). Acts as a regulator of cilium length together with PKD1 (By similarity). Mediates systemic blood pressure and contributes to the myogenic response in cerebral arteries though vasoconstriction (By similarity). {ECO:0000250\|UniProtKB:O35245, ECO:0000269\|PubMed:11854751, ECO:0000269\|PubMed:11991947, ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:18695040, ECO:0000269\|PubMed:26269590, ECO:0000269\|PubMed:27071085, ECO:0000269\|PubMed:27214281, ECO:0000269\|PubMed:29899465, ECO:0000269\|PubMed:31441214, ECO:0000269\|PubMed:33164752, ECO:0000269\|PubMed:39009345}.
Q13568	IRF5	S446	ochoa\|psp	Interferon regulatory factor 5 (IRF-5)	Transcription factor that plays a critical role in innate immunity by activating expression of type I interferon (IFN) IFNA and INFB and inflammatory cytokines downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 (PubMed:11303025, PubMed:15695821, PubMed:22412986, PubMed:25326418, PubMed:32433612). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (By similarity). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction downstream of the TLR-activated, MyD88-dependent pathway (By similarity). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000250\|UniProtKB:P56477, ECO:0000269\|PubMed:11303025, ECO:0000269\|PubMed:15695821, ECO:0000269\|PubMed:22412986, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:32433612, ECO:0000269\|PubMed:33440148}.
Q13613	MTMR1	S49	ochoa	Phosphatidylinositol-3-phosphate phosphatase MTMR1 (EC 3.1.3.-) (Myotubularin-related protein 1) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate, generating phosphatidylinositol (PubMed:11733541, PubMed:27018598). Could also dephosphorylate phosphatidylinositol 3,5-bisphosphate to produce phosphatidylinositol 5-phosphate (PubMed:27018598). {ECO:0000269\|PubMed:11733541, ECO:0000269\|PubMed:27018598}.
Q13620	CUL4B	S53	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S67	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S69	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S70	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S84	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S145	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13620	CUL4B	S146	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13761	RUNX3	S220	ochoa	Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit)	Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (By similarity). May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Necessary for the development and survival of sensory neurons expressing parvalbumin (By similarity). {ECO:0000250\|UniProtKB:Q64131, ECO:0000269\|PubMed:20599712}.
Q13761	RUNX3	S226	ochoa	Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit)	Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (By similarity). May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Necessary for the development and survival of sensory neurons expressing parvalbumin (By similarity). {ECO:0000250\|UniProtKB:Q64131, ECO:0000269\|PubMed:20599712}.
Q13796	SHROOM2	S157	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13796	SHROOM2	S158	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13796	SHROOM2	S159	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13796	SHROOM2	S180	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13796	SHROOM2	S195	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13835	PKP1	S60	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13835	PKP1	S63	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13835	PKP1	S65	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13835	PKP1	S127	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13835	PKP1	S191	ochoa\|psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13838	DDX39B	S44	ochoa	Spliceosome RNA helicase DDX39B (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (ATP-dependent RNA helicase p47) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein)	Involved in nuclear export of spliced and unspliced mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). The THOC1-THOC2-THOC3 core complex alone is sufficient to promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). Associates with SARNP/CIP29, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC4 and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability. {ECO:0000269\|PubMed:11675789, ECO:0000269\|PubMed:15585580, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:17562711, ECO:0000269\|PubMed:17984224, ECO:0000269\|PubMed:20844015, ECO:0000269\|PubMed:22144908, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:23299939, ECO:0000269\|PubMed:33191911, ECO:0000269\|PubMed:37578863, ECO:0000269\|PubMed:9242493}.; FUNCTION: Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect. {ECO:0000269\|PubMed:23299939, ECO:0000269\|PubMed:9242493}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q13884	SNTB1	S225	ochoa	Beta-1-syntrophin (59 kDa dystrophin-associated protein A1 basic component 1) (DAPA1B) (BSYN2) (Syntrophin-2) (Tax interaction protein 43) (TIP-43)	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex.
Q13884	SNTB1	S231	ochoa	Beta-1-syntrophin (59 kDa dystrophin-associated protein A1 basic component 1) (DAPA1B) (BSYN2) (Syntrophin-2) (Tax interaction protein 43) (TIP-43)	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex.
Q13905	RAPGEF1	S358	ochoa	Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G)	Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1 (PubMed:12432078). Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:7806500}.
Q13905	RAPGEF1	S371	ochoa	Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G)	Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1 (PubMed:12432078). Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:7806500}.
Q13950	RUNX2	S243	ochoa	Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)	Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis (PubMed:28505335, PubMed:28703881, PubMed:28738062). Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Inhibits KAT6B-dependent transcriptional activation. {ECO:0000250, ECO:0000269\|PubMed:11965546, ECO:0000269\|PubMed:28505335, ECO:0000269\|PubMed:28703881, ECO:0000269\|PubMed:28738062}.
Q14004	CDK13	S391	ochoa	Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)	Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269\|PubMed:16721827, ECO:0000269\|PubMed:1731328, ECO:0000269\|PubMed:18480452, ECO:0000269\|PubMed:20952539}.
Q14004	CDK13	S1152	ochoa	Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)	Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269\|PubMed:16721827, ECO:0000269\|PubMed:1731328, ECO:0000269\|PubMed:18480452, ECO:0000269\|PubMed:20952539}.
Q14004	CDK13	S1351	ochoa	Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)	Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269\|PubMed:16721827, ECO:0000269\|PubMed:1731328, ECO:0000269\|PubMed:18480452, ECO:0000269\|PubMed:20952539}.
Q14005	IL16	S1032	ochoa	Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]	Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: [Isoform 1]: May act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Q14005	IL16	S1083	ochoa	Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]	Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: [Isoform 1]: May act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Q14008	CKAP5	S2005	ochoa	Cytoskeleton-associated protein 5 (Colonic and hepatic tumor overexpressed gene protein) (Ch-TOG)	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448). {ECO:0000269\|PubMed:12569123, ECO:0000269\|PubMed:18809577, ECO:0000269\|PubMed:21297582, ECO:0000269\|PubMed:21646404, ECO:0000269\|PubMed:23532825, ECO:0000269\|PubMed:27156448, ECO:0000269\|PubMed:9570755}.
Q14008	CKAP5	S2010	ochoa	Cytoskeleton-associated protein 5 (Colonic and hepatic tumor overexpressed gene protein) (Ch-TOG)	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448). {ECO:0000269\|PubMed:12569123, ECO:0000269\|PubMed:18809577, ECO:0000269\|PubMed:21297582, ECO:0000269\|PubMed:21646404, ECO:0000269\|PubMed:23532825, ECO:0000269\|PubMed:27156448, ECO:0000269\|PubMed:9570755}.
Q14126	DSG2	S893	ochoa	Desmoglein-2 (Cadherin family member 5) (HDGC)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:38395410). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Required for proliferation and viability of embryonic stem cells in the blastocyst, thereby crucial for progression of post-implantation embryonic development (By similarity). Maintains pluripotency by regulating epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via interacting with and sequestering CTNNB1 to sites of cell-cell contact, thereby reducing translocation of CTNNB1 to the nucleus and subsequent transcription of CTNNB1/TCF-target genes (PubMed:29910125). Promotes pluripotency and the multi-lineage differentiation potential of hematopoietic stem cells (PubMed:27338829). Plays a role in endothelial cell sprouting and elongation via mediating the junctional-association of cortical actin fibers and CDH5 (PubMed:27338829). Plays a role in limiting inflammatory infiltration and the apoptotic response to injury in kidney tubular epithelial cells, potentially via its role in maintaining cell-cell adhesion and the epithelial barrier (PubMed:38395410). {ECO:0000250\|UniProtKB:O55111, ECO:0000269\|PubMed:27338829, ECO:0000269\|PubMed:29910125, ECO:0000269\|PubMed:38395410}.
Q14149	MORC3	S503	ochoa	MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)	Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696). Binds RNA in vitro (PubMed:11927593). Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034). {ECO:0000269\|PubMed:11927593, ECO:0000269\|PubMed:17332504, ECO:0000269\|PubMed:20501696, ECO:0000269\|PubMed:26933034, ECO:0000269\|PubMed:27440897, ECO:0000269\|PubMed:34759314}.; FUNCTION: (Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269\|PubMed:26202233}.
Q14149	MORC3	S566	ochoa	MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)	Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696). Binds RNA in vitro (PubMed:11927593). Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034). {ECO:0000269\|PubMed:11927593, ECO:0000269\|PubMed:17332504, ECO:0000269\|PubMed:20501696, ECO:0000269\|PubMed:26933034, ECO:0000269\|PubMed:27440897, ECO:0000269\|PubMed:34759314}.; FUNCTION: (Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269\|PubMed:26202233}.
Q14151	SAFB2	S17	ochoa	Scaffold attachment factor B2 (SAF-B2)	Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.
Q14151	SAFB2	S282	ochoa	Scaffold attachment factor B2 (SAF-B2)	Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.
Q14155	ARHGEF7	S153	ochoa	Rho guanine nucleotide exchange factor 7 (Beta-Pix) (COOL-1) (PAK-interacting exchange factor beta) (p85)	Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. {ECO:0000250, ECO:0000269\|PubMed:18184567, ECO:0000269\|PubMed:18716323, ECO:0000269\|PubMed:19041750}.
Q14155	ARHGEF7	S159	ochoa	Rho guanine nucleotide exchange factor 7 (Beta-Pix) (COOL-1) (PAK-interacting exchange factor beta) (p85)	Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. {ECO:0000250, ECO:0000269\|PubMed:18184567, ECO:0000269\|PubMed:18716323, ECO:0000269\|PubMed:19041750}.
Q14155	ARHGEF7	S167	ochoa	Rho guanine nucleotide exchange factor 7 (Beta-Pix) (COOL-1) (PAK-interacting exchange factor beta) (p85)	Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. {ECO:0000250, ECO:0000269\|PubMed:18184567, ECO:0000269\|PubMed:18716323, ECO:0000269\|PubMed:19041750}.
Q14157	UBAP2L	S416	ochoa	Ubiquitin-associated protein 2-like (Protein NICE-4) (RNA polymerase II degradation factor UBAP2L)	Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled nucleotide excision repair (TC-NER) machinery fails to resolve DNA damage (PubMed:35633597). Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs) (By similarity). Is a regulator of stress granule assembly, required for their efficient formation (PubMed:29395067, PubMed:35977029). Required for proper brain development and neocortex lamination (By similarity). {ECO:0000250\|UniProtKB:Q80X50, ECO:0000269\|PubMed:29395067, ECO:0000269\|PubMed:35633597}.
Q14160	SCRIB	S1226	ochoa	Protein scribble homolog (Scribble) (hScrib) (Protein LAP4)	Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization (PubMed:15182672, PubMed:16344308, PubMed:16965391, PubMed:18641685, PubMed:18716323, PubMed:19041750, PubMed:27380321). Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production (By similarity). Plays a role in cell directional movement, cell orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). Most probably functions in the establishment of apico-basal cell polarity (PubMed:16344308, PubMed:19041750). May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium (PubMed:16965391, PubMed:19041750). May regulate cell invasion via MAPK-mediated cell migration and adhesion (PubMed:18641685, PubMed:18716323). May play a role in exocytosis and in the targeting of synaptic vesicles to synapses (PubMed:15182672). Functions as an activator of Rac GTPase activity (PubMed:15182672). {ECO:0000250\|UniProtKB:A0A8P0N4K0, ECO:0000250\|UniProtKB:Q80U72, ECO:0000269\|PubMed:15182672, ECO:0000269\|PubMed:16344308, ECO:0000269\|PubMed:16965391, ECO:0000269\|PubMed:18641685, ECO:0000269\|PubMed:18716323, ECO:0000269\|PubMed:19041750, ECO:0000269\|PubMed:27380321}.
Q14160	SCRIB	S1285	ochoa	Protein scribble homolog (Scribble) (hScrib) (Protein LAP4)	Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization (PubMed:15182672, PubMed:16344308, PubMed:16965391, PubMed:18641685, PubMed:18716323, PubMed:19041750, PubMed:27380321). Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production (By similarity). Plays a role in cell directional movement, cell orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). Most probably functions in the establishment of apico-basal cell polarity (PubMed:16344308, PubMed:19041750). May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium (PubMed:16965391, PubMed:19041750). May regulate cell invasion via MAPK-mediated cell migration and adhesion (PubMed:18641685, PubMed:18716323). May play a role in exocytosis and in the targeting of synaptic vesicles to synapses (PubMed:15182672). Functions as an activator of Rac GTPase activity (PubMed:15182672). {ECO:0000250\|UniProtKB:A0A8P0N4K0, ECO:0000250\|UniProtKB:Q80U72, ECO:0000269\|PubMed:15182672, ECO:0000269\|PubMed:16344308, ECO:0000269\|PubMed:16965391, ECO:0000269\|PubMed:18641685, ECO:0000269\|PubMed:18716323, ECO:0000269\|PubMed:19041750, ECO:0000269\|PubMed:27380321}.
Q14161	GIT2	S562	ochoa	ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. {ECO:0000269\|PubMed:10896954}.
Q14161	GIT2	S565	ochoa	ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. {ECO:0000269\|PubMed:10896954}.
Q14162	SCARF1	S611	ochoa	Scavenger receptor class F member 1 (Acetyl LDL receptor) (Scavenger receptor expressed by endothelial cells 1) (SREC-I)	Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). {ECO:0000250}.
Q14185	DOCK1	S1764	ochoa	Dedicator of cytokinesis protein 1 (180 kDa protein downstream of CRK) (DOCK180)	Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (PubMed:19004829). Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1 (PubMed:8657152). {ECO:0000269\|PubMed:19004829, ECO:0000269\|PubMed:8657152}.
Q14202	ZMYM3	S1055	ochoa	Zinc finger MYM-type protein 3 (Zinc finger protein 261)	Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269\|PubMed:21834987}.
Q14207	NPAT	S377	ochoa	Protein NPAT (Nuclear protein of the ataxia telangiectasia mutated locus) (Nuclear protein of the ATM locus) (p220)	Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters. {ECO:0000269\|PubMed:10995386, ECO:0000269\|PubMed:10995387, ECO:0000269\|PubMed:12665581, ECO:0000269\|PubMed:12724424, ECO:0000269\|PubMed:14585971, ECO:0000269\|PubMed:14612403, ECO:0000269\|PubMed:15555599, ECO:0000269\|PubMed:15988025, ECO:0000269\|PubMed:16131487, ECO:0000269\|PubMed:17163457, ECO:0000269\|PubMed:17826007, ECO:0000269\|PubMed:17967892, ECO:0000269\|PubMed:17974976, ECO:0000269\|PubMed:9472014}.
Q14207	NPAT	S1302	ochoa	Protein NPAT (Nuclear protein of the ataxia telangiectasia mutated locus) (Nuclear protein of the ATM locus) (p220)	Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters. {ECO:0000269\|PubMed:10995386, ECO:0000269\|PubMed:10995387, ECO:0000269\|PubMed:12665581, ECO:0000269\|PubMed:12724424, ECO:0000269\|PubMed:14585971, ECO:0000269\|PubMed:14612403, ECO:0000269\|PubMed:15555599, ECO:0000269\|PubMed:15988025, ECO:0000269\|PubMed:16131487, ECO:0000269\|PubMed:17163457, ECO:0000269\|PubMed:17826007, ECO:0000269\|PubMed:17967892, ECO:0000269\|PubMed:17974976, ECO:0000269\|PubMed:9472014}.
Q14244	MAP7	S209	ochoa	Ensconsin (Epithelial microtubule-associated protein of 115 kDa) (E-MAP-115) (Microtubule-associated protein 7) (MAP-7)	Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269\|PubMed:11719555, ECO:0000269\|PubMed:8408219, ECO:0000269\|PubMed:9989799}.
Q14244	MAP7	S663	ochoa	Ensconsin (Epithelial microtubule-associated protein of 115 kDa) (E-MAP-115) (Microtubule-associated protein 7) (MAP-7)	Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269\|PubMed:11719555, ECO:0000269\|PubMed:8408219, ECO:0000269\|PubMed:9989799}.
Q14247	CTTN	S156	ochoa	Src substrate cortactin (Amplaxin) (Oncogene EMS1)	Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (PubMed:20861316). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (PubMed:23144454). Plays a role in the invasiveness of cancer cells, and the formation of metastases (PubMed:16636290). {ECO:0000250\|UniProtKB:Q60598, ECO:0000250\|UniProtKB:Q66HL2, ECO:0000269\|PubMed:16636290, ECO:0000269\|PubMed:17959782, ECO:0000269\|PubMed:21296879, ECO:0000269\|PubMed:23144454}.
Q14289	PTK2B	S758	ochoa	Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)	Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. {ECO:0000269\|PubMed:10022920, ECO:0000269\|PubMed:12771146, ECO:0000269\|PubMed:12893833, ECO:0000269\|PubMed:14585963, ECO:0000269\|PubMed:15050747, ECO:0000269\|PubMed:15166227, ECO:0000269\|PubMed:17634955, ECO:0000269\|PubMed:18086875, ECO:0000269\|PubMed:18339875, ECO:0000269\|PubMed:18587400, ECO:0000269\|PubMed:18765415, ECO:0000269\|PubMed:19086031, ECO:0000269\|PubMed:19207108, ECO:0000269\|PubMed:19244237, ECO:0000269\|PubMed:19428251, ECO:0000269\|PubMed:19648005, ECO:0000269\|PubMed:19880522, ECO:0000269\|PubMed:20001213, ECO:0000269\|PubMed:20381867, ECO:0000269\|PubMed:20521079, ECO:0000269\|PubMed:21357692, ECO:0000269\|PubMed:21533080, ECO:0000269\|PubMed:7544443, ECO:0000269\|PubMed:8670418, ECO:0000269\|PubMed:8849729}.
Q14315	FLNC	S2152	ochoa	Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)	Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250\|UniProtKB:Q8VHX6, ECO:0000269\|PubMed:34405687}.
Q14315	FLNC	S2632	ochoa	Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)	Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250\|UniProtKB:Q8VHX6, ECO:0000269\|PubMed:34405687}.
Q14432	PDE3A	S496	ochoa	cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A) (cGMP-inhibited cAMP phosphodiesterase) (cGI-PDE)	Cyclic nucleotide phosphodiesterase with specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:1315035, PubMed:25961942, PubMed:8155697, PubMed:8695850). Also has activity toward cUMP (PubMed:27975297). Independently of its catalytic activity it is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling (PubMed:31420216, PubMed:34707099). {ECO:0000269\|PubMed:1315035, ECO:0000269\|PubMed:25961942, ECO:0000269\|PubMed:27975297, ECO:0000269\|PubMed:31420216, ECO:0000269\|PubMed:34707099, ECO:0000269\|PubMed:8155697, ECO:0000269\|PubMed:8695850}.
Q14449	GRB14	S372	ochoa\|psp	Growth factor receptor-bound protein 14 (GRB14 adapter protein)	Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal. {ECO:0000269\|PubMed:15210700, ECO:0000269\|PubMed:19648926}.
Q14457	BECN1	S96	psp	Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) (Protein GT197) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa]	Plays a central role in autophagy (PubMed:18570871, PubMed:21358617, PubMed:23184933, PubMed:23974797, PubMed:25484083, PubMed:28445460, PubMed:37776275). Acts as a core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20208530, PubMed:20643123, PubMed:23974797, PubMed:26783301). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). May play a role in antiviral host defense. {ECO:0000269\|PubMed:18570871, ECO:0000269\|PubMed:20208530, ECO:0000269\|PubMed:20643123, ECO:0000269\|PubMed:21358617, ECO:0000269\|PubMed:23184933, ECO:0000269\|PubMed:23974797, ECO:0000269\|PubMed:25275521, ECO:0000269\|PubMed:25484083, ECO:0000269\|PubMed:26783301, ECO:0000269\|PubMed:28445460, ECO:0000269\|PubMed:37776275, ECO:0000269\|PubMed:9765397}.; FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors. {ECO:0000269\|PubMed:21364619, ECO:0000269\|PubMed:26263979}.; FUNCTION: (Microbial infection) Protects against infection by a neurovirulent strain of Sindbis virus. {ECO:0000269\|PubMed:9765397}.
Q14573	ITPR3	S940	ochoa	Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3 (IP3 receptor isoform 3) (IP3R-3) (InsP3R3) (Type 3 inositol 1,4,5-trisphosphate receptor) (Type 3 InsP3 receptor)	Inositol 1,4,5-trisphosphate-gated calcium channel that, upon 1D-myo-inositol 1,4,5-trisphosphate binding, transports calcium from the endoplasmic reticulum lumen to cytoplasm, thus releasing the intracellular calcium and therefore participates in cellular calcium ion homeostasis (PubMed:32949214, PubMed:37898605, PubMed:8081734, PubMed:8288584). 1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (PubMed:30013099, PubMed:35301323, PubMed:37898605). Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (PubMed:30013099, PubMed:35301323, PubMed:37898605). {ECO:0000269\|PubMed:30013099, ECO:0000269\|PubMed:32949214, ECO:0000269\|PubMed:35301323, ECO:0000269\|PubMed:37898605, ECO:0000269\|PubMed:8081734, ECO:0000269\|PubMed:8288584}.
Q14573	ITPR3	S946	ochoa	Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3 (IP3 receptor isoform 3) (IP3R-3) (InsP3R3) (Type 3 inositol 1,4,5-trisphosphate receptor) (Type 3 InsP3 receptor)	Inositol 1,4,5-trisphosphate-gated calcium channel that, upon 1D-myo-inositol 1,4,5-trisphosphate binding, transports calcium from the endoplasmic reticulum lumen to cytoplasm, thus releasing the intracellular calcium and therefore participates in cellular calcium ion homeostasis (PubMed:32949214, PubMed:37898605, PubMed:8081734, PubMed:8288584). 1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (PubMed:30013099, PubMed:35301323, PubMed:37898605). Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (PubMed:30013099, PubMed:35301323, PubMed:37898605). {ECO:0000269\|PubMed:30013099, ECO:0000269\|PubMed:32949214, ECO:0000269\|PubMed:35301323, ECO:0000269\|PubMed:37898605, ECO:0000269\|PubMed:8081734, ECO:0000269\|PubMed:8288584}.
Q14573	ITPR3	S1838	ochoa	Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3 (IP3 receptor isoform 3) (IP3R-3) (InsP3R3) (Type 3 inositol 1,4,5-trisphosphate receptor) (Type 3 InsP3 receptor)	Inositol 1,4,5-trisphosphate-gated calcium channel that, upon 1D-myo-inositol 1,4,5-trisphosphate binding, transports calcium from the endoplasmic reticulum lumen to cytoplasm, thus releasing the intracellular calcium and therefore participates in cellular calcium ion homeostasis (PubMed:32949214, PubMed:37898605, PubMed:8081734, PubMed:8288584). 1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (PubMed:30013099, PubMed:35301323, PubMed:37898605). Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (PubMed:30013099, PubMed:35301323, PubMed:37898605). {ECO:0000269\|PubMed:30013099, ECO:0000269\|PubMed:32949214, ECO:0000269\|PubMed:35301323, ECO:0000269\|PubMed:37898605, ECO:0000269\|PubMed:8081734, ECO:0000269\|PubMed:8288584}.
Q14596	NBR1	S596	ochoa	Next to BRCA1 gene 1 protein (Cell migration-inducing gene 19 protein) (Membrane component chromosome 17 surface marker 2) (Neighbor of BRCA1 gene 1 protein) (Protein 1A1-3B)	Ubiquitin-binding autophagy adapter that participates in different processes including host defense or intracellular homeostasis (PubMed:24692539, PubMed:33577621). Possesses a double function during the selective autophagy by acting as a shuttle bringing ubiquitinated proteins to autophagosomes and also by participating in the formation of protein aggregates (PubMed:24879152, PubMed:34471133). Plays a role in the regulation of the innate immune response by modulating type I interferon production and targeting ubiquitinated IRF3 for autophagic degradation (PubMed:35914352). In response to oxidative stress, promotes an increase in SQSTM1 levels, phosphorylation, and body formation by preventing its autophagic degradation (By similarity). In turn, activates the KEAP1-NRF2/NFE2L2 antioxidant pathway (By similarity). Also plays non-autophagy role by mediating the shuttle of IL-12 to late endosome for subsequent secretion (By similarity). {ECO:0000250\|UniProtKB:P97432, ECO:0000269\|PubMed:19250911, ECO:0000269\|PubMed:24692539, ECO:0000269\|PubMed:24879152, ECO:0000269\|PubMed:33577621, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:35914352}.
Q14653	IRF3	S402	psp	Interferon regulatory factor 3 (IRF-3)	Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:22394562, PubMed:25636800, PubMed:27302953, PubMed:36603579). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16154084, PubMed:27302953, PubMed:33440148, PubMed:36603579). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591). In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis (PubMed:25609812). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000269\|PubMed:16154084, ECO:0000269\|PubMed:22394562, ECO:0000269\|PubMed:24049179, ECO:0000269\|PubMed:25609812, ECO:0000269\|PubMed:25636800, ECO:0000269\|PubMed:27302953, ECO:0000269\|PubMed:31340999, ECO:0000269\|PubMed:31413131, ECO:0000269\|PubMed:32972995, ECO:0000269\|PubMed:33440148, ECO:0000269\|PubMed:36603579, ECO:0000269\|PubMed:8524823, ECO:0000303\|PubMed:11846977, ECO:0000303\|PubMed:16846591, ECO:0000303\|PubMed:16979567, ECO:0000303\|PubMed:20049431}.
Q14669	TRIP12	S997	ochoa	E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (E3 ubiquitin-protein ligase for Arf) (ULF) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)	E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair (PubMed:19028681, PubMed:22884692). Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins (PubMed:19028681). Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress (PubMed:20208519). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (PubMed:20208519). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (PubMed:20208519). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (PubMed:18627766). Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins (PubMed:20829358). Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex (PubMed:30982744). {ECO:0000269\|PubMed:18627766, ECO:0000269\|PubMed:19028681, ECO:0000269\|PubMed:20208519, ECO:0000269\|PubMed:20829358, ECO:0000269\|PubMed:22884692, ECO:0000269\|PubMed:30982744}.
Q14669	TRIP12	S1036	ochoa	E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (E3 ubiquitin-protein ligase for Arf) (ULF) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)	E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair (PubMed:19028681, PubMed:22884692). Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins (PubMed:19028681). Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress (PubMed:20208519). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (PubMed:20208519). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (PubMed:20208519). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (PubMed:18627766). Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins (PubMed:20829358). Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex (PubMed:30982744). {ECO:0000269\|PubMed:18627766, ECO:0000269\|PubMed:19028681, ECO:0000269\|PubMed:20208519, ECO:0000269\|PubMed:20829358, ECO:0000269\|PubMed:22884692, ECO:0000269\|PubMed:30982744}.
Q14671	PUM1	S806	ochoa	Pumilio homolog 1 (HsPUM) (Pumilio-1)	Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:18328718, PubMed:21397187, PubMed:21572425, PubMed:21653694). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517, PubMed:29474920). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000250\|UniProtKB:Q80U78, ECO:0000269\|PubMed:18328718, ECO:0000269\|PubMed:18776931, ECO:0000269\|PubMed:20818387, ECO:0000269\|PubMed:20860814, ECO:0000269\|PubMed:21397187, ECO:0000269\|PubMed:21572425, ECO:0000269\|PubMed:21653694, ECO:0000269\|PubMed:22345517, ECO:0000269\|PubMed:22955276, ECO:0000269\|PubMed:25340845, ECO:0000269\|PubMed:25768905, ECO:0000269\|PubMed:26724866, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:29474920}.
Q14676	MDC1	S1570	ochoa	Mediator of DNA damage checkpoint protein 1 (Nuclear factor with BRCT domains 1)	Histone reader protein required for checkpoint-mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle (PubMed:12475977, PubMed:12499369, PubMed:12551934, PubMed:12607003, PubMed:12607004, PubMed:12607005, PubMed:12611903, PubMed:14695167, PubMed:15201865, PubMed:15377652, PubMed:16049003, PubMed:16377563, PubMed:30898438). Specifically recognizes and binds histone H2AX phosphorylated at 'Ser-139', a marker of DNA damage, serving as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage sites (PubMed:12607005, PubMed:15201865, PubMed:16049003, PubMed:16377563, PubMed:30898438). Also required for downstream events subsequent to the recruitment of these proteins (PubMed:12607005, PubMed:15201865, PubMed:16049003, PubMed:16377563, PubMed:18582474). These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53/p53 and apoptosis (PubMed:12499369, PubMed:12551934, PubMed:12607004). ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1 (PubMed:12499369, PubMed:12551934, PubMed:12607004). Required for chromosomal stability during mitosis by promoting recruitment of TOPBP1 to DNA double strand breaks (DSBs): TOPBP1 forms filamentous assemblies that bridge MDC1 and tether broken chromosomes during mitosis (PubMed:30898438). Required for the repair of DSBs via homologous recombination by promoting recruitment of NBN component of the MRN complex to DSBs (PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890). {ECO:0000269\|PubMed:12475977, ECO:0000269\|PubMed:12499369, ECO:0000269\|PubMed:12551934, ECO:0000269\|PubMed:12607003, ECO:0000269\|PubMed:12607004, ECO:0000269\|PubMed:12607005, ECO:0000269\|PubMed:12611903, ECO:0000269\|PubMed:14695167, ECO:0000269\|PubMed:15201865, ECO:0000269\|PubMed:15377652, ECO:0000269\|PubMed:16049003, ECO:0000269\|PubMed:16377563, ECO:0000269\|PubMed:18411307, ECO:0000269\|PubMed:18582474, ECO:0000269\|PubMed:18583988, ECO:0000269\|PubMed:18678890, ECO:0000269\|PubMed:30898438}.
Q14677	CLINT1	S305	ochoa	Clathrin interactor 1 (Clathrin-interacting protein localized in the trans-Golgi region) (Clint) (Enthoprotin) (Epsin-4) (Epsin-related protein) (EpsinR)	Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269\|PubMed:12429846, ECO:0000269\|PubMed:12538641}.
Q14677	CLINT1	S311	ochoa	Clathrin interactor 1 (Clathrin-interacting protein localized in the trans-Golgi region) (Clint) (Enthoprotin) (Epsin-4) (Epsin-related protein) (EpsinR)	Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269\|PubMed:12429846, ECO:0000269\|PubMed:12538641}.
Q14683	SMC1A	S962	ochoa	Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Sb1.8)	Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269\|PubMed:11877377}.
Q14683	SMC1A	S970	ochoa	Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Sb1.8)	Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269\|PubMed:11877377}.
Q14684	RRP1B	S341	ochoa	Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)	Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015). {ECO:0000250\|UniProtKB:Q91YK2, ECO:0000269\|PubMed:19710015, ECO:0000269\|PubMed:20040599, ECO:0000269\|PubMed:20926688}.; FUNCTION: (Microbial infection) Following influenza A virus (IAV) infection, promotes viral mRNA transcription by facilitating the binding of IAV RNA-directed RNA polymerase to capped mRNA. {ECO:0000269\|PubMed:26311876}.
Q14684	RRP1B	S344	ochoa	Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)	Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015). {ECO:0000250\|UniProtKB:Q91YK2, ECO:0000269\|PubMed:19710015, ECO:0000269\|PubMed:20040599, ECO:0000269\|PubMed:20926688}.; FUNCTION: (Microbial infection) Following influenza A virus (IAV) infection, promotes viral mRNA transcription by facilitating the binding of IAV RNA-directed RNA polymerase to capped mRNA. {ECO:0000269\|PubMed:26311876}.
Q14684	RRP1B	S458	ochoa	Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)	Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015). {ECO:0000250\|UniProtKB:Q91YK2, ECO:0000269\|PubMed:19710015, ECO:0000269\|PubMed:20040599, ECO:0000269\|PubMed:20926688}.; FUNCTION: (Microbial infection) Following influenza A virus (IAV) infection, promotes viral mRNA transcription by facilitating the binding of IAV RNA-directed RNA polymerase to capped mRNA. {ECO:0000269\|PubMed:26311876}.
Q14684	RRP1B	S630	ochoa	Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)	Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015). {ECO:0000250\|UniProtKB:Q91YK2, ECO:0000269\|PubMed:19710015, ECO:0000269\|PubMed:20040599, ECO:0000269\|PubMed:20926688}.; FUNCTION: (Microbial infection) Following influenza A virus (IAV) infection, promotes viral mRNA transcription by facilitating the binding of IAV RNA-directed RNA polymerase to capped mRNA. {ECO:0000269\|PubMed:26311876}.
Q14687	GSE1	S84	ochoa	Genetic suppressor element 1	None
Q14687	GSE1	S87	ochoa	Genetic suppressor element 1	None
Q14692	BMS1	S558	ochoa	Ribosome biogenesis protein BMS1 homolog (EC 3.6.5.-) (Ribosome assembly protein BMS1 homolog)	GTPase required for the synthesis of 40S ribosomal subunits and for processing of pre-ribosomal RNA (pre-rRNA) at sites A0, A1, and A2. Controls access of pre-rRNA intermediates to RCL1 during ribosome biogenesis by binding RCL1 in a GTP-dependent manner, and delivering it to pre-ribosomes. GTP-binding and/or GTP hydrolysis may induce conformational rearrangements within the BMS1-RCL1 complex allowing the interaction of RCL1 with its RNA substrate. Required for RCL1 import into the nucleus. {ECO:0000250\|UniProtKB:Q08965}.
Q14699	RFTN1	S174	ochoa	Raftlin (Cell migration-inducing gene 2 protein) (Raft-linking protein)	Involved in protein trafficking via association with clathrin and AP2 complex (PubMed:21266579, PubMed:27022195). Upon bacterial lipopolysaccharide stimulation, mediates internalization of TLR4 to endosomes in dendritic cells and macrophages; and internalization of poly(I:C) to TLR3-positive endosomes in myeloid dendritic cells and epithelial cells; resulting in activation of TICAM1-mediated signaling and subsequent IFNB1 production (PubMed:21266579, PubMed:27022195). Involved in T-cell antigen receptor-mediated signaling by regulating tyrosine kinase LCK localization, T-cell dependent antibody production and cytokine secretion (By similarity). May regulate B-cell antigen receptor-mediated signaling (PubMed:12805216). May play a pivotal role in the formation and/or maintenance of lipid rafts (PubMed:12805216). {ECO:0000250\|UniProtKB:Q6A0D4, ECO:0000269\|PubMed:12805216, ECO:0000269\|PubMed:21266579, ECO:0000269\|PubMed:27022195}.
Q14738	PPP2R5D	S95	ochoa	Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta)	The B regulatory subunit might modulate substrate selectivity and catalytic activity, and might also direct the localization of the catalytic enzyme to a particular subcellular compartment.
Q14739	LBR	S160	ochoa	Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (LMN2R) (Lamin-B receptor) (Sterol C14-reductase)	Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963). {ECO:0000250\|UniProtKB:Q3U9G9, ECO:0000269\|PubMed:10828963, ECO:0000269\|PubMed:12618959, ECO:0000269\|PubMed:16784888, ECO:0000269\|PubMed:21327084, ECO:0000269\|PubMed:27336722, ECO:0000269\|PubMed:9630650}.
Q14789	GOLGB1	S543	ochoa	Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin)	May participate in forming intercisternal cross-bridges of the Golgi complex.
Q14789	GOLGB1	S2878	ochoa	Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin)	May participate in forming intercisternal cross-bridges of the Golgi complex.
Q14789	GOLGB1	S3016	ochoa	Golgin subfamily B member 1 (372 kDa Golgi complex-associated protein) (GCP372) (Giantin) (Macrogolgin)	May participate in forming intercisternal cross-bridges of the Golgi complex.
Q147X3	NAA30	S196	ochoa	N-alpha-acetyltransferase 30 (EC 2.3.1.256) (N-acetyltransferase 12) (N-acetyltransferase MAK3 homolog) (NatC catalytic subunit)	Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex (PubMed:19398576, PubMed:37891180). Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly (PubMed:19398576, PubMed:37891180). N-terminal acetylation protects proteins from ubiquitination and degradation by the N-end rule pathway (PubMed:37891180). Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate (PubMed:19398576). {ECO:0000269\|PubMed:19398576, ECO:0000269\|PubMed:37891180}.
Q14807	KIF22	S427	ochoa\|psp	Kinesin-like protein KIF22 (Kinesin-like DNA-binding protein) (Kinesin-like protein 4)	Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). Plays a role in congression of laterally attached chromosomes in NDC80-depleted cells (PubMed:25743205). {ECO:0000250\|UniProtKB:Q9I869, ECO:0000269\|PubMed:25743205}.
Q14849	STARD3	S209	ochoa\|psp	StAR-related lipid transfer protein 3 (Metastatic lymph node gene 64 protein) (MLN 64) (Protein CAB1) (START domain-containing protein 3) (StARD3)	Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:11053434, PubMed:15930133, PubMed:22514632, PubMed:28377464, PubMed:33124732). The sterol transport mechanism is triggered by phosphorylation of FFAT motif that leads to membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB (PubMed:24105263, PubMed:28377464, PubMed:33124732). Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes (PubMed:28377464). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (PubMed:12070139, PubMed:19965586). However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:28377464). Does not activate transcriptional cholesterol sensing (PubMed:28377464). Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina (PubMed:21322544). {ECO:0000269\|PubMed:11053434, ECO:0000269\|PubMed:12070139, ECO:0000269\|PubMed:15930133, ECO:0000269\|PubMed:19965586, ECO:0000269\|PubMed:21322544, ECO:0000269\|PubMed:22514632, ECO:0000269\|PubMed:24105263, ECO:0000269\|PubMed:28377464, ECO:0000269\|PubMed:33124732}.
Q14934	NFATC4	S278	ochoa	Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)	Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems (PubMed:11514544, PubMed:11997522, PubMed:17213202, PubMed:17875713, PubMed:18668201, PubMed:25663301, PubMed:7749981). Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4 (PubMed:18347059, PubMed:18668201, PubMed:7749981). Along with NFATC3, involved in embryonic heart development. Following JAK/STAT signaling activation and as part of a complex with NFATC3 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity). Involved in mitochondrial energy metabolism required for cardiac morphogenesis and function (By similarity). Transactivates many genes involved in the cardiovascular system, including AGTR2, NPPB/BNP (in synergy with GATA4), NPPA/ANP/ANF and MYH7/beta-MHC (By similarity). Involved in the regulation of adult hippocampal neurogenesis. Involved in BDNF-driven pro-survival signaling in hippocampal adult-born neurons. Involved in the formation of long-term spatial memory and long-term potentiation (By similarity). In cochlear nucleus neurons, may play a role in deafferentation-induced apoptosis during the developmental critical period, when auditory neurons depend on afferent input for survival (By similarity). Binds to and activates the BACE1/Beta-secretase 1 promoter, hence may regulate the proteolytic processing of the amyloid precursor protein (APP) (PubMed:25663301). Plays a role in adipocyte differentiation (PubMed:11997522). May be involved in myoblast differentiation into myotubes (PubMed:17213202). Binds the consensus DNA sequence 5'-GGAAAAT-3' (Probable). In the presence of CREBBP, activates TNF transcription (PubMed:11514544). Binds to PPARG gene promoter and regulates its activity (PubMed:11997522). Binds to PPARG and REG3G gene promoters (By similarity). {ECO:0000250\|UniProtKB:D3Z9H7, ECO:0000250\|UniProtKB:Q8K120, ECO:0000269\|PubMed:11514544, ECO:0000269\|PubMed:11997522, ECO:0000269\|PubMed:17213202, ECO:0000269\|PubMed:17875713, ECO:0000269\|PubMed:18347059, ECO:0000269\|PubMed:18668201, ECO:0000269\|PubMed:25663301, ECO:0000269\|PubMed:7749981, ECO:0000305}.
Q14934	NFATC4	S279	ochoa	Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)	Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems (PubMed:11514544, PubMed:11997522, PubMed:17213202, PubMed:17875713, PubMed:18668201, PubMed:25663301, PubMed:7749981). Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4 (PubMed:18347059, PubMed:18668201, PubMed:7749981). Along with NFATC3, involved in embryonic heart development. Following JAK/STAT signaling activation and as part of a complex with NFATC3 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity). Involved in mitochondrial energy metabolism required for cardiac morphogenesis and function (By similarity). Transactivates many genes involved in the cardiovascular system, including AGTR2, NPPB/BNP (in synergy with GATA4), NPPA/ANP/ANF and MYH7/beta-MHC (By similarity). Involved in the regulation of adult hippocampal neurogenesis. Involved in BDNF-driven pro-survival signaling in hippocampal adult-born neurons. Involved in the formation of long-term spatial memory and long-term potentiation (By similarity). In cochlear nucleus neurons, may play a role in deafferentation-induced apoptosis during the developmental critical period, when auditory neurons depend on afferent input for survival (By similarity). Binds to and activates the BACE1/Beta-secretase 1 promoter, hence may regulate the proteolytic processing of the amyloid precursor protein (APP) (PubMed:25663301). Plays a role in adipocyte differentiation (PubMed:11997522). May be involved in myoblast differentiation into myotubes (PubMed:17213202). Binds the consensus DNA sequence 5'-GGAAAAT-3' (Probable). In the presence of CREBBP, activates TNF transcription (PubMed:11514544). Binds to PPARG gene promoter and regulates its activity (PubMed:11997522). Binds to PPARG and REG3G gene promoters (By similarity). {ECO:0000250\|UniProtKB:D3Z9H7, ECO:0000250\|UniProtKB:Q8K120, ECO:0000269\|PubMed:11514544, ECO:0000269\|PubMed:11997522, ECO:0000269\|PubMed:17213202, ECO:0000269\|PubMed:17875713, ECO:0000269\|PubMed:18347059, ECO:0000269\|PubMed:18668201, ECO:0000269\|PubMed:25663301, ECO:0000269\|PubMed:7749981, ECO:0000305}.
Q14934	NFATC4	S295	ochoa	Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)	Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems (PubMed:11514544, PubMed:11997522, PubMed:17213202, PubMed:17875713, PubMed:18668201, PubMed:25663301, PubMed:7749981). Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4 (PubMed:18347059, PubMed:18668201, PubMed:7749981). Along with NFATC3, involved in embryonic heart development. Following JAK/STAT signaling activation and as part of a complex with NFATC3 and STAT3, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity). Involved in mitochondrial energy metabolism required for cardiac morphogenesis and function (By similarity). Transactivates many genes involved in the cardiovascular system, including AGTR2, NPPB/BNP (in synergy with GATA4), NPPA/ANP/ANF and MYH7/beta-MHC (By similarity). Involved in the regulation of adult hippocampal neurogenesis. Involved in BDNF-driven pro-survival signaling in hippocampal adult-born neurons. Involved in the formation of long-term spatial memory and long-term potentiation (By similarity). In cochlear nucleus neurons, may play a role in deafferentation-induced apoptosis during the developmental critical period, when auditory neurons depend on afferent input for survival (By similarity). Binds to and activates the BACE1/Beta-secretase 1 promoter, hence may regulate the proteolytic processing of the amyloid precursor protein (APP) (PubMed:25663301). Plays a role in adipocyte differentiation (PubMed:11997522). May be involved in myoblast differentiation into myotubes (PubMed:17213202). Binds the consensus DNA sequence 5'-GGAAAAT-3' (Probable). In the presence of CREBBP, activates TNF transcription (PubMed:11514544). Binds to PPARG gene promoter and regulates its activity (PubMed:11997522). Binds to PPARG and REG3G gene promoters (By similarity). {ECO:0000250\|UniProtKB:D3Z9H7, ECO:0000250\|UniProtKB:Q8K120, ECO:0000269\|PubMed:11514544, ECO:0000269\|PubMed:11997522, ECO:0000269\|PubMed:17213202, ECO:0000269\|PubMed:17875713, ECO:0000269\|PubMed:18347059, ECO:0000269\|PubMed:18668201, ECO:0000269\|PubMed:25663301, ECO:0000269\|PubMed:7749981, ECO:0000305}.
Q14938	NFIX	S250	ochoa	Nuclear factor 1 X-type (NF1-X) (Nuclear factor 1/X) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/X) (NF-I/X) (NFI-X) (TGGCA-binding protein)	Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Q14966	ZNF638	S289	ochoa	Zinc finger protein 638 (Cutaneous T-cell lymphoma-associated antigen se33-1) (CTCL-associated antigen se33-1) (Nuclear protein 220) (Zinc finger matrin-like protein)	Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250\|UniProtKB:Q61464, ECO:0000269\|PubMed:30487602, ECO:0000269\|PubMed:8647861}.
Q14966	ZNF638	S630	ochoa	Zinc finger protein 638 (Cutaneous T-cell lymphoma-associated antigen se33-1) (CTCL-associated antigen se33-1) (Nuclear protein 220) (Zinc finger matrin-like protein)	Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250\|UniProtKB:Q61464, ECO:0000269\|PubMed:30487602, ECO:0000269\|PubMed:8647861}.
Q14966	ZNF638	S636	ochoa	Zinc finger protein 638 (Cutaneous T-cell lymphoma-associated antigen se33-1) (CTCL-associated antigen se33-1) (Nuclear protein 220) (Zinc finger matrin-like protein)	Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250\|UniProtKB:Q61464, ECO:0000269\|PubMed:30487602, ECO:0000269\|PubMed:8647861}.
Q14978	NOLC1	S132	ochoa	Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) (Hepatitis C virus NS5A-transactivated protein 13) (HCV NS5A-transactivated protein 13) (Nucleolar 130 kDa protein) (Nucleolar phosphoprotein p130)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:10567578, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:9016786). It has intrinsic GTPase and ATPase activities (PubMed:9016786). {ECO:0000269\|PubMed:10567578, ECO:0000269\|PubMed:26399832, ECO:0000269\|PubMed:9016786}.
Q14978	NOLC1	S133	ochoa	Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) (Hepatitis C virus NS5A-transactivated protein 13) (HCV NS5A-transactivated protein 13) (Nucleolar 130 kDa protein) (Nucleolar phosphoprotein p130)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:10567578, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:9016786). It has intrinsic GTPase and ATPase activities (PubMed:9016786). {ECO:0000269\|PubMed:10567578, ECO:0000269\|PubMed:26399832, ECO:0000269\|PubMed:9016786}.
Q14980	NUMA1	S83	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1840	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1853	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1862	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14BN4	SLMAP	S458	ochoa	Sarcolemmal membrane-associated protein (Sarcolemmal-associated protein)	Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex, forming the extended (SIKE1:SLMAP)STRIPAK complex (PubMed:29063833, PubMed:30622739). The (SIKE1:SLMAP)STRIPAK complex dephosphorylates STK3 leading to the inhibition of Hippo signaling and the control of cell growth (PubMed:29063833, PubMed:30622739). May play a role during myoblast fusion (By similarity). {ECO:0000250\|UniProtKB:Q3URD3, ECO:0000269\|PubMed:29063833, ECO:0000269\|PubMed:30622739}.
Q15003	NCAPH	S87	ochoa	Condensin complex subunit 2 (Barren homolog protein 1) (Chromosome-associated protein H) (hCAP-H) (Non-SMC condensin I complex subunit H) (XCAP-H homolog)	Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). {ECO:0000269\|PubMed:11136719, ECO:0000269\|PubMed:27737959}.
Q15004	PCLAF	S37	ochoa	PCNA-associated factor (Hepatitis C virus NS5A-transactivated protein 9) (HCV NS5A-transactivated protein 9) (Overexpressed in anaplastic thyroid carcinoma 1) (OEATC-1) (PCNA-associated factor of 15 kDa) (PAF15) (p15PAF) (PCNA-clamp-associated factor)	PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number. {ECO:0000269\|PubMed:21673012, ECO:0000269\|PubMed:23000965}.
Q15007	WTAP	S288	ochoa	Pre-mRNA-splicing regulator WTAP (Female-lethal(2)D homolog) (hFL(2)D) (WT1-associated protein) (Wilms tumor 1-associating protein)	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Required for accumulation of METTL3 and METTL14 to nuclear speckle (PubMed:24316715, PubMed:24407421, PubMed:24981863). Acts as a mRNA splicing regulator (PubMed:12444081). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (PubMed:17088532). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (PubMed:17095724). {ECO:0000269\|PubMed:12444081, ECO:0000269\|PubMed:17088532, ECO:0000269\|PubMed:17095724, ECO:0000269\|PubMed:24316715, ECO:0000269\|PubMed:24407421, ECO:0000269\|PubMed:24981863, ECO:0000269\|PubMed:29507755}.
Q15036	SNX17	S415	ochoa	Sorting nexin-17	Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472, PubMed:39587083). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:22492727, PubMed:28892079, PubMed:39587083). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). {ECO:0000269\|PubMed:15121882, ECO:0000269\|PubMed:15769472, ECO:0000269\|PubMed:16712798, ECO:0000269\|PubMed:19005208, ECO:0000269\|PubMed:21512128, ECO:0000269\|PubMed:22492727, ECO:0000269\|PubMed:28892079}.
Q15036	SNX17	S434	ochoa	Sorting nexin-17	Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472, PubMed:39587083). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:22492727, PubMed:28892079, PubMed:39587083). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). {ECO:0000269\|PubMed:15121882, ECO:0000269\|PubMed:15769472, ECO:0000269\|PubMed:16712798, ECO:0000269\|PubMed:19005208, ECO:0000269\|PubMed:21512128, ECO:0000269\|PubMed:22492727, ECO:0000269\|PubMed:28892079}.
Q15036	SNX17	S440	ochoa	Sorting nexin-17	Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472, PubMed:39587083). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:22492727, PubMed:28892079, PubMed:39587083). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). {ECO:0000269\|PubMed:15121882, ECO:0000269\|PubMed:15769472, ECO:0000269\|PubMed:16712798, ECO:0000269\|PubMed:19005208, ECO:0000269\|PubMed:21512128, ECO:0000269\|PubMed:22492727, ECO:0000269\|PubMed:28892079}.
Q15036	SNX17	S446	ochoa	Sorting nexin-17	Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472, PubMed:39587083). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:22492727, PubMed:28892079, PubMed:39587083). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). {ECO:0000269\|PubMed:15121882, ECO:0000269\|PubMed:15769472, ECO:0000269\|PubMed:16712798, ECO:0000269\|PubMed:19005208, ECO:0000269\|PubMed:21512128, ECO:0000269\|PubMed:22492727, ECO:0000269\|PubMed:28892079}.
Q15052	ARHGEF6	S150	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15052	ARHGEF6	S569	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15057	ACAP2	S387	ochoa	Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2)	GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). Doesn't show GAP activity for RAB35 (PubMed:30905672). {ECO:0000269\|PubMed:11062263, ECO:0000269\|PubMed:30905672}.
Q15058	KIF14	S1226	ochoa	Kinesin-like protein KIF14	Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:16648480, PubMed:24784001). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250\|UniProtKB:L0N7N1, ECO:0000269\|PubMed:15843429, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:16648480, ECO:0000269\|PubMed:23209302, ECO:0000269\|PubMed:24784001, ECO:0000269\|PubMed:24854087}.
Q15058	KIF14	S1233	ochoa	Kinesin-like protein KIF14	Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:16648480, PubMed:24784001). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250\|UniProtKB:L0N7N1, ECO:0000269\|PubMed:15843429, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:16648480, ECO:0000269\|PubMed:23209302, ECO:0000269\|PubMed:24784001, ECO:0000269\|PubMed:24854087}.
Q15149	PLEC	S4390	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4392	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4406	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4613	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4622	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4626	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4648	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15149	PLEC	S4657	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15276	RABEP1	S416	ochoa	Rab GTPase-binding effector protein 1 (Rabaptin-4) (Rabaptin-5) (Rabaptin-5alpha) (Renal carcinoma antigen NY-REN-17)	Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane (PubMed:22841712). Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium (By similarity). {ECO:0000250\|UniProtKB:O35551, ECO:0000269\|PubMed:10698684, ECO:0000269\|PubMed:11452015, ECO:0000269\|PubMed:12773381, ECO:0000269\|PubMed:22841712, ECO:0000269\|PubMed:8521472}.
Q15398	DLGAP5	S624	ochoa	Disks large-associated protein 5 (DAP-5) (Discs large homolog 7) (Disks large-associated protein DLG7) (Hepatoma up-regulated protein) (HURP)	Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269\|PubMed:12527899, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15145941}.
Q15398	DLGAP5	S630	ochoa	Disks large-associated protein 5 (DAP-5) (Discs large homolog 7) (Disks large-associated protein DLG7) (Hepatoma up-regulated protein) (HURP)	Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269\|PubMed:12527899, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15145941}.
Q15398	DLGAP5	S812	ochoa	Disks large-associated protein 5 (DAP-5) (Discs large homolog 7) (Disks large-associated protein DLG7) (Hepatoma up-regulated protein) (HURP)	Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269\|PubMed:12527899, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15145941}.
Q15418	RPS6KA1	S369	ochoa	Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1 (PubMed:10679322, PubMed:12213813, PubMed:15117958, PubMed:16223362, PubMed:17360704, PubMed:18722121, PubMed:26158630, PubMed:35772404, PubMed:9430688). In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes (PubMed:18508509, PubMed:18813292). In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:12213813, PubMed:16223362). Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:18508509, PubMed:18813292). Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex (PubMed:17360704). In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:16763566). Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway (PubMed:15342917). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:10679322, PubMed:16213824). Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:11684016). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (PubMed:18508509, PubMed:18813292). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (PubMed:18508509, PubMed:18813292). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630). In response to mTORC1 activation, phosphorylates EIF4B at 'Ser-406' and 'Ser-422' which stimulates bicarbonate cotransporter SLC4A7 mRNA translation, increasing SLC4A7 protein abundance and function (PubMed:35772404). {ECO:0000269\|PubMed:10679322, ECO:0000269\|PubMed:11684016, ECO:0000269\|PubMed:12213813, ECO:0000269\|PubMed:15117958, ECO:0000269\|PubMed:15342917, ECO:0000269\|PubMed:16213824, ECO:0000269\|PubMed:16223362, ECO:0000269\|PubMed:16763566, ECO:0000269\|PubMed:17360704, ECO:0000269\|PubMed:18722121, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:26158630, ECO:0000269\|PubMed:35772404, ECO:0000269\|PubMed:9430688, ECO:0000303\|PubMed:18508509, ECO:0000303\|PubMed:18813292}.; FUNCTION: (Microbial infection) Promotes the late transcription and translation of viral lytic genes during Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, when constitutively activated. {ECO:0000269\|PubMed:30842327}.
Q15424	SAFB	S283	ochoa	Scaffold attachment factor B1 (SAF-B) (SAF-B1) (HSP27 estrogen response element-TATA box-binding protein) (HSP27 ERE-TATA-binding protein)	Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (PubMed:9671816). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (PubMed:12660241). Thereby acts as a negative regulator of cell proliferation (PubMed:12660241). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). {ECO:0000250\|UniProtKB:D3YXK2, ECO:0000269\|PubMed:12660241, ECO:0000269\|PubMed:9671816}.
Q15554	TERF2	S416	ochoa	Telomeric repeat-binding factor 2 (TTAGGG repeat-binding factor 2) (Telomeric DNA-binding protein)	Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:15608617, PubMed:16166375, PubMed:20655466, PubMed:28216226, PubMed:9326950, PubMed:9326951, PubMed:9476899). In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375). Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (PubMed:16166375). Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (PubMed:20655466). Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:20655466, PubMed:28216226). Preferentially binds to positive supercoiled DNA (PubMed:15608617, PubMed:20655466). Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (PubMed:20655466). Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length (By similarity). {ECO:0000250\|UniProtKB:O35144, ECO:0000269\|PubMed:15608617, ECO:0000269\|PubMed:16166375, ECO:0000269\|PubMed:20655466, ECO:0000269\|PubMed:28216226, ECO:0000269\|PubMed:9326950, ECO:0000269\|PubMed:9326951, ECO:0000269\|PubMed:9476899}.
Q15555	MAPRE2	S222	ochoa	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15555	MAPRE2	S229	ochoa	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15555	MAPRE2	S236	ochoa\|psp	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15642	TRIP10	S304	ochoa	Cdc42-interacting protein 4 (Protein Felic) (Salt tolerant protein) (hSTP) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10)	Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269\|PubMed:11069762, ECO:0000269\|PubMed:16318909, ECO:0000269\|PubMed:16326391}.
Q15642	TRIP10	S506	ochoa	Cdc42-interacting protein 4 (Protein Felic) (Salt tolerant protein) (hSTP) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10)	Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269\|PubMed:11069762, ECO:0000269\|PubMed:16318909, ECO:0000269\|PubMed:16326391}.
Q15648	MED1	S1140	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1143	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1147	psp	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1229	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1232	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1439	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1453	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15652	JMJD1C	S384	ochoa	Probable JmjC domain-containing histone demethylation protein 2C (EC 1.14.11.-) (Jumonji domain-containing protein 1C) (Thyroid receptor-interacting protein 8) (TR-interacting protein 8) (TRIP-8)	Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). {ECO:0000250}.
Q15678	PTPN14	S438	ochoa	Tyrosine-protein phosphatase non-receptor type 14 (EC 3.1.3.48) (Protein-tyrosine phosphatase pez)	Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. {ECO:0000269\|PubMed:10934049, ECO:0000269\|PubMed:12808048, ECO:0000269\|PubMed:17893246, ECO:0000269\|PubMed:20826270, ECO:0000269\|PubMed:22233626, ECO:0000269\|PubMed:22525271, ECO:0000269\|PubMed:22948661}.
Q15678	PTPN14	S620	ochoa	Tyrosine-protein phosphatase non-receptor type 14 (EC 3.1.3.48) (Protein-tyrosine phosphatase pez)	Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. {ECO:0000269\|PubMed:10934049, ECO:0000269\|PubMed:12808048, ECO:0000269\|PubMed:17893246, ECO:0000269\|PubMed:20826270, ECO:0000269\|PubMed:22233626, ECO:0000269\|PubMed:22525271, ECO:0000269\|PubMed:22948661}.
Q15696	ZRSR2	S355	ochoa	U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2) (Renal carcinoma antigen NY-REN-20) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 2) (U2AF35-related protein) (URP)	Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the pre-spliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing. {ECO:0000269\|PubMed:21041408, ECO:0000269\|PubMed:9237760}.
Q15722	LTB4R	S320	ochoa\|psp	Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (Chemoattractant receptor-like 1) (G-protein coupled receptor 16) (P2Y purinoceptor 7) (P2Y7)	Receptor for extracellular ATP > UTP and ADP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.
Q15723	ELF2	S369	ochoa	ETS-related transcription factor Elf-2 (E74-like factor 2) (New ETS-related factor)	Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter.; FUNCTION: Isoform 2 may function in repression of RUNX1-mediated transactivation.
Q15723	ELF2	S430	ochoa	ETS-related transcription factor Elf-2 (E74-like factor 2) (New ETS-related factor)	Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter.; FUNCTION: Isoform 2 may function in repression of RUNX1-mediated transactivation.
Q15746	MYLK	S1779	ochoa\|psp	Myosin light chain kinase, smooth muscle (MLCK) (smMLCK) (EC 2.7.11.18) (Kinase-related protein) (KRP) (Telokin) [Cleaved into: Myosin light chain kinase, smooth muscle, deglutamylated form]	Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. {ECO:0000269\|PubMed:11113114, ECO:0000269\|PubMed:11976941, ECO:0000269\|PubMed:15020676, ECO:0000269\|PubMed:15825080, ECO:0000269\|PubMed:16284075, ECO:0000269\|PubMed:16723733, ECO:0000269\|PubMed:18587400, ECO:0000269\|PubMed:18710790, ECO:0000269\|PubMed:19826488, ECO:0000269\|PubMed:20139351, ECO:0000269\|PubMed:20181817, ECO:0000269\|PubMed:20375339, ECO:0000269\|PubMed:20453870}.
Q15751	HERC1	S2726	ochoa	Probable E3 ubiquitin-protein ligase HERC1 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 1) (HECT-type E3 ubiquitin transferase HERC1) (p532) (p619)	Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269\|PubMed:15642342, ECO:0000269\|PubMed:8861955, ECO:0000269\|PubMed:9233772}.
Q15811	ITSN1	S321	ochoa	Intersectin-1 (SH3 domain-containing protein 1A) (SH3P17)	Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (PubMed:22648170). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (By similarity). Inhibits ARHGAP31 activity toward RAC1 (PubMed:11744688). {ECO:0000250\|UniProtKB:Q9WVE9, ECO:0000250\|UniProtKB:Q9Z0R4, ECO:0000269\|PubMed:11584276, ECO:0000269\|PubMed:11744688, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:29887380}.; FUNCTION: [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250\|UniProtKB:Q9Z0R4}.
Q15811	ITSN1	S989	ochoa	Intersectin-1 (SH3 domain-containing protein 1A) (SH3P17)	Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (PubMed:22648170). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (By similarity). Inhibits ARHGAP31 activity toward RAC1 (PubMed:11744688). {ECO:0000250\|UniProtKB:Q9WVE9, ECO:0000250\|UniProtKB:Q9Z0R4, ECO:0000269\|PubMed:11584276, ECO:0000269\|PubMed:11744688, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:29887380}.; FUNCTION: [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250\|UniProtKB:Q9Z0R4}.
Q15911	ZFHX3	S431	ochoa	Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3)	Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD-dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression (PubMed:11312261). Down-regulates the MUC5AC promoter in gastric cancer (PubMed:17330845). In association with RUNX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen receptor (ESR1) function by selectively competing with coactivator NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells (PubMed:20720010). {ECO:0000250\|UniProtKB:Q61329, ECO:0000269\|PubMed:11312261, ECO:0000269\|PubMed:17330845, ECO:0000269\|PubMed:20599712, ECO:0000269\|PubMed:20720010, ECO:0000269\|PubMed:25105025}.
Q16512	PKN1	S380	ochoa	Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)	PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269\|PubMed:11104762, ECO:0000269\|PubMed:12514133, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:24248594, ECO:0000269\|PubMed:8557118, ECO:0000269\|PubMed:8621664, ECO:0000269\|PubMed:9175763}.
Q16512	PKN1	S567	ochoa	Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)	PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269\|PubMed:11104762, ECO:0000269\|PubMed:12514133, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:24248594, ECO:0000269\|PubMed:8557118, ECO:0000269\|PubMed:8621664, ECO:0000269\|PubMed:9175763}.
Q16512	PKN1	S579	ochoa	Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)	PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269\|PubMed:11104762, ECO:0000269\|PubMed:12514133, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:24248594, ECO:0000269\|PubMed:8557118, ECO:0000269\|PubMed:8621664, ECO:0000269\|PubMed:9175763}.
Q16594	TAF9	S158	ochoa	Transcription initiation factor TFIID subunit 9 (RNA polymerase II TBP-associated factor subunit G) (STAF31/32) (Transcription initiation factor TFIID 31 kDa subunit) (TAFII-31) (TAFII31) (Transcription initiation factor TFIID 32 kDa subunit) (TAFII-32) (TAFII32)	The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF9 is also a component of the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex (PubMed:15899866). TAF9 and its paralog TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes (PubMed:15899866). Essential for cell viability (PubMed:15899866). May have a role in gene regulation associated with apoptosis (PubMed:15899866). {ECO:0000269\|PubMed:15899866, ECO:0000269\|PubMed:33795473}.
Q16625	OCLN	S327	ochoa	Occludin	May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. {ECO:0000269\|PubMed:19114660}.; FUNCTION: (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes. {ECO:0000269\|PubMed:19182773, ECO:0000269\|PubMed:20375010}.
Q16643	DBN1	S345	ochoa	Drebrin (Developmentally-regulated brain protein)	Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity). {ECO:0000250\|UniProtKB:Q9QXS6, ECO:0000269\|PubMed:20215400}.
Q16666	IFI16	S112	ochoa	Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)	Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269\|PubMed:11146555, ECO:0000269\|PubMed:12894224, ECO:0000269\|PubMed:14654789, ECO:0000269\|PubMed:20890285, ECO:0000269\|PubMed:21573174, ECO:0000269\|PubMed:21575908, ECO:0000269\|PubMed:22046441, ECO:0000269\|PubMed:22291595, ECO:0000269\|PubMed:23027953, ECO:0000269\|PubMed:24198334, ECO:0000269\|PubMed:24413532, ECO:0000269\|PubMed:9642285}.; FUNCTION: [Isoform IFI16-beta]: Isoform that specifically inhibits the AIM2 inflammasome (PubMed:30104205). Binds double-stranded DNA (dsDNA) in the cytoplasm, impeding its detection by AIM2 (PubMed:30104205). Also prevents the interaction between AIM2 and PYCARD/ASC via its interaction with AIM2, thereby inhibiting assembly of the AIM2 inflammasome (PubMed:30104205). This isoform also weakly induce production of type I interferon-beta (IFNB1) via its interaction with STING1 (PubMed:30104205). {ECO:0000269\|PubMed:30104205}.
Q16799	RTN1	S336	ochoa	Reticulon-1 (Neuroendocrine-specific protein)	Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. {ECO:0000269\|PubMed:15286784}.
Q16832	DDR2	S467	ochoa	Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Discoidin domain-containing receptor tyrosine kinase 2) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b)	Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as a cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. {ECO:0000269\|PubMed:16186104, ECO:0000269\|PubMed:16186108, ECO:0000269\|PubMed:17665456, ECO:0000269\|PubMed:18201965, ECO:0000269\|PubMed:20004161, ECO:0000269\|PubMed:20564243, ECO:0000269\|PubMed:20734453, ECO:0000269\|PubMed:30449416, ECO:0000269\|PubMed:9659899}.
Q18PE1	DOK7	S425	ochoa	Protein Dok-7 (Downstream of tyrosine kinase 7)	Probable muscle-intrinsic activator of MUSK that plays an essential role in neuromuscular synaptogenesis. Acts in aneural activation of MUSK and subsequent acetylcholine receptor (AchR) clustering in myotubes. Induces autophosphorylation of MUSK. {ECO:0000269\|PubMed:20603078}.
Q1ED39	KNOP1	S48	ochoa	Lysine-rich nucleolar protein 1 (Protein FAM191A) (Testis-specific gene 118 protein)	None
Q27J81	INF2	S1083	ochoa	Inverted formin-2 (HBEBP2-binding protein C)	Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.
Q2KHR3	QSER1	S1211	ochoa	Glutamine and serine-rich protein 1	Plays an essential role in the protection and maintenance of transcriptional and developmental programs. Protects many bivalent promoters and poised enhancers from hypermethylation, showing a marked preference for these regulatory elements over other types of promoters or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in a common complex to inhibit the binding of DNMT3A/3B and therefore de novo methylation. {ECO:0000269\|PubMed:33833093}.
Q2KJY2	KIF26B	S1046	ochoa	Kinesin-like protein KIF26B	Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.
Q2KJY2	KIF26B	S1500	ochoa	Kinesin-like protein KIF26B	Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.
Q2KJY2	KIF26B	S1619	ochoa	Kinesin-like protein KIF26B	Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.
Q2M1K9	ZNF423	S614	ochoa	Zinc finger protein 423 (Olf1/EBF-associated zinc finger protein) (hOAZ) (Smad- and Olf-interacting zinc finger protein)	Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. {ECO:0000269\|PubMed:10660046}.
Q2M1P5	KIF7	S458	ochoa	Kinesin-like protein KIF7	Essential for hedgehog signaling regulation: acts both as a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250\|UniProtKB:B7ZNG0, ECO:0000269\|PubMed:21633164}.
Q2M1P5	KIF7	S462	ochoa	Kinesin-like protein KIF7	Essential for hedgehog signaling regulation: acts both as a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250\|UniProtKB:B7ZNG0, ECO:0000269\|PubMed:21633164}.
Q2M1Z3	ARHGAP31	S388	ochoa	Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein)	Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269\|PubMed:12192056, ECO:0000269\|PubMed:16519628}.
Q2M1Z3	ARHGAP31	S1384	ochoa	Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein)	Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration. {ECO:0000269\|PubMed:12192056, ECO:0000269\|PubMed:16519628}.
Q2M3G4	SHROOM1	S308	ochoa	Protein Shroom1 (Apical protein 2)	May be involved in the assembly of microtubule arrays during cell elongation. {ECO:0000250}.
Q2M3G4	SHROOM1	S314	ochoa	Protein Shroom1 (Apical protein 2)	May be involved in the assembly of microtubule arrays during cell elongation. {ECO:0000250}.
Q2NKX8	ERCC6L	S1082	ochoa	DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) (PLK1-interacting checkpoint helicase) (Tumor antigen BJ-HCC-15)	DNA helicase that acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase (PubMed:17218258, PubMed:23973328). Functions as ATP-dependent DNA translocase (PubMed:23973328, PubMed:28977671). Can promote Holliday junction branch migration (in vitro) (PubMed:23973328). {ECO:0000269\|PubMed:17218258, ECO:0000269\|PubMed:23973328, ECO:0000269\|PubMed:28977671}.
Q2PPJ7	RALGAPA2	S379	ochoa	Ral GTPase-activating protein subunit alpha-2 (250 kDa substrate of Akt) (AS250) (p220)	Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.
Q2TAZ0	ATG2A	S1269	ochoa	Autophagy-related protein 2 homolog A	Lipid transfer protein involved in autophagosome assembly (PubMed:28561066, PubMed:30952800, PubMed:31271352). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:30952800, PubMed:31271352). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion (PubMed:30952800, PubMed:31271352). Lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31271352). Also regulates lipid droplets morphology and distribution within the cell (PubMed:22219374, PubMed:28561066). {ECO:0000269\|PubMed:22219374, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:30952800, ECO:0000269\|PubMed:31271352}.
Q32MZ4	LRRFIP1	S116	ochoa	Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (GC-binding factor 2) (TAR RNA-interacting protein)	Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269\|PubMed:10364563, ECO:0000269\|PubMed:14522076, ECO:0000269\|PubMed:16199883, ECO:0000269\|PubMed:19265123, ECO:0000269\|PubMed:9705290}.
Q32MZ4	LRRFIP1	S720	ochoa	Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (GC-binding factor 2) (TAR RNA-interacting protein)	Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269\|PubMed:10364563, ECO:0000269\|PubMed:14522076, ECO:0000269\|PubMed:16199883, ECO:0000269\|PubMed:19265123, ECO:0000269\|PubMed:9705290}.
Q32MZ4	LRRFIP1	S739	ochoa	Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (GC-binding factor 2) (TAR RNA-interacting protein)	Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269\|PubMed:10364563, ECO:0000269\|PubMed:14522076, ECO:0000269\|PubMed:16199883, ECO:0000269\|PubMed:19265123, ECO:0000269\|PubMed:9705290}.
Q32P44	EML3	S204	ochoa	Echinoderm microtubule-associated protein-like 3 (EMAP-3)	Regulates mitotic spindle assembly, microtubule (MT)-kinetochore attachment and chromosome separation via recruitment of HAUS augmin-like complex and TUBG1 to the existing MTs and promoting MT-based MT nucleation (PubMed:30723163). Required for proper alignnment of chromosomes during metaphase (PubMed:18445686). {ECO:0000269\|PubMed:18445686, ECO:0000269\|PubMed:30723163}.
Q3KQU3	MAP7D1	S280	ochoa	MAP7 domain-containing protein 1 (Arginine/proline-rich coiled-coil domain-containing protein 1) (Proline/arginine-rich coiled-coil domain-containing protein 1)	Microtubule-stabilizing protein involved in the control of cell motility and neurite outgrowth. Facilitate microtubule stabilization through the maintenance of acetylated stable microtubules. {ECO:0000250\|UniProtKB:A2AJI0}.
Q3KQU3	MAP7D1	S452	ochoa	MAP7 domain-containing protein 1 (Arginine/proline-rich coiled-coil domain-containing protein 1) (Proline/arginine-rich coiled-coil domain-containing protein 1)	Microtubule-stabilizing protein involved in the control of cell motility and neurite outgrowth. Facilitate microtubule stabilization through the maintenance of acetylated stable microtubules. {ECO:0000250\|UniProtKB:A2AJI0}.
Q3KR16	PLEKHG6	S543	ochoa	Pleckstrin homology domain-containing family G member 6 (PH domain-containing family G member 6) (Myosin-interacting guanine nucleotide exchange factor) (MyoGEF)	Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis. {ECO:0000269\|PubMed:16721066, ECO:0000269\|PubMed:17881735}.
Q4ADV7	RIC1	S1021	ochoa	Guanine nucleotide exchange factor subunit RIC1 (Connexin-43-interacting protein of 150 kDa) (Protein RIC1 homolog) (RAB6A-GEF complex partner protein 1)	The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP, and may thereby be required for efficient fusion of endosome-derived vesicles with the Golgi compartment (PubMed:23091056). The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors (PubMed:23091056). Required for phosphorylation and localization of GJA1 (PubMed:16112082). Is a regulator of procollagen transport and secretion, and is required for correct cartilage morphogenesis and development of the craniofacial skeleton (PubMed:31932796). {ECO:0000269\|PubMed:16112082, ECO:0000269\|PubMed:23091056, ECO:0000269\|PubMed:31932796}.
Q4G0J3	LARP7	S305	ochoa	La-related protein 7 (La ribonucleoprotein domain family member 7) (hLARP7) (P-TEFb-interaction protein for 7SK stability) (PIP7S)	RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function (PubMed:18249148, PubMed:32017898). Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (PubMed:18249148, PubMed:18483487). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:18249148, PubMed:18483487). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (PubMed:18281698, PubMed:18483487). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing (PubMed:32017898). Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (PubMed:32017898). U6 snRNA processing is required for spermatogenesis (By similarity). {ECO:0000250\|UniProtKB:Q05CL8, ECO:0000269\|PubMed:18249148, ECO:0000269\|PubMed:18281698, ECO:0000269\|PubMed:18483487, ECO:0000269\|PubMed:28254838, ECO:0000269\|PubMed:32017898}.
Q4L180	FILIP1L	S932	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4L180	FILIP1L	S1019	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4L180	FILIP1L	S1041	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4L180	FILIP1L	S1047	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4L180	FILIP1L	S1053	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4V328	GRIPAP1	S671	ochoa	GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]	Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity). {ECO:0000250\|UniProtKB:Q9JHZ4}.; FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity. {ECO:0000269\|PubMed:17761173}.
Q4VCS5	AMOT	S319	ochoa	Angiomotin	Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. Repressor of YAP1 and WWTR1/TAZ transcription of target genes, potentially via regulation of Hippo signaling-mediated phosphorylation of YAP1 which results in its recruitment to tight junctions (PubMed:21205866). {ECO:0000269\|PubMed:11257124, ECO:0000269\|PubMed:16678097, ECO:0000269\|PubMed:21205866}.
Q52LW3	ARHGAP29	S182	ochoa	Rho GTPase-activating protein 29 (PTPL1-associated RhoGAP protein 1) (Rho-type GTPase-activating protein 29)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269\|PubMed:15752761, ECO:0000269\|PubMed:9305890}.
Q52LW3	ARHGAP29	S190	ochoa	Rho GTPase-activating protein 29 (PTPL1-associated RhoGAP protein 1) (Rho-type GTPase-activating protein 29)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269\|PubMed:15752761, ECO:0000269\|PubMed:9305890}.
Q52LW3	ARHGAP29	S578	ochoa	Rho GTPase-activating protein 29 (PTPL1-associated RhoGAP protein 1) (Rho-type GTPase-activating protein 29)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269\|PubMed:15752761, ECO:0000269\|PubMed:9305890}.
Q53EL6	PDCD4	S82	ochoa\|psp	Programmed cell death protein 4 (Neoplastic transformation inhibitor protein) (Nuclear antigen H731-like) (Protein 197/15a)	Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity). {ECO:0000250, ECO:0000269\|PubMed:16357133, ECO:0000269\|PubMed:16449643, ECO:0000269\|PubMed:17053147, ECO:0000269\|PubMed:18296639, ECO:0000269\|PubMed:19153607, ECO:0000269\|PubMed:19204291}.
Q53EP0	FNDC3B	S260	ochoa	Fibronectin type III domain-containing protein 3B (Factor for adipocyte differentiation 104) (HCV NS5A-binding protein 37)	May be a positive regulator of adipogenesis. {ECO:0000269\|PubMed:15564382}.
Q53F19	NCBP3	S506	ochoa	Nuclear cap-binding protein subunit 3 (Protein ELG)	Associates with NCBP1/CBP80 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. The alternative CBC is particularly important in cellular stress situations such as virus infections and the NCBP3 activity is critical to inhibit virus growth (PubMed:26382858). {ECO:0000269\|PubMed:26382858}.
Q53GG5	PDLIM3	S139	ochoa	PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein)	May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
Q53HL2	CDCA8	S244	ochoa	Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)	Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. {ECO:0000269\|PubMed:15249581, ECO:0000269\|PubMed:15260989, ECO:0000269\|PubMed:16571674, ECO:0000269\|PubMed:18243099}.
Q53QZ3	ARHGAP15	S217	ochoa	Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction. {ECO:0000269\|PubMed:12650940}.
Q53TN4	CYBRD1	S266	ochoa	Plasma membrane ascorbate-dependent reductase CYBRD1 (EC 7.2.1.3) (Cytochrome b reductase 1) (Duodenal cytochrome b) (Ferric-chelate reductase 3)	Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+) (PubMed:30272000). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe(2+), the divalent form of iron that can be transported into enterocytes (PubMed:30272000). It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration by erythrocytes in blood (PubMed:17068337). May also act as a ferrireductase in airway epithelial cells (Probable). May also function as a cupric transmembrane reductase (By similarity). {ECO:0000250\|UniProtKB:Q925G2, ECO:0000269\|PubMed:17068337, ECO:0000269\|PubMed:30272000, ECO:0000305\|PubMed:16510471}.
Q562E7	WDR81	S1118	ochoa	WD repeat-containing protein 81	Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport (PubMed:26783301). It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome (PubMed:27126989). May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated protein aggregates. In this process, may regulate the interaction of SQSTM1 with ubiquitinated proteins and also recruit MAP1LC3C (PubMed:28404643). May also be involved in maintenance of normal mitochondrial structure and organization (By similarity). {ECO:0000250\|UniProtKB:Q5ND34, ECO:0000269\|PubMed:26783301, ECO:0000269\|PubMed:27126989, ECO:0000269\|PubMed:28404643}.
Q562F6	SGO2	S1144	ochoa	Shugoshin 2 (Shugoshin-2) (Shugoshin-like 2) (Tripin)	Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By similarity). Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase. {ECO:0000250, ECO:0000269\|PubMed:16541025, ECO:0000269\|PubMed:17485487, ECO:0000269\|PubMed:20739936}.
Q562F6	SGO2	S1150	ochoa	Shugoshin 2 (Shugoshin-2) (Shugoshin-like 2) (Tripin)	Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By similarity). Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase. {ECO:0000250, ECO:0000269\|PubMed:16541025, ECO:0000269\|PubMed:17485487, ECO:0000269\|PubMed:20739936}.
Q5BKX6	SLC45A4	S339	ochoa	Solute carrier family 45 member 4	Proton-associated sucrose transporter. May be able to transport also glucose and fructose. {ECO:0000250\|UniProtKB:Q0P5V9}.
Q5BKZ1	ZNF326	S137	ochoa	DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs and DBC1)	Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. {ECO:0000269\|PubMed:22446626}.
Q5CZC0	FSIP2	S3181	ochoa	Fibrous sheath-interacting protein 2	Plays a role in spermatogenesis. {ECO:0000305\|PubMed:30137358}.
Q5D1E8	ZC3H12A	S365	ochoa	Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)	Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay (PubMed:19909337). Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation (PubMed:26320658). Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL) (By similarity). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity). Self regulates by destabilizing its own mRNA (By similarity). Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (PubMed:19909337, PubMed:22561375, PubMed:26134560, PubMed:26320658). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (PubMed:22055188). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (PubMed:22055188). Also plays a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (PubMed:24048733). Affects the overall ubiquitination of cellular proteins (By similarity). Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Also induces deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes (PubMed:24048733). Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Prevents stress granule (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock and energy deprivation (By similarity). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state (By similarity). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:16574901, PubMed:18364357). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (PubMed:19185603). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-inflammatory cytokine production (By similarity). {ECO:0000250\|UniProtKB:Q5D1E7, ECO:0000269\|PubMed:16574901, ECO:0000269\|PubMed:18364357, ECO:0000269\|PubMed:19185603, ECO:0000269\|PubMed:19909337, ECO:0000269\|PubMed:22055188, ECO:0000269\|PubMed:22561375, ECO:0000269\|PubMed:24048733, ECO:0000269\|PubMed:25861989, ECO:0000269\|PubMed:26134560, ECO:0000269\|PubMed:26320658}.; FUNCTION: (Microbial infection) Binds to Japanese encephalitis virus (JEV) and Dengue virus (DEN) RNAs. {ECO:0000269\|PubMed:23355615}.; FUNCTION: (Microbial infection) Exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species. {ECO:0000269\|PubMed:24191027}.
Q5FWE3	PRRT3	S906	ochoa	Proline-rich transmembrane protein 3	None
Q5FWE3	PRRT3	S908	ochoa	Proline-rich transmembrane protein 3	None
Q5HYJ3	FAM76B	S154	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5HYJ3	FAM76B	S157	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5HYJ3	FAM76B	S158	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5HYJ3	FAM76B	S160	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5HYJ3	FAM76B	S237	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5JRA6	MIA3	S1731	ochoa	Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)	Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum (PubMed:19269366, PubMed:27138255). Required for correct assembly of COPII coat components at endoplasmic reticulum exit sites (ERES) and for the localization of SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and PREB/SEC12 to ERES (PubMed:28442536). {ECO:0000269\|PubMed:19269366, ECO:0000269\|PubMed:27138255, ECO:0000269\|PubMed:28442536}.
Q5JRA6	MIA3	S1745	ochoa	Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)	Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum (PubMed:19269366, PubMed:27138255). Required for correct assembly of COPII coat components at endoplasmic reticulum exit sites (ERES) and for the localization of SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and PREB/SEC12 to ERES (PubMed:28442536). {ECO:0000269\|PubMed:19269366, ECO:0000269\|PubMed:27138255, ECO:0000269\|PubMed:28442536}.
Q5JSH3	WDR44	S571	ochoa	WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11)	Downstream effector for Rab11 which regulates Rab11 intracellular membrane trafficking functions such as endocytic recycling, intracellular ciliogenesis and protein export (PubMed:31204173, PubMed:32344433). ATK1-mediated phosphorylation of WDR44 induces binding to Rab11 which activates endocytic recycling of transferrin receptor back to the plasma membrane (PubMed:31204173). When bound to Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-RAB11FIP3 complex, therefore inhibiting preciliary trafficking and ciliogenesis (PubMed:31204173). Participates in neo-synthesized protein export by connecting the endoplasmic reticulum (ER) with the endosomal tubule via direct interactions with the integral ER proteins VAPA or VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route (PubMed:32344433). {ECO:0000269\|PubMed:31204173, ECO:0000269\|PubMed:32344433}.
Q5JSH3	WDR44	S574	ochoa	WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11)	Downstream effector for Rab11 which regulates Rab11 intracellular membrane trafficking functions such as endocytic recycling, intracellular ciliogenesis and protein export (PubMed:31204173, PubMed:32344433). ATK1-mediated phosphorylation of WDR44 induces binding to Rab11 which activates endocytic recycling of transferrin receptor back to the plasma membrane (PubMed:31204173). When bound to Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-RAB11FIP3 complex, therefore inhibiting preciliary trafficking and ciliogenesis (PubMed:31204173). Participates in neo-synthesized protein export by connecting the endoplasmic reticulum (ER) with the endosomal tubule via direct interactions with the integral ER proteins VAPA or VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route (PubMed:32344433). {ECO:0000269\|PubMed:31204173, ECO:0000269\|PubMed:32344433}.
Q5JSZ5	PRRC2B	S232	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5JSZ5	PRRC2B	S1489	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5JTC6	AMER1	S324	psp	APC membrane recruitment protein 1 (Amer1) (Protein FAM123B) (Wilms tumor gene on the X chromosome protein)	Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development. {ECO:0000269\|PubMed:17510365, ECO:0000269\|PubMed:17925383, ECO:0000269\|PubMed:19416806, ECO:0000269\|PubMed:21304492, ECO:0000269\|PubMed:21498506}.
Q5JTD0	TJAP1	S531	ochoa	Tight junction-associated protein 1 (Protein incorporated later into tight junctions) (Tight junction protein 4)	Plays a role in regulating the structure of the Golgi apparatus. {ECO:0000250\|UniProtKB:Q9DCD5}.
Q5JTV8	TOR1AIP1	S163	ochoa	Torsin-1A-interacting protein 1 (Lamin-associated protein 1B) (LAP1B)	Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269\|PubMed:23569223}.
Q5M775	SPECC1	S137	ochoa	Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1)	None
Q5M775	SPECC1	S366	ochoa	Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1)	None
Q5M775	SPECC1	S923	ochoa	Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1)	None
Q5M7Z0	RNFT1	S53	ochoa	E3 ubiquitin-protein ligase RNFT1 (EC 2.3.2.27) (Protein PTD016) (RING finger and transmembrane domain-containing protein 1)	E3 ubiquitin-protein ligase that acts in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, which targets misfolded proteins that accumulate in the endoplasmic reticulum (ER) for ubiquitination and subsequent proteasome-mediated degradation. Protects cells from ER stress-induced apoptosis. {ECO:0000269\|PubMed:27485036}.
Q5PRF9	SAMD4B	S281	ochoa	Protein Smaug homolog 2 (Smaug 2) (hSmaug2) (Sterile alpha motif domain-containing protein 4B) (SAM domain-containing protein 4B)	Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A. {ECO:0000269\|PubMed:20510020}.
Q5QJE6	DNTTIP2	S151	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5QJE6	DNTTIP2	S184	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5QJE6	DNTTIP2	S245	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5QJE6	DNTTIP2	S251	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5SNT2	TMEM201	S460	ochoa	Transmembrane protein 201 (Spindle-associated membrane protein 1)	Critical regulator of angiogenesis and endothelial cell (EC) migration (PubMed:35311970). Promotes the migration of endothelial cells, which is essential for angiogenesis (PubMed:35311970). Interacts with the linker of nucleoskeleton and cytoskeleton (LINC) complex, which plays a vital role in connecting the cell's cytoskeleton to the nuclear envelope (PubMed:35311970). This interaction is essential for maintaining cellular structure and facilitating the movement of endothelial cells, which is critical for proper vascular development (PubMed:35311970). Involved in nuclear movement during fibroblast polarization and migration (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery (PubMed:27541860). {ECO:0000250\|UniProtKB:A2A8U2, ECO:0000269\|PubMed:35311970, ECO:0000305\|PubMed:27541860}.; FUNCTION: [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle (PubMed:19494128). Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina (PubMed:21610090). {ECO:0000269\|PubMed:19494128, ECO:0000269\|PubMed:21610090}.
Q5SW79	CEP170	S633	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S636	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S871	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S887	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S939	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S1085	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S1216	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S1225	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S1279	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SYE7	NHSL1	S328	ochoa	NHS-like protein 1	None
Q5SYE7	NHSL1	S857	ochoa	NHS-like protein 1	None
Q5SYE7	NHSL1	S860	ochoa	NHS-like protein 1	None
Q5T0W9	FAM83B	S317	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S318	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S428	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S564	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S875	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S920	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T0W9	FAM83B	S921	ochoa	Protein FAM83B	Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269\|PubMed:22886302, ECO:0000269\|PubMed:23676467, ECO:0000269\|PubMed:23912460}.
Q5T1M5	FKBP15	S301	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1M5	FKBP15	S303	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1M5	FKBP15	S962	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1M5	FKBP15	S1145	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1M5	FKBP15	S1164	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1R4	HIVEP3	S811	ochoa	Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Zinc finger protein ZAS3)	Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Also binds to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and pro-inflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation. {ECO:0000269\|PubMed:11161801}.
Q5T200	ZC3H13	S335	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T200	ZC3H13	S346	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T200	ZC3H13	S378	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T3F8	TMEM63B	S102	ochoa	Mechanosensitive cation channel TMEM63B (Transmembrane protein 63B) (hTMEM63B)	Mechanosensitive cation channel with low conductance and high activation threshold (PubMed:37543036, PubMed:38127458). Osmosensitive cation channel preferentially activated by hypotonic stress (PubMed:37543036, PubMed:38127458). Also acts as a phospholipid scramblase in response to changes in membrane structure: upon changes in membrane curvature and thickness, alters its conformation and translocates phospholipids, such as phosphatidylcholine and sphingomyelin, thereby controlling plasma membrane lipid distribution (PubMed:39217145, PubMed:39424995, PubMed:39716028). Forms a heterodimer with SLC19A2, which mediates phospholipid scramblase activity following Ca(2+) stimulation (By similarity). Expressed in excitatory neurons of the subfornical organ and functions as a thirst receptor that mediates neuronal response to hyperosmolality to drive thirst and drinking behavior (By similarity). Facilitates intestinal motility by promoting proliferation of intestinal stem cells (By similarity). Essential for the baby's first breath and respiration throughout life (PubMed:38127458). Upon lung inflation conducts cation currents in alveolar type 1 and 2 cells triggering lamellar body exocytosis and surfactant secretion into airspace (PubMed:38127458). Acts as an osmosensor in cochlear outer hair cells (OHCs) where it mediates calcium influx and regulatory volume decrease response (By similarity). Required for the maintenance of OHC morphology, OHC survival and normal hearing (By similarity). {ECO:0000250\|UniProtKB:Q3TWI9, ECO:0000269\|PubMed:37543036, ECO:0000269\|PubMed:38127458, ECO:0000269\|PubMed:39217145, ECO:0000269\|PubMed:39424995, ECO:0000269\|PubMed:39716028}.
Q5T5P2	KIAA1217	S532	ochoa	Sickle tail protein homolog	Required for normal development of intervertebral disks. {ECO:0000250\|UniProtKB:A2AQ25}.
Q5T5P2	KIAA1217	S1033	ochoa	Sickle tail protein homolog	Required for normal development of intervertebral disks. {ECO:0000250\|UniProtKB:A2AQ25}.
Q5T5Y3	CAMSAP1	S506	ochoa	Calmodulin-regulated spectrin-associated protein 1	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:21834987, PubMed:24117850, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (PubMed:24486153, PubMed:24706919). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850). {ECO:0000269\|PubMed:19508979, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:24117850, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919}.
Q5T5Y3	CAMSAP1	S728	ochoa	Calmodulin-regulated spectrin-associated protein 1	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:21834987, PubMed:24117850, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (PubMed:24486153, PubMed:24706919). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850). {ECO:0000269\|PubMed:19508979, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:24117850, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919}.
Q5T5Y3	CAMSAP1	S1406	ochoa	Calmodulin-regulated spectrin-associated protein 1	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:21834987, PubMed:24117850, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (PubMed:24486153, PubMed:24706919). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850). {ECO:0000269\|PubMed:19508979, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:24117850, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919}.
Q5T7N3	KANK4	S636	ochoa	KN motif and ankyrin repeat domain-containing protein 4 (Ankyrin repeat domain-containing protein 38)	May be involved in the control of cytoskeleton formation by regulating actin polymerization. {ECO:0000269\|PubMed:17996375}.
Q5TAQ9	DCAF8	S27	ochoa	DDB1- and CUL4-associated factor 8 (WD repeat-containing protein 42A)	May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269\|PubMed:16949367, ECO:0000269\|PubMed:16964240}.
Q5TBA9	FRY	S1945	ochoa	Protein furry homolog	Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269\|PubMed:22753416}.
Q5TBA9	FRY	S1946	ochoa	Protein furry homolog	Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269\|PubMed:22753416}.
Q5TBA9	FRY	S2371	ochoa	Protein furry homolog	Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269\|PubMed:22753416}.
Q5TCZ1	SH3PXD2A	S644	ochoa	SH3 and PX domain-containing protein 2A (Adapter protein TKS5) (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains)	Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells (PubMed:27789576). Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide. {ECO:0000269\|PubMed:12615925, ECO:0000269\|PubMed:15710328, ECO:0000269\|PubMed:15710903, ECO:0000269\|PubMed:19755710, ECO:0000269\|PubMed:20609497, ECO:0000269\|PubMed:27789576}.
Q5TH69	ARFGEF3	S2101	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (ARFGEF family member 3)	Participates in the regulation of systemic glucose homeostasis, where it negatively regulates insulin granule biogenesis in pancreatic islet beta cells (By similarity). Also regulates glucagon granule production in pancreatic alpha cells (By similarity). Inhibits nuclear translocation of the transcriptional coregulator PHB2 and may enhance estrogen receptor alpha (ESR1) transcriptional activity in breast cancer cells (PubMed:19496786). {ECO:0000250\|UniProtKB:Q3UGY8, ECO:0000269\|PubMed:19496786}.
Q5TH69	ARFGEF3	S2103	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (ARFGEF family member 3)	Participates in the regulation of systemic glucose homeostasis, where it negatively regulates insulin granule biogenesis in pancreatic islet beta cells (By similarity). Also regulates glucagon granule production in pancreatic alpha cells (By similarity). Inhibits nuclear translocation of the transcriptional coregulator PHB2 and may enhance estrogen receptor alpha (ESR1) transcriptional activity in breast cancer cells (PubMed:19496786). {ECO:0000250\|UniProtKB:Q3UGY8, ECO:0000269\|PubMed:19496786}.
Q5TZA2	CROCC	S518	ochoa	Rootletin (Ciliary rootlet coiled-coil protein)	Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus (By similarity). Furthermore, is required for the correct positioning of the cilium basal body relative to the cell nucleus, to allow for ciliogenesis (PubMed:27623382). Contributes to centrosome cohesion before mitosis (PubMed:16203858). {ECO:0000250\|UniProtKB:Q8CJ40, ECO:0000269\|PubMed:16203858, ECO:0000269\|PubMed:27623382}.
Q5UIP0	RIF1	S989	ochoa	Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)	Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250\|UniProtKB:Q6PR54, ECO:0000269\|PubMed:15342490, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:28241136}.
Q5UIP0	RIF1	S1168	ochoa	Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)	Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250\|UniProtKB:Q6PR54, ECO:0000269\|PubMed:15342490, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:28241136}.
Q5UIP0	RIF1	S1244	ochoa	Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)	Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250\|UniProtKB:Q6PR54, ECO:0000269\|PubMed:15342490, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:28241136}.
Q5UIP0	RIF1	S1548	ochoa	Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)	Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250\|UniProtKB:Q6PR54, ECO:0000269\|PubMed:15342490, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:28241136}.
Q5UIP0	RIF1	S1709	ochoa	Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog)	Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250\|UniProtKB:Q6PR54, ECO:0000269\|PubMed:15342490, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:28241136}.
Q5VSL9	STRIP1	S341	ochoa	Striatin-interacting protein 1 (Protein FAM40A)	Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation. {ECO:0000269\|PubMed:18782753, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:30622739, ECO:0000269\|PubMed:33633399}.
Q5VSY0	GKAP1	S29	ochoa	G kinase-anchoring protein 1 (cGMP-dependent protein kinase-anchoring protein of 42 kDa)	Regulates insulin-dependent IRS1 tyrosine phosphorylation in adipocytes by modulating the availability of IRS1 to IR tyrosine kinase. Its association with IRS1 is required for insulin-induced translocation of SLC2A4 to the cell membrane. Involved in TNF-induced impairment of insulin-dependent IRS1 tyrosine phosphorylation. {ECO:0000250\|UniProtKB:Q9JMB0}.
Q5VT06	CEP350	S715	ochoa	Centrosome-associated protein 350 (Cep350) (Centrosome-associated protein of 350 kDa)	Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CPAP (PubMed:19052644). Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity (PubMed:15615782). Required for ciliation (PubMed:28659385). {ECO:0000269\|PubMed:15615782, ECO:0000269\|PubMed:16314388, ECO:0000269\|PubMed:17878239, ECO:0000269\|PubMed:19052644, ECO:0000269\|PubMed:28659385}.
Q5VT06	CEP350	S1265	ochoa	Centrosome-associated protein 350 (Cep350) (Centrosome-associated protein of 350 kDa)	Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CPAP (PubMed:19052644). Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity (PubMed:15615782). Required for ciliation (PubMed:28659385). {ECO:0000269\|PubMed:15615782, ECO:0000269\|PubMed:16314388, ECO:0000269\|PubMed:17878239, ECO:0000269\|PubMed:19052644, ECO:0000269\|PubMed:28659385}.
Q5VT25	CDC42BPA	S1635	ochoa	Serine/threonine-protein kinase MRCK alpha (EC 2.7.11.1) (CDC42-binding protein kinase alpha) (DMPK-like alpha) (Myotonic dystrophy kinase-related CDC42-binding kinase alpha) (MRCK alpha) (Myotonic dystrophy protein kinase-like alpha)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:15723050, PubMed:9092543, PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates: PPP1R12A, LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775). May play a role in TFRC-mediated iron uptake (PubMed:20188707). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (PubMed:29162624). {ECO:0000250\|UniProtKB:Q3UU96, ECO:0000269\|PubMed:11340065, ECO:0000269\|PubMed:11399775, ECO:0000269\|PubMed:15723050, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:20188707, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:29162624, ECO:0000269\|PubMed:9092543, ECO:0000269\|PubMed:9418861}.
Q5VT25	CDC42BPA	S1672	ochoa	Serine/threonine-protein kinase MRCK alpha (EC 2.7.11.1) (CDC42-binding protein kinase alpha) (DMPK-like alpha) (Myotonic dystrophy kinase-related CDC42-binding kinase alpha) (MRCK alpha) (Myotonic dystrophy protein kinase-like alpha)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:15723050, PubMed:9092543, PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates: PPP1R12A, LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775). May play a role in TFRC-mediated iron uptake (PubMed:20188707). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (PubMed:29162624). {ECO:0000250\|UniProtKB:Q3UU96, ECO:0000269\|PubMed:11340065, ECO:0000269\|PubMed:11399775, ECO:0000269\|PubMed:15723050, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:20188707, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:29162624, ECO:0000269\|PubMed:9092543, ECO:0000269\|PubMed:9418861}.
Q5VT52	RPRD2	S479	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S491	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S599	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S783	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S936	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S1143	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S1183	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VUA4	ZNF318	S653	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q5VUA4	ZNF318	S665	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q5VUA4	ZNF318	S1616	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q5VWJ9	SNX30	S73	ochoa	Sorting nexin-30	Involved in the regulation of endocytosis and in several stages of intracellular trafficking (PubMed:32513819). Together with SNX4, involved in autophagosome assembly (PubMed:32513819). {ECO:0000269\|PubMed:32513819}.
Q5VWQ8	DAB2IP	S728	ochoa\|psp	Disabled homolog 2-interacting protein (DAB2 interaction protein) (DAB2-interacting protein) (ASK-interacting protein 1) (AIP-1) (DOC-2/DAB-2 interactive protein)	Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Also plays a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to pro-inflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Also mediates TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6), Ras and RAB40C (PubMed:29156729). Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Also functions as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269\|PubMed:12813029, ECO:0000269\|PubMed:17389591, ECO:0000269\|PubMed:18292600, ECO:0000269\|PubMed:19033661, ECO:0000269\|PubMed:19903888, ECO:0000269\|PubMed:19948740, ECO:0000269\|PubMed:20080667, ECO:0000269\|PubMed:20154697, ECO:0000269\|PubMed:21700930, ECO:0000269\|PubMed:22696229, ECO:0000269\|PubMed:29156729}.
Q5VWQ8	DAB2IP	S978	ochoa	Disabled homolog 2-interacting protein (DAB2 interaction protein) (DAB2-interacting protein) (ASK-interacting protein 1) (AIP-1) (DOC-2/DAB-2 interactive protein)	Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Also plays a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to pro-inflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Also mediates TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6), Ras and RAB40C (PubMed:29156729). Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Also functions as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269\|PubMed:12813029, ECO:0000269\|PubMed:17389591, ECO:0000269\|PubMed:18292600, ECO:0000269\|PubMed:19033661, ECO:0000269\|PubMed:19903888, ECO:0000269\|PubMed:19948740, ECO:0000269\|PubMed:20080667, ECO:0000269\|PubMed:20154697, ECO:0000269\|PubMed:21700930, ECO:0000269\|PubMed:22696229, ECO:0000269\|PubMed:29156729}.
Q5VYS8	TUT7	S724	ochoa	Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 6)	Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:19703396, PubMed:25480299). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (By similarity). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299). Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (PubMed:25979828). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:25979828, PubMed:28671666). Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (PubMed:25979828). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:18172165, PubMed:19703396, PubMed:22898984, PubMed:25480299, PubMed:25979828, PubMed:28671666). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (PubMed:30122351). {ECO:0000250\|UniProtKB:Q5BLK4, ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:19703396, ECO:0000269\|PubMed:22898984, ECO:0000269\|PubMed:25480299, ECO:0000269\|PubMed:25979828, ECO:0000269\|PubMed:28671666, ECO:0000269\|PubMed:30122351}.
Q5VZ89	DENND4C	S1005	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1067	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1333	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1346	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1559	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1629	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5W0B1	OBI1	S574	ochoa	ORC ubiquitin ligase 1 (OBI1) (EC 2.3.2.27) (RING finger protein 219)	E3 ubiquitin ligase essential for DNA replication origin activation during S phase (PubMed:31160578). Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-phase (PubMed:31160578). {ECO:0000269\|PubMed:31160578}.
Q5XKK7	FAM219B	S133	ochoa	Protein FAM219B	None
Q63HR2	TNS2	S909	ochoa	Tensin-2 (EC 3.1.3.48) (C1 domain-containing phosphatase and tensin homolog) (C1-TEN) (Tensin-like C1 domain-containing phosphatase)	Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1 for binding to phosphatidylinositol 3-kinase (PI3K) which balances mTORC1 activity but high glucose conditions lead to up-regulation of TNS2, increased NPHS1 dephosphorylation and activation of mTORC1, contributing to podocyte hypertrophy and proteinuria (PubMed:28955049). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (PubMed:20069572). {ECO:0000250\|UniProtKB:Q8CGB6, ECO:0000269\|PubMed:15817639, ECO:0000269\|PubMed:20069572, ECO:0000269\|PubMed:23401856, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:28955049, ECO:0000269\|PubMed:30092354}.
Q63ZY3	KANK2	S92	ochoa	KN motif and ankyrin repeat domain-containing protein 2 (Ankyrin repeat domain-containing protein 25) (Matrix-remodeling-associated protein 3) (SRC-1-interacting protein) (SIP) (SRC-interacting protein) (SRC1-interacting protein)	Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 (PubMed:17476305). Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria (PubMed:22371500). Pro-apoptotic stimuli can induce its proteasomal degradation allowing the translocation of AIFM1 to the nucleus to induce apoptosis (PubMed:22371500). Involved in the negative control of vitamin D receptor signaling pathway (PubMed:24671081). Involved in actin stress fibers formation through its interaction with ARHGDIA and the regulation of the Rho signaling pathway (PubMed:17996375, PubMed:25961457). May thereby play a role in cell adhesion and migration, regulating for instance podocytes migration during development of the kidney (PubMed:25961457). Through the Rho signaling pathway may also regulate cell proliferation (By similarity). {ECO:0000250\|UniProtKB:Q8BX02, ECO:0000269\|PubMed:17476305, ECO:0000269\|PubMed:17996375, ECO:0000269\|PubMed:22371500, ECO:0000269\|PubMed:24671081, ECO:0000269\|PubMed:25961457}.
Q641Q2	WASHC2A	S362	ochoa	WASH complex subunit 2A	Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1 and CCDC93 as well as the retriever complex subunit VPS35L. {ECO:0000269\|PubMed:25355947, ECO:0000269\|PubMed:28892079}.
Q658Y4	FAM91A1	S346	ochoa	Protein FAM91A1	As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1. {ECO:0000269\|PubMed:29426865}.
Q659A1	ICE2	S614	ochoa	Little elongation complex subunit 2 (Interactor of little elongator complex ELL subunit 2) (NMDA receptor-regulated protein 2)	Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. {ECO:0000269\|PubMed:23932780}.
Q66K14	TBC1D9B	S438	ochoa	TBC1 domain family member 9B	May act as a GTPase-activating protein for Rab family protein(s).
Q66K14	TBC1D9B	S1138	ochoa	TBC1 domain family member 9B	May act as a GTPase-activating protein for Rab family protein(s).
Q66K74	MAP1S	S478	ochoa	Microtubule-associated protein 1S (MAP-1S) (BPY2-interacting protein 1) (Microtubule-associated protein 8) (Variable charge Y chromosome 2-interacting protein 1) (VCY2-interacting protein 1) (VCY2IP-1) [Cleaved into: MAP1S heavy chain; MAP1S light chain]	Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). {ECO:0000250, ECO:0000269\|PubMed:15899810, ECO:0000269\|PubMed:17234756}.
Q66K74	MAP1S	S646	ochoa	Microtubule-associated protein 1S (MAP-1S) (BPY2-interacting protein 1) (Microtubule-associated protein 8) (Variable charge Y chromosome 2-interacting protein 1) (VCY2-interacting protein 1) (VCY2IP-1) [Cleaved into: MAP1S heavy chain; MAP1S light chain]	Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). {ECO:0000250, ECO:0000269\|PubMed:15899810, ECO:0000269\|PubMed:17234756}.
Q674X7	KAZN	S352	ochoa	Kazrin	Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known. {ECO:0000269\|PubMed:15337775}.
Q684P5	RAP1GAP2	S643	ochoa	Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4)	GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269\|PubMed:15632203}.
Q68CP9	ARID2	S1476	ochoa	AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200)	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000269\|PubMed:16782067, ECO:0000303\|PubMed:22952240, ECO:0000303\|PubMed:26601204}.
Q68CZ2	TNS3	S959	ochoa	Tensin-3 (EC 3.1.3.-) (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)	May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115). EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115). Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433). Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433). Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021). Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841). {ECO:0000250\|UniProtKB:Q5SSZ5, ECO:0000269\|PubMed:17643115, ECO:0000269\|PubMed:26166433, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:31905841, ECO:0000269\|PubMed:35687021, ECO:0000305}.
Q68CZ2	TNS3	S1123	ochoa	Tensin-3 (EC 3.1.3.-) (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)	May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115). EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115). Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433). Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433). Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021). Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841). {ECO:0000250\|UniProtKB:Q5SSZ5, ECO:0000269\|PubMed:17643115, ECO:0000269\|PubMed:26166433, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:31905841, ECO:0000269\|PubMed:35687021, ECO:0000305}.
Q68CZ2	TNS3	S1128	ochoa	Tensin-3 (EC 3.1.3.-) (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)	May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115). EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115). Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433). Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433). Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021). Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841). {ECO:0000250\|UniProtKB:Q5SSZ5, ECO:0000269\|PubMed:17643115, ECO:0000269\|PubMed:26166433, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:31905841, ECO:0000269\|PubMed:35687021, ECO:0000305}.
Q68DK2	ZFYVE26	S1768	ochoa	Zinc finger FYVE domain-containing protein 26 (FYVE domain-containing centrosomal protein) (FYVE-CENT) (Spastizin)	Phosphatidylinositol 3-phosphate-binding protein required for the abscission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abscission. May also be required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269\|PubMed:20208530}.
Q69YH5	CDCA2	S936	ochoa	Cell division cycle-associated protein 2 (Recruits PP1 onto mitotic chromatin at anaphase protein) (Repo-Man)	Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates. {ECO:0000269\|PubMed:16492807, ECO:0000269\|PubMed:16998479}.
Q69YQ0	SPECC1L	S887	ochoa	Cytospin-A (Renal carcinoma antigen NY-REN-22) (Sperm antigen with calponin homology and coiled-coil domains 1-like) (SPECC1-like protein)	Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration. {ECO:0000269\|PubMed:21703590}.
Q69YQ0	SPECC1L	S893	ochoa	Cytospin-A (Renal carcinoma antigen NY-REN-22) (Sperm antigen with calponin homology and coiled-coil domains 1-like) (SPECC1-like protein)	Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration. {ECO:0000269\|PubMed:21703590}.
Q6AI08	HEATR6	S395	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6AI08	HEATR6	S396	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6AI08	HEATR6	S402	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6DCA0	AMMECR1L	S33	ochoa	AMMECR1-like protein	None
Q6FI81	CIAPIN1	S183	ochoa	Anamorsin (Cytokine-induced apoptosis inhibitor 1) (Fe-S cluster assembly protein DRE2 homolog)	Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1 (PubMed:23596212). NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity). {ECO:0000250\|UniProtKB:P36152, ECO:0000250\|UniProtKB:Q8WTY4, ECO:0000255\|HAMAP-Rule:MF_03115, ECO:0000269\|PubMed:23596212}.
Q6FIF0	ZFAND6	S182	ochoa	AN1-type zinc finger protein 6 (Associated with PRK1 protein) (Zinc finger A20 domain-containing protein 3)	Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'-linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1. Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes (By similarity). {ECO:0000250, ECO:0000269\|PubMed:19285159, ECO:0000269\|PubMed:21810480}.
Q6H8Q1	ABLIM2	S285	ochoa	Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2)	May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269\|PubMed:17194709}.
Q6H8Q1	ABLIM2	S370	ochoa	Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2)	May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269\|PubMed:17194709}.
Q6IA17	SIGIRR	S382	ochoa	Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)	Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP. {ECO:0000269\|PubMed:12925853, ECO:0000269\|PubMed:14715412, ECO:0000269\|PubMed:15866876, ECO:0000269\|PubMed:25963006}.
Q6IEG0	SNRNP48	S283	ochoa	U11/U12 small nuclear ribonucleoprotein 48 kDa protein (U11/U12 snRNP 48 kDa protein) (U11/U12-48K)	Likely involved in U12-type 5' splice site recognition. {ECO:0000269\|PubMed:19217400}.
Q6IN85	PPP4R3A	S783	ochoa	Serine/threonine-protein phosphatase 4 regulatory subunit 3A (SMEK homolog 1)	Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA DSB repair. {ECO:0000269\|PubMed:18614045}.
Q6IQ23	PLEKHA7	S124	ochoa	Pleckstrin homology domain-containing family A member 7 (PH domain-containing family A member 7)	Required for zonula adherens biogenesis and maintenance (PubMed:19041755). Acts via its interaction with CAMSAP3, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site (PubMed:19041755). Mediates docking of ADAM10 to zonula adherens through a PDZD11-dependent interaction with the ADAM10-binding protein TSPAN33 (PubMed:30463011). {ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:30463011}.
Q6IQ55	TTBK2	S428	ochoa	Tau-tubulin kinase 2 (EC 2.7.11.1)	Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro (PubMed:23141541). Phosphorylates MPHOSPH9 which promotes its ubiquitination and proteasomal degradation, loss of MPHOSPH9 facilitates the removal of the CP110-CEP97 complex (a negative regulator of ciliogenesis) from the mother centrioles, promoting the initiation of ciliogenesis (PubMed:30375385). Required for recruitment of CPLANE2 and INTU to the mother centriole (By similarity). {ECO:0000250\|UniProtKB:Q3UVR3, ECO:0000269\|PubMed:21548880, ECO:0000269\|PubMed:23141541, ECO:0000269\|PubMed:30375385}.
Q6L8Q7	PDE12	S223	ochoa	2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4)	Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of oligoadenylates (PubMed:21666256, PubMed:26055709, PubMed:30389976). Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells (PubMed:26055709). {ECO:0000269\|PubMed:15231837, ECO:0000269\|PubMed:21245038, ECO:0000269\|PubMed:21666256, ECO:0000269\|PubMed:22285541, ECO:0000269\|PubMed:26055709, ECO:0000269\|PubMed:30389976}.
Q6N021	TET2	S21	ochoa	Methylcytosine dioxygenase TET2 (EC 1.14.11.80)	Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269\|PubMed:19483684, ECO:0000269\|PubMed:21057493, ECO:0000269\|PubMed:21817016, ECO:0000269\|PubMed:23222540, ECO:0000269\|PubMed:23353889, ECO:0000269\|PubMed:24315485, ECO:0000269\|PubMed:32518946}.
Q6N021	TET2	S75	ochoa	Methylcytosine dioxygenase TET2 (EC 1.14.11.80)	Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT. {ECO:0000269\|PubMed:19483684, ECO:0000269\|PubMed:21057493, ECO:0000269\|PubMed:21817016, ECO:0000269\|PubMed:23222540, ECO:0000269\|PubMed:23353889, ECO:0000269\|PubMed:24315485, ECO:0000269\|PubMed:32518946}.
Q6N043	ZNF280D	S527	ochoa	Zinc finger protein 280D (Suppressor of hairy wing homolog 4) (Zinc finger protein 634)	May function as a transcription factor.
Q6NUJ5	PWWP2B	S453	ochoa	PWWP domain-containing protein 2B	Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260). Plays a role in facilitating transcriptional elongation through regulation of histone acetylation (By similarity). Negatively regulates brown adipocyte thermogenesis by interacting with and stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone deacetylation at the promoter leading to the repression of UCP1 expression (By similarity). {ECO:0000250\|UniProtKB:Q69Z61, ECO:0000269\|PubMed:30228260}.
Q6NV74	CRACDL	S321	ochoa	CRACD-like protein	None
Q6NV74	CRACDL	S609	ochoa	CRACD-like protein	None
Q6NXT4	SLC30A6	S388	ochoa	Zinc transporter 6 (ZnT-6) (Solute carrier family 30 member 6)	Has probably no intrinsic transporter activity but together with SLC30A5 forms a functional zinc ion:proton antiporter heterodimer, mediating zinc entry into the lumen of organelles along the secretory pathway (PubMed:15994300, PubMed:19366695, PubMed:19759014). As part of that zinc ion:proton antiporter, contributes to zinc ion homeostasis within the early secretory pathway and regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis (PubMed:15994300, PubMed:19759014, PubMed:35525268). {ECO:0000269\|PubMed:15994300, ECO:0000269\|PubMed:19366695, ECO:0000269\|PubMed:19759014, ECO:0000269\|PubMed:35525268}.
Q6P1L5	FAM117B	S414	ochoa	Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein)	None
Q6P2E9	EDC4	S729	ochoa	Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls)	In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269\|PubMed:16364915}.
Q6P2E9	EDC4	S735	ochoa	Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls)	In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269\|PubMed:16364915}.
Q6P2E9	EDC4	S774	ochoa	Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls)	In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269\|PubMed:16364915}.
Q6P2H3	CEP85	S108	ochoa	Centrosomal protein of 85 kDa (Cep85) (Coiled-coil domain-containing protein 21)	Acts as a regulator of centriole duplication through a direct interaction with STIL, a key factor involved in the early steps of centriole formation. The CEP85-STIL protein complex acts as a modulator of PLK4-driven cytoskeletal rearrangements and directional cell motility (PubMed:29712910, PubMed:32107292). Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity (PubMed:26220856). {ECO:0000269\|PubMed:26220856, ECO:0000269\|PubMed:29712910, ECO:0000269\|PubMed:32107292}.
Q6P3S6	FBXO42	S373	ochoa	F-box only protein 42 (Just one F-box and Kelch domain-containing protein)	Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Specifically recognizes p53/TP53, promoting its ubiquitination and degradation. {ECO:0000269\|PubMed:19509332}.
Q6P4F7	ARHGAP11A	S569	ochoa	Rho GTPase-activating protein 11A (Rho-type GTPase-activating protein 11A)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000269\|PubMed:27957544}.
Q6P996	PDXDC1	S724	ochoa	Pyridoxal-dependent decarboxylase domain-containing protein 1 (EC 4.1.1.-)	None
Q6P9F7	LRRC8B	S192	ochoa	Volume-regulated anion channel subunit LRRC8B (Leucine-rich repeat-containing protein 8B) (T-cell activation leucine repeat-rich protein) (TA-LRRP)	Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:24790029, PubMed:26824658, PubMed:28193731). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658, PubMed:28193731). {ECO:0000269\|PubMed:24790029, ECO:0000269\|PubMed:26824658, ECO:0000269\|PubMed:28193731}.
Q6PCB5	RSBN1L	S105	ochoa	Lysine-specific demethylase RSBN1L (EC 1.14.11.-) (Round spermatid basic protein 1-like protein)	Lysine-specific demethylase that specifically demethylates methylated lysine residues of proteins. {ECO:0000250\|UniProtKB:Q80T69}.
Q6PD62	CTR9	S1087	ochoa	RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1)	Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity). {ECO:0000250\|UniProtKB:Q62018, ECO:0000269\|PubMed:16024656, ECO:0000269\|PubMed:16307923, ECO:0000269\|PubMed:19345177, ECO:0000269\|PubMed:19952111, ECO:0000269\|PubMed:20178742, ECO:0000269\|PubMed:20541477, ECO:0000269\|PubMed:21329879}.
Q6PEY2	TUBA3E	S54	ochoa	Tubulin alpha-3E chain (EC 3.6.5.-) (Alpha-tubulin 3E) [Cleaved into: Detyrosinated tubulin alpha-3E chain]	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Q6PGQ7	BORA	S189	ochoa	Protein aurora borealis (HsBora)	Required for the activation of AURKA at the onset of mitosis. {ECO:0000269\|PubMed:16890155}.
Q6PI98	INO80C	S32	ochoa	INO80 complex subunit C (IES6 homolog) (hIes6)	Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Q6PIJ6	FBXO38	S722	ochoa	F-box only protein 38	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of PDCD1/PD-1, thereby regulating T-cells-mediated immunity (PubMed:30487606). Required for anti-tumor activity of T-cells by promoting the degradation of PDCD1/PD-1; the PDCD1-mediated inhibitory pathway being exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (PubMed:30487606). May indirectly stimulate the activity of transcription factor KLF7, a regulator of neuronal differentiation, without promoting KLF7 ubiquitination (By similarity). {ECO:0000250\|UniProtKB:Q8BMI0, ECO:0000269\|PubMed:30487606}.
Q6PJI9	WDR59	S756	ochoa	GATOR2 complex protein WDR59 (WD repeat-containing protein 59)	As a component of the GATOR2 complex, functions as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway (PubMed:23723238, PubMed:25457612, PubMed:27487210, PubMed:35831510, PubMed:36528027, PubMed:36577058). The GATOR2 complex indirectly activates mTORC1 through the inhibition of the GATOR1 subcomplex (PubMed:23723238, PubMed:27487210, PubMed:35831510, PubMed:36528027). GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 (PubMed:36528027). In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2 core component of the GATOR1 complex, leading to GATOR1 inactivation (PubMed:36528027). In the absence of amino acids, GATOR2 is inhibited, activating the GATOR1 complex (PubMed:25457612, PubMed:27487210). {ECO:0000269\|PubMed:23723238, ECO:0000269\|PubMed:25457612, ECO:0000269\|PubMed:27487210, ECO:0000269\|PubMed:35831510, ECO:0000269\|PubMed:36528027, ECO:0000269\|PubMed:36577058}.
Q6PJI9	WDR59	S822	ochoa	GATOR2 complex protein WDR59 (WD repeat-containing protein 59)	As a component of the GATOR2 complex, functions as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway (PubMed:23723238, PubMed:25457612, PubMed:27487210, PubMed:35831510, PubMed:36528027, PubMed:36577058). The GATOR2 complex indirectly activates mTORC1 through the inhibition of the GATOR1 subcomplex (PubMed:23723238, PubMed:27487210, PubMed:35831510, PubMed:36528027). GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 (PubMed:36528027). In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2 core component of the GATOR1 complex, leading to GATOR1 inactivation (PubMed:36528027). In the absence of amino acids, GATOR2 is inhibited, activating the GATOR1 complex (PubMed:25457612, PubMed:27487210). {ECO:0000269\|PubMed:23723238, ECO:0000269\|PubMed:25457612, ECO:0000269\|PubMed:27487210, ECO:0000269\|PubMed:35831510, ECO:0000269\|PubMed:36528027, ECO:0000269\|PubMed:36577058}.
Q6PKG0	LARP1	S580	ochoa	La-related protein 1 (La ribonucleoprotein domain family member 1)	RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543). {ECO:0000269\|PubMed:20430826, ECO:0000269\|PubMed:23711370, ECO:0000269\|PubMed:24532714, ECO:0000269\|PubMed:25940091, ECO:0000269\|PubMed:26206669, ECO:0000269\|PubMed:28379136, ECO:0000269\|PubMed:28650797, ECO:0000269\|PubMed:28673543, ECO:0000269\|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269\|PubMed:26735137}.
Q6PL18	ATAD2	S1283	ochoa	ATPase family AAA domain-containing protein 2 (EC 3.6.1.-) (AAA nuclear coregulator cancer-associated protein) (ANCCA)	May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. {ECO:0000269\|PubMed:17998543}.
Q6Q0C0	TRAF7	S69	ochoa	E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.-) (EC 2.3.2.27) (RING finger and WD repeat-containing protein 1) (RING finger protein 119) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7)	E3 ubiquitin and SUMO-protein ligase that plays a role in different biological processes such as innate immunity, inflammation or apoptosis (PubMed:15001576, PubMed:37086853). Potentiates MAP3K3-mediated activation of JUN/AP1 and DDIT3 transcriptional regulators (PubMed:14743216). Negatively regulates MYB transcriptional activity by sequestering it to the cytosol via SUMOylation (By similarity). Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3. Negatively regulates RLR-mediated innate immunity by promoting 'Lys-48'-linked ubiquitination of TBK1 through its RING domain to inhibit the cellular antiviral response (PubMed:37086853). Promotes 'Lys-29'-linked polyubiquitination of NEMO/IKBKG and RELA leading to targeting these two proteins to lysosomal degradative pathways, reducing the transcriptional activity of NF-kappa-B (PubMed:21518757). {ECO:0000250\|UniProtKB:Q922B6, ECO:0000269\|PubMed:14743216, ECO:0000269\|PubMed:15001576, ECO:0000269\|PubMed:21518757, ECO:0000269\|PubMed:29961569, ECO:0000269\|PubMed:37086853}.
Q6Q0C0	TRAF7	S100	ochoa	E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.-) (EC 2.3.2.27) (RING finger and WD repeat-containing protein 1) (RING finger protein 119) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7)	E3 ubiquitin and SUMO-protein ligase that plays a role in different biological processes such as innate immunity, inflammation or apoptosis (PubMed:15001576, PubMed:37086853). Potentiates MAP3K3-mediated activation of JUN/AP1 and DDIT3 transcriptional regulators (PubMed:14743216). Negatively regulates MYB transcriptional activity by sequestering it to the cytosol via SUMOylation (By similarity). Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3. Negatively regulates RLR-mediated innate immunity by promoting 'Lys-48'-linked ubiquitination of TBK1 through its RING domain to inhibit the cellular antiviral response (PubMed:37086853). Promotes 'Lys-29'-linked polyubiquitination of NEMO/IKBKG and RELA leading to targeting these two proteins to lysosomal degradative pathways, reducing the transcriptional activity of NF-kappa-B (PubMed:21518757). {ECO:0000250\|UniProtKB:Q922B6, ECO:0000269\|PubMed:14743216, ECO:0000269\|PubMed:15001576, ECO:0000269\|PubMed:21518757, ECO:0000269\|PubMed:29961569, ECO:0000269\|PubMed:37086853}.
Q6R327	RICTOR	S1284	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1286	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1577	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1587	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1591	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6S8J3	POTEE	S939	ochoa	POTE ankyrin domain family member E (ANKRD26-like family C member 1A) (Prostate, ovary, testis-expressed protein on chromosome 2) (POTE-2)	None
Q6T4R5	NHS	S477	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6T4R5	NHS	S999	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6T4R5	NHS	S1486	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6UUV7	CRTC3	S326	ochoa	CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3)	Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269\|PubMed:14506290, ECO:0000269\|PubMed:15454081, ECO:0000269\|PubMed:15466468, ECO:0000269\|PubMed:16817901, ECO:0000269\|PubMed:16980408, ECO:0000269\|PubMed:17210223, ECO:0000269\|PubMed:17644518}.
Q6UUV7	CRTC3	S327	ochoa	CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3)	Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269\|PubMed:14506290, ECO:0000269\|PubMed:15454081, ECO:0000269\|PubMed:15466468, ECO:0000269\|PubMed:16817901, ECO:0000269\|PubMed:16980408, ECO:0000269\|PubMed:17210223, ECO:0000269\|PubMed:17644518}.
Q6UUV7	CRTC3	S332	ochoa	CREB-regulated transcription coactivator 3 (Transducer of regulated cAMP response element-binding protein 3) (TORC-3) (Transducer of CREB protein 3)	Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269\|PubMed:14506290, ECO:0000269\|PubMed:15454081, ECO:0000269\|PubMed:15466468, ECO:0000269\|PubMed:16817901, ECO:0000269\|PubMed:16980408, ECO:0000269\|PubMed:17210223, ECO:0000269\|PubMed:17644518}.
Q6UXY1	BAIAP2L2	S231	ochoa	BAR/IMD domain-containing adapter protein 2-like 2 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2) (BAI1-associated protein 2-like protein 2) (Planar intestinal- and kidney-specific BAR domain protein) (Pinkbar)	Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide (By similarity). {ECO:0000250}.
Q6VMQ6	ATF7IP	S483	ochoa	Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621)	Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Required for HUSH-mediated heterochromatin formation and gene silencing (PubMed:27732843). Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1 (PubMed:12665582). Stabilizes SETDB1, is required to stimulate histone methyltransferase activity of SETDB1 and facilitates the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) (PubMed:14536086, PubMed:27732843). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells (PubMed:19106100). {ECO:0000269\|PubMed:12665582, ECO:0000269\|PubMed:14536086, ECO:0000269\|PubMed:19106100, ECO:0000269\|PubMed:27732843}.
Q6VN20	RANBP10	S375	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S418	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S419	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S420	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S421	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S422	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VY07	PACS1	S417	ochoa	Phosphofurin acidic cluster sorting protein 1 (PACS-1)	Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (By similarity). {ECO:0000250\|UniProtKB:Q8K212, ECO:0000269\|PubMed:11331585, ECO:0000269\|PubMed:15692563}.
Q6VY07	PACS1	S534	ochoa	Phosphofurin acidic cluster sorting protein 1 (PACS-1)	Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (By similarity). {ECO:0000250\|UniProtKB:Q8K212, ECO:0000269\|PubMed:11331585, ECO:0000269\|PubMed:15692563}.
Q6WCQ1	MPRIP	S187	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6WCQ1	MPRIP	S188	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6WCQ1	MPRIP	S189	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6WCQ1	MPRIP	S192	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6WCQ1	MPRIP	S625	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6XE24	RBMS3	S45	ochoa	RNA-binding motif, single-stranded-interacting protein 3	Binds poly(A) and poly(U) oligoribonucleotides. {ECO:0000269\|PubMed:10675610}.
Q6XZF7	DNMBP	S1359	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6XZF7	DNMBP	S1362	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6XZF7	DNMBP	S1436	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6ZMT1	STAC2	S234	ochoa	SH3 and cysteine-rich domain-containing protein 2 (24b2/STAC2) (Src homology 3 and cysteine-rich domain-containing protein 2)	Plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. Slows down the inactivation rate of the calcium channel CACNA1C. {ECO:0000250\|UniProtKB:Q8R1B0}.
Q6ZN16	MAP3K15	S950	ochoa	Mitogen-activated protein kinase kinase kinase 15 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 3) (MAPK/ERK kinase kinase 15) (MEK kinase 15) (MEKK 15)	Serine/threonine kinase which acts as a component of the MAP kinase signal transduction pathway (PubMed:20362554, PubMed:26732173). Once activated, acts as an upstream activator of the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases (PubMed:20362554, PubMed:26732173). May function in a signal transduction pathway that is activated by various cell stresses and leads to apoptosis (PubMed:20362554). Involved in phosphorylation of WNK4 in response to osmotic stress or hypotonic low-chloride stimulation via the p38 MAPK signal transduction cascade (PubMed:26732173). {ECO:0000269\|PubMed:20362554, ECO:0000269\|PubMed:26732173}.
Q6ZN16	MAP3K15	S952	ochoa	Mitogen-activated protein kinase kinase kinase 15 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 3) (MAPK/ERK kinase kinase 15) (MEK kinase 15) (MEKK 15)	Serine/threonine kinase which acts as a component of the MAP kinase signal transduction pathway (PubMed:20362554, PubMed:26732173). Once activated, acts as an upstream activator of the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases (PubMed:20362554, PubMed:26732173). May function in a signal transduction pathway that is activated by various cell stresses and leads to apoptosis (PubMed:20362554). Involved in phosphorylation of WNK4 in response to osmotic stress or hypotonic low-chloride stimulation via the p38 MAPK signal transduction cascade (PubMed:26732173). {ECO:0000269\|PubMed:20362554, ECO:0000269\|PubMed:26732173}.
Q6ZN18	AEBP2	S147	ochoa	Zinc finger protein AEBP2 (Adipocyte enhancer-binding protein 2) (AE-binding protein 2)	Acts as an accessory subunit for the core Polycomb repressive complex 2 (PRC2), which mediates histone H3K27 (H3K27me3) trimethylation on chromatin leading to transcriptional repression of the affected target gene (PubMed:15225548, PubMed:29499137, PubMed:31959557). Plays a role in nucleosome localization of the PRC2 complex (PubMed:29499137). {ECO:0000269\|PubMed:15225548, ECO:0000269\|PubMed:29499137, ECO:0000269\|PubMed:31959557}.
Q6ZNJ1	NBEAL2	S763	ochoa	Neurobeachin-like protein 2	Probably involved in thrombopoiesis. Plays a role in the development or secretion of alpha-granules, that contain several growth factors important for platelet biogenesis. {ECO:0000269\|PubMed:21765411, ECO:0000269\|PubMed:21765412}.
Q6ZNJ1	NBEAL2	S1836	ochoa	Neurobeachin-like protein 2	Probably involved in thrombopoiesis. Plays a role in the development or secretion of alpha-granules, that contain several growth factors important for platelet biogenesis. {ECO:0000269\|PubMed:21765411, ECO:0000269\|PubMed:21765412}.
Q6ZNL6	FGD5	S1323	ochoa	FYVE, RhoGEF and PH domain-containing protein 5 (Zinc finger FYVE domain-containing protein 23)	Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Mediates VEGF-induced CDC42 activation. May regulate proangiogenic action of VEGF in vascular endothelial cells, including network formation, directional movement and proliferation. May play a role in regulating the actin cytoskeleton and cell shape. {ECO:0000269\|PubMed:22328776}.
Q6ZRS2	SRCAP	S263	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q6ZRS2	SRCAP	S268	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q6ZRV2	FAM83H	S691	ochoa	Protein FAM83H	May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269\|PubMed:18252228, ECO:0000269\|PubMed:23902688}.
Q6ZRV2	FAM83H	S850	ochoa	Protein FAM83H	May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269\|PubMed:18252228, ECO:0000269\|PubMed:23902688}.
Q6ZRV2	FAM83H	S942	ochoa	Protein FAM83H	May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269\|PubMed:18252228, ECO:0000269\|PubMed:23902688}.
Q6ZRV2	FAM83H	S1009	ochoa	Protein FAM83H	May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269\|PubMed:18252228, ECO:0000269\|PubMed:23902688}.
Q6ZS17	RIPOR1	S357	ochoa	Rho family-interacting cell polarization regulator 1	Downstream effector protein for Rho-type small GTPases that plays a role in cell polarity and directional migration (PubMed:27807006). Acts as an adapter protein, linking active Rho proteins to STK24 and STK26 kinases, and hence positively regulates Golgi reorientation in polarized cell migration upon Rho activation (PubMed:27807006). Involved in the subcellular relocation of STK26 from the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner upon serum stimulation (PubMed:27807006). {ECO:0000269\|PubMed:27807006}.
Q6ZSR9	None	S300	ochoa	Uncharacterized protein FLJ45252	None
Q6ZT07	TBC1D9	S434	ochoa	TBC1 domain family member 9 (TBC1 domain family member 9A)	May act as a GTPase-activating protein for Rab family protein(s).
Q6ZU35	CRACD	S1143	ochoa	Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics)	Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin. {ECO:0000269\|PubMed:30361697}.
Q6ZU65	UBN2	S1108	ochoa	Ubinuclein-2	None
Q6ZUJ8	PIK3AP1	S737	ochoa	Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1)	Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269\|PubMed:15893754}.
Q6ZV73	FGD6	S1299	ochoa	FYVE, RhoGEF and PH domain-containing protein 6 (Zinc finger FYVE domain-containing protein 24)	May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}.
Q6ZVL6	KIAA1549L	S1479	ochoa	UPF0606 protein KIAA1549L	None
Q6ZW31	SYDE1	S66	ochoa	Rho GTPase-activating protein SYDE1 (Synapse defective protein 1 homolog 1) (Protein syd-1 homolog 1)	GTPase activator for the Rho-type GTPases. As a GCM1 downstream effector, it is involved in placental development and positively regulates trophoblast cells migration. It regulates cytoskeletal remodeling by controlling the activity of Rho GTPases including RHOA, CDC42 and RAC1 (PubMed:27917469). {ECO:0000269\|PubMed:27917469}.
Q70CQ2	USP34	S1469	ochoa	Ubiquitin carboxyl-terminal hydrolase 34 (EC 3.4.19.12) (Deubiquitinating enzyme 34) (Ubiquitin thioesterase 34) (Ubiquitin-specific-processing protease 34)	Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000269\|PubMed:21383061}.
Q70CQ4	USP31	S57	ochoa	Ubiquitin carboxyl-terminal hydrolase 31 (EC 3.4.19.12) (Deubiquitinating enzyme 31) (Ubiquitin thioesterase 31) (Ubiquitin-specific-processing protease 31)	Deubiquitinase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. May play a role in the regulation of NF-kappa-B signaling pathway by deubiquitinating TRAF2. {ECO:0000269\|PubMed:34184746}.; FUNCTION: (Microbial infection) Plays a positive role in foot-and-mouth disease and classical swine fever viral infection. Mechanistically, associates with internal ribosomal entry site (IRES) element within the 5'-untranslated region of viral genomes to promote translation of the virus-encoded polyprotein. {ECO:0000269\|PubMed:35468926}.
Q70CQ4	USP31	S887	ochoa	Ubiquitin carboxyl-terminal hydrolase 31 (EC 3.4.19.12) (Deubiquitinating enzyme 31) (Ubiquitin thioesterase 31) (Ubiquitin-specific-processing protease 31)	Deubiquitinase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. May play a role in the regulation of NF-kappa-B signaling pathway by deubiquitinating TRAF2. {ECO:0000269\|PubMed:34184746}.; FUNCTION: (Microbial infection) Plays a positive role in foot-and-mouth disease and classical swine fever viral infection. Mechanistically, associates with internal ribosomal entry site (IRES) element within the 5'-untranslated region of viral genomes to promote translation of the virus-encoded polyprotein. {ECO:0000269\|PubMed:35468926}.
Q70E73	RAPH1	S546	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q70E73	RAPH1	S548	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q71RC2	LARP4	S388	ochoa	La-related protein 4 (La ribonucleoprotein domain family member 4)	RNA binding protein that binds to the poly-A tract of mRNA molecules (PubMed:21098120). Associates with the 40S ribosomal subunit and with polysomes (PubMed:21098120). Plays a role in the regulation of mRNA translation (PubMed:21098120). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987, PubMed:27615744). {ECO:0000269\|PubMed:21098120, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:27615744}.
Q71RC2	LARP4	S394	ochoa	La-related protein 4 (La ribonucleoprotein domain family member 4)	RNA binding protein that binds to the poly-A tract of mRNA molecules (PubMed:21098120). Associates with the 40S ribosomal subunit and with polysomes (PubMed:21098120). Plays a role in the regulation of mRNA translation (PubMed:21098120). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987, PubMed:27615744). {ECO:0000269\|PubMed:21098120, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:27615744}.
Q71U36	TUBA1A	S54	ochoa	Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Q765P7	MTSS2	S274	ochoa	Protein MTSS 2 (Actin-bundling with BAIAP2 homology protein 1) (ABBA-1) (MTSS1-like protein)	Involved in plasma membrane dynamics. Potentiated PDGF-mediated formation of membrane ruffles and lamellipodia in fibroblasts, acting via RAC1 activation (PubMed:14752106). May function in actin bundling (PubMed:14752106). {ECO:0000269\|PubMed:14752106}.
Q765P7	MTSS2	S328	ochoa	Protein MTSS 2 (Actin-bundling with BAIAP2 homology protein 1) (ABBA-1) (MTSS1-like protein)	Involved in plasma membrane dynamics. Potentiated PDGF-mediated formation of membrane ruffles and lamellipodia in fibroblasts, acting via RAC1 activation (PubMed:14752106). May function in actin bundling (PubMed:14752106). {ECO:0000269\|PubMed:14752106}.
Q76L83	ASXL2	S1290	ochoa	Putative Polycomb group protein ASXL2 (Additional sex combs-like protein 2)	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (PubMed:30664650, PubMed:36180891). The PR-DUB complex is an epigenetic regulator of gene expression and acts as a transcriptional coactivator, affecting genes involved in development, cell communication, signaling, cell proliferation and cell viability (PubMed:30664650, PubMed:36180891). ASXL1, ASXL2 and ASXL3 function redundantly in the PR-DUB complex (By similarity) (PubMed:30664650). The ASXL proteins are essential for chromatin recruitment and transcriptional activation of associated genes (By similarity). ASXL1 and ASXL2 are important for BAP1 protein stability (PubMed:30664650). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BZ32, ECO:0000269\|PubMed:21047783, ECO:0000269\|PubMed:30664650, ECO:0000269\|PubMed:36180891}.
Q7KZI7	MARK2	S577	ochoa	Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:12429843, ECO:0000269\|PubMed:14976552, ECO:0000269\|PubMed:15158914, ECO:0000269\|PubMed:15324659, ECO:0000269\|PubMed:15365179, ECO:0000269\|PubMed:16775013, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:18626018, ECO:0000269\|PubMed:20194617, ECO:0000269\|PubMed:23666762}.
Q7L9B9	EEPD1	S25	ochoa	Endonuclease/exonuclease/phosphatase family domain-containing protein 1	None
Q7LBC6	KDM3B	S779	ochoa	Lysine-specific demethylase 3B (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3B)	Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269\|PubMed:16603237}.
Q7LBC6	KDM3B	S784	ochoa	Lysine-specific demethylase 3B (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3B)	Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269\|PubMed:16603237}.
Q7LDG7	RASGRP2	S123	ochoa	RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein)	Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269\|PubMed:10918068, ECO:0000269\|PubMed:14702343, ECO:0000269\|PubMed:17576779, ECO:0000269\|PubMed:17702895, ECO:0000269\|PubMed:24958846, ECO:0000269\|PubMed:27235135}.
Q7LDG7	RASGRP2	S397	ochoa	RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein)	Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269\|PubMed:10918068, ECO:0000269\|PubMed:14702343, ECO:0000269\|PubMed:17576779, ECO:0000269\|PubMed:17702895, ECO:0000269\|PubMed:24958846, ECO:0000269\|PubMed:27235135}.
Q7LDG7	RASGRP2	S560	ochoa	RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein)	Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. {ECO:0000269\|PubMed:10918068, ECO:0000269\|PubMed:14702343, ECO:0000269\|PubMed:17576779, ECO:0000269\|PubMed:17702895, ECO:0000269\|PubMed:24958846, ECO:0000269\|PubMed:27235135}.
Q7RTP6	MICAL3	S1352	ochoa	[F-actin]-monooxygenase MICAL3 (EC 1.14.13.225) (Molecule interacting with CasL protein 3) (MICAL-3)	Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission. {ECO:0000269\|PubMed:21596566, ECO:0000269\|PubMed:24440334}.
Q7RTP6	MICAL3	S1371	ochoa	[F-actin]-monooxygenase MICAL3 (EC 1.14.13.225) (Molecule interacting with CasL protein 3) (MICAL-3)	Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission. {ECO:0000269\|PubMed:21596566, ECO:0000269\|PubMed:24440334}.
Q7RTP6	MICAL3	S1448	ochoa	[F-actin]-monooxygenase MICAL3 (EC 1.14.13.225) (Molecule interacting with CasL protein 3) (MICAL-3)	Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission. {ECO:0000269\|PubMed:21596566, ECO:0000269\|PubMed:24440334}.
Q7RTP6	MICAL3	S1800	ochoa	[F-actin]-monooxygenase MICAL3 (EC 1.14.13.225) (Molecule interacting with CasL protein 3) (MICAL-3)	Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission. {ECO:0000269\|PubMed:21596566, ECO:0000269\|PubMed:24440334}.
Q7Z2W4	ZC3HAV1	S361	ochoa	Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)	Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of RIGI signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269\|PubMed:18225958, ECO:0000269\|PubMed:21102435, ECO:0000269\|PubMed:21876179, ECO:0000269\|PubMed:22720057}.
Q7Z2W4	ZC3HAV1	S498	ochoa	Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)	Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of RIGI signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269\|PubMed:18225958, ECO:0000269\|PubMed:21102435, ECO:0000269\|PubMed:21876179, ECO:0000269\|PubMed:22720057}.
Q7Z2Z1	TICRR	S1167	ochoa	Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein)	Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269\|PubMed:20116089}.
Q7Z2Z1	TICRR	S1352	ochoa	Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein)	Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269\|PubMed:20116089}.
Q7Z2Z1	TICRR	S1354	ochoa	Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein)	Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269\|PubMed:20116089}.
Q7Z3B3	KANSL1	S33	ochoa	KAT8 regulatory NSL complex subunit 1 (MLL1/MLL complex subunit KANSL1) (MSL1 homolog 1) (hMSL1v1) (NSL complex protein NSL1) (Non-specific lethal 1 homolog)	Non-catalytic component of the NSL histone acetyltransferase complex, a multiprotein complex that mediates histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) at transcription start sites and promotes transcription initiation (PubMed:20018852, PubMed:22547026, PubMed:33657400). The NSL complex also acts as a regulator of gene expression in mitochondria (PubMed:27768893). In addition to its role in transcription, KANSL1 also plays an essential role in spindle assembly during mitosis (PubMed:26243146). Associates with microtubule ends and contributes to microtubule stability (PubMed:26243146). {ECO:0000269\|PubMed:20018852, ECO:0000269\|PubMed:22547026, ECO:0000269\|PubMed:26243146, ECO:0000269\|PubMed:27768893, ECO:0000269\|PubMed:33657400}.
Q7Z3B3	KANSL1	S977	ochoa	KAT8 regulatory NSL complex subunit 1 (MLL1/MLL complex subunit KANSL1) (MSL1 homolog 1) (hMSL1v1) (NSL complex protein NSL1) (Non-specific lethal 1 homolog)	Non-catalytic component of the NSL histone acetyltransferase complex, a multiprotein complex that mediates histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) at transcription start sites and promotes transcription initiation (PubMed:20018852, PubMed:22547026, PubMed:33657400). The NSL complex also acts as a regulator of gene expression in mitochondria (PubMed:27768893). In addition to its role in transcription, KANSL1 also plays an essential role in spindle assembly during mitosis (PubMed:26243146). Associates with microtubule ends and contributes to microtubule stability (PubMed:26243146). {ECO:0000269\|PubMed:20018852, ECO:0000269\|PubMed:22547026, ECO:0000269\|PubMed:26243146, ECO:0000269\|PubMed:27768893, ECO:0000269\|PubMed:33657400}.
Q7Z3C6	ATG9A	S741	ochoa	Autophagy-related protein 9A (APG9-like 1) (mATG9)	Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:22456507, PubMed:27510922, PubMed:29437695, PubMed:32513819, PubMed:32610138, PubMed:33106659, PubMed:33468622, PubMed:33850023). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:16940348, PubMed:22456507, PubMed:33106659). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106659). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (PubMed:30917996). In addition to autophagy, also plays a role in necrotic cell death (By similarity). {ECO:0000250\|UniProtKB:Q68FE2, ECO:0000269\|PubMed:16940348, ECO:0000269\|PubMed:22456507, ECO:0000269\|PubMed:27510922, ECO:0000269\|PubMed:29437695, ECO:0000269\|PubMed:30917996, ECO:0000269\|PubMed:32513819, ECO:0000269\|PubMed:32610138, ECO:0000269\|PubMed:33106659, ECO:0000269\|PubMed:33468622, ECO:0000269\|PubMed:33850023}.
Q7Z3E2	CCDC186	S746	ochoa	Coiled-coil domain-containing protein 186 (CTCL tumor antigen HD-CL-01/L14-2)	None
Q7Z3J3	RGPD4	S1487	ochoa	RanBP2-like and GRIP domain-containing protein 4	None
Q7Z3J3	RGPD4	S1586	ochoa	RanBP2-like and GRIP domain-containing protein 4	None
Q7Z3J3	RGPD4	S1593	ochoa	RanBP2-like and GRIP domain-containing protein 4	None
Q7Z3K3	POGZ	S710	ochoa	Pogo transposable element with ZNF domain (Suppressor of hairy wing homolog 5) (Zinc finger protein 280E) (Zinc finger protein 635)	Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (PubMed:20562864). Promotes the repair of DNA double-strand breaks through the homologous recombination pathway (PubMed:26721387). {ECO:0000269\|PubMed:20562864, ECO:0000269\|PubMed:26721387}.
Q7Z401	DENND4A	S1099	ochoa	C-myc promoter-binding protein (DENN domain-containing protein 4A)	Probable guanine nucleotide exchange factor (GEF) which may activate RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. According to PubMed:8056341, it may bind to ISRE-like element (interferon-stimulated response element) of MYC P2 promoter. {ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:8056341}.
Q7Z417	NUFIP2	S379	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S382	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S385	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S386	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S588	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z422	SZRD1	S74	ochoa	SUZ RNA-binding domain-containing (SUZ domain-containing protein 1) (Putative MAPK-activating protein PM18/PM20/PM22)	None
Q7Z434	MAVS	S407	ochoa	Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)	Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325). {ECO:0000269\|PubMed:16125763, ECO:0000269\|PubMed:16127453, ECO:0000269\|PubMed:16153868, ECO:0000269\|PubMed:16177806, ECO:0000269\|PubMed:19631370, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20451243, ECO:0000269\|PubMed:20628368, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:23087404, ECO:0000269\|PubMed:23582325, ECO:0000269\|PubMed:25636800, ECO:0000269\|PubMed:27736772, ECO:0000269\|PubMed:27992402, ECO:0000269\|PubMed:33110251, ECO:0000269\|PubMed:33139700, ECO:0000269\|PubMed:37582970}.
Q7Z434	MAVS	S408	ochoa	Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA)	Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325). {ECO:0000269\|PubMed:16125763, ECO:0000269\|PubMed:16127453, ECO:0000269\|PubMed:16153868, ECO:0000269\|PubMed:16177806, ECO:0000269\|PubMed:19631370, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20451243, ECO:0000269\|PubMed:20628368, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:23087404, ECO:0000269\|PubMed:23582325, ECO:0000269\|PubMed:25636800, ECO:0000269\|PubMed:27736772, ECO:0000269\|PubMed:27992402, ECO:0000269\|PubMed:33110251, ECO:0000269\|PubMed:33139700, ECO:0000269\|PubMed:37582970}.
Q7Z460	CLASP1	S562	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S655	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S1091	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z4H7	HAUS6	S530	ochoa	HAUS augmin-like complex subunit 6	Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. Promotes the nucleation of microtubules from the spindle through recruitment of NEDD1 and gamma-tubulin. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19369198, ECO:0000269\|PubMed:19427217}.
Q7Z4H7	HAUS6	S914	ochoa	HAUS augmin-like complex subunit 6	Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. Promotes the nucleation of microtubules from the spindle through recruitment of NEDD1 and gamma-tubulin. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19369198, ECO:0000269\|PubMed:19427217}.
Q7Z4K8	TRIM46	S85	ochoa	Tripartite motif-containing protein 46 (Gene Y protein) (GeneY) (Tripartite, fibronectin type-III and C-terminal SPRY motif protein)	Microtubule-associated protein that is involved in the formation of parallel microtubule bundles linked by cross-bridges in the proximal axon. Required for the uniform orientation and maintenance of the parallel microtubule fascicles, which are important for efficient cargo delivery and trafficking in axons. Thereby also required for proper axon specification, the establishment of neuronal polarity and proper neuronal migration. {ECO:0000250\|UniProtKB:Q7TNM2}.
Q7Z4S6	KIF21A	S524	ochoa	Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)	Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250\|UniProtKB:Q9QXL2, ECO:0000269\|PubMed:24120883}.
Q7Z4S6	KIF21A	S530	ochoa	Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)	Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250\|UniProtKB:Q9QXL2, ECO:0000269\|PubMed:24120883}.
Q7Z4S6	KIF21A	S1229	ochoa	Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)	Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250\|UniProtKB:Q9QXL2, ECO:0000269\|PubMed:24120883}.
Q7Z4S6	KIF21A	S1231	ochoa	Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)	Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250\|UniProtKB:Q9QXL2, ECO:0000269\|PubMed:24120883}.
Q7Z4S6	KIF21A	S1310	ochoa	Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)	Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250\|UniProtKB:Q9QXL2, ECO:0000269\|PubMed:24120883}.
Q7Z4V5	HDGFL2	S236	ochoa	Hepatoma-derived growth factor-related protein 2 (HDGF-related protein 2) (HRP-2) (Hepatoma-derived growth factor 2) (HDGF-2)	Acts as an epigenetic regulator of myogenesis in cooperation with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350). Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350). Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (PubMed:26721387). Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2 (PubMed:26721387, PubMed:32459350). Involved in cellular growth control, through the regulation of cyclin D1 expression (PubMed:25689719). {ECO:0000269\|PubMed:25689719, ECO:0000269\|PubMed:26721387, ECO:0000269\|PubMed:32459350}.
Q7Z591	AKNA	S540	ochoa	Microtubule organization protein AKNA (AT-hook-containing transcription factor)	Centrosomal protein that plays a key role in cell delamination by regulating microtubule organization (By similarity). Required for the delamination and retention of neural stem cells from the subventricular zone during neurogenesis (By similarity). Also regulates the epithelial-to-mesenchymal transition in other epithelial cells (By similarity). Acts by increasing centrosomal microtubule nucleation and recruiting nucleation factors and minus-end stabilizers, thereby destabilizing microtubules at the adherens junctions and mediating constriction of the apical endfoot (By similarity). In addition, may also act as a transcription factor that specifically activates the expression of the CD40 receptor and its ligand CD40L/CD154, two cell surface molecules on lymphocytes that are critical for antigen-dependent-B-cell development (PubMed:11268217). Binds to A/T-rich promoters (PubMed:11268217). It is unclear how it can both act as a microtubule organizer and as a transcription factor; additional evidences are required to reconcile these two apparently contradictory functions (Probable). {ECO:0000250\|UniProtKB:Q80VW7, ECO:0000269\|PubMed:11268217, ECO:0000305}.
Q7Z591	AKNA	S935	ochoa	Microtubule organization protein AKNA (AT-hook-containing transcription factor)	Centrosomal protein that plays a key role in cell delamination by regulating microtubule organization (By similarity). Required for the delamination and retention of neural stem cells from the subventricular zone during neurogenesis (By similarity). Also regulates the epithelial-to-mesenchymal transition in other epithelial cells (By similarity). Acts by increasing centrosomal microtubule nucleation and recruiting nucleation factors and minus-end stabilizers, thereby destabilizing microtubules at the adherens junctions and mediating constriction of the apical endfoot (By similarity). In addition, may also act as a transcription factor that specifically activates the expression of the CD40 receptor and its ligand CD40L/CD154, two cell surface molecules on lymphocytes that are critical for antigen-dependent-B-cell development (PubMed:11268217). Binds to A/T-rich promoters (PubMed:11268217). It is unclear how it can both act as a microtubule organizer and as a transcription factor; additional evidences are required to reconcile these two apparently contradictory functions (Probable). {ECO:0000250\|UniProtKB:Q80VW7, ECO:0000269\|PubMed:11268217, ECO:0000305}.
Q7Z5J4	RAI1	S345	ochoa	Retinoic acid-induced protein 1	Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269\|PubMed:22578325}.
Q7Z5J4	RAI1	S571	ochoa	Retinoic acid-induced protein 1	Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269\|PubMed:22578325}.
Q7Z5J4	RAI1	S574	ochoa	Retinoic acid-induced protein 1	Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269\|PubMed:22578325}.
Q7Z5L9	IRF2BP2	S463	ochoa	Interferon regulatory factor 2-binding protein 2 (IRF-2-binding protein 2) (IRF-2BP2)	Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities (PubMed:12799427). Represses the NFAT1-dependent transactivation of NFAT-responsive promoters (PubMed:21576369). Acts as a coactivator of VEGFA expression in cardiac and skeletal muscles (PubMed:20702774). Plays a role in immature B-cell differentiation (PubMed:27016798). {ECO:0000269\|PubMed:12799427, ECO:0000269\|PubMed:20702774, ECO:0000269\|PubMed:21576369, ECO:0000269\|PubMed:27016798}.
Q7Z628	NET1	S38	ochoa	Neuroepithelial cell-transforming gene 1 protein (Proto-oncogene p65 Net1) (Rho guanine nucleotide exchange factor 8)	Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269\|PubMed:21373644}.
Q7Z6B7	SRGAP1	S413	ochoa	SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13)	GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269\|PubMed:11672528}.
Q7Z6B7	SRGAP1	S416	ochoa	SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13)	GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269\|PubMed:11672528}.
Q7Z6E9	RBBP6	S1347	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6E9	RBBP6	S1625	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6I6	ARHGAP30	S1040	ochoa	Rho GTPase-activating protein 30 (Rho-type GTPase-activating protein 30)	GTPase-activating protein (GAP) for RAC1 and RHOA, but not for CDC42. {ECO:0000269\|PubMed:21565175}.
Q7Z6I6	ARHGAP30	S1043	ochoa	Rho GTPase-activating protein 30 (Rho-type GTPase-activating protein 30)	GTPase-activating protein (GAP) for RAC1 and RHOA, but not for CDC42. {ECO:0000269\|PubMed:21565175}.
Q7Z6L1	TECPR1	S418	ochoa	Tectonin beta-propeller repeat-containing protein 1	Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. {ECO:0000269\|PubMed:21575909, ECO:0000269\|PubMed:22342342}.
Q7Z6Z7	HUWE1	S2532	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S2600	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S2931	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S3165	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S3379	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S3382	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S3759	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z6Z7	HUWE1	S3824	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q7Z7B0	FILIP1	S938	ochoa	Filamin-A-interacting protein 1 (FILIP)	By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of filamin-A. {ECO:0000250\|UniProtKB:Q8K4T4}.
Q86SQ0	PHLDB2	S569	ochoa	Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)	Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12376540}.
Q86SQ4	ADGRG6	S1170	ochoa	Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: Adhesion G-protein coupled receptor G6, N-terminal fragment (ADGRG6 N-terminal fragment) (ADGRG6-NTF); Adhesion G-protein coupled receptor G6, C-terminal fragment (ADGRG6 C-terminal fragment) (ADGRG6-CTF)]	Adhesion G-protein coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (PubMed:35394864, PubMed:39884271). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:24227709, PubMed:35394864). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:24227709, PubMed:35394864). Also able to couple to G(q) G proteins (PubMed:24227709). Involved in myelination of the peripheral nervous system: required for differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Also acts as a regulator of body length and bone mass (PubMed:18391950). Acts as a regulator of blood-brain barrier formation in the central nervous system vie its association with LRP1 and ITGB1 (By similarity). {ECO:0000250\|UniProtKB:Q6F3F9, ECO:0000269\|PubMed:18391950, ECO:0000269\|PubMed:24227709, ECO:0000269\|PubMed:35394864, ECO:0000269\|PubMed:39884271}.
Q86SQ4	ADGRG6	T1171	ochoa	Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: Adhesion G-protein coupled receptor G6, N-terminal fragment (ADGRG6 N-terminal fragment) (ADGRG6-NTF); Adhesion G-protein coupled receptor G6, C-terminal fragment (ADGRG6 C-terminal fragment) (ADGRG6-CTF)]	Adhesion G-protein coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (PubMed:35394864, PubMed:39884271). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:24227709, PubMed:35394864). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:24227709, PubMed:35394864). Also able to couple to G(q) G proteins (PubMed:24227709). Involved in myelination of the peripheral nervous system: required for differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Also acts as a regulator of body length and bone mass (PubMed:18391950). Acts as a regulator of blood-brain barrier formation in the central nervous system vie its association with LRP1 and ITGB1 (By similarity). {ECO:0000250\|UniProtKB:Q6F3F9, ECO:0000269\|PubMed:18391950, ECO:0000269\|PubMed:24227709, ECO:0000269\|PubMed:35394864, ECO:0000269\|PubMed:39884271}.
Q86TC9	MYPN	S391	ochoa	Myopalladin (145 kDa sarcomeric protein)	Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines. {ECO:0000269\|PubMed:11309420}.
Q86TI0	TBC1D1	S263	ochoa	TBC1 domain family member 1	May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity). {ECO:0000250}.
Q86TI0	TBC1D1	S565	ochoa\|psp	TBC1 domain family member 1	May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity). {ECO:0000250}.
Q86TI0	TBC1D1	S571	ochoa	TBC1 domain family member 1	May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity). {ECO:0000250}.
Q86TL2	STIMATE	S255	ochoa	Store-operated calcium entry regulator STIMATE (STIM-activating enhancer encoded by TMEM110) (Transmembrane protein 110)	Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the endoplasmic reticulum (ER) and plasma membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical ER (PubMed:26322679, PubMed:26644574). SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores (PubMed:26322679). Acts by interacting with STIM1, promoting STIM1 conformational switch (PubMed:26322679). Involved in STIM1 relocalization to ER-PM junctions (PubMed:26644574). Contributes to the maintenance and reorganization of store-dependent ER-PM junctions (PubMed:26644574). {ECO:0000269\|PubMed:26322679, ECO:0000269\|PubMed:26644574}.
Q86TP1	PRUNE1	S399	ochoa	Exopolyphosphatase PRUNE1 (EC 3.6.1.1) (Drosophila-related expressed sequence 17) (DRES-17) (DRES17) (HTcD37) (Protein prune homolog 1) (hPrune)	Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, migration and differentiation, and acts as a negative regulator of NME1. Plays a role in the regulation of neurogenesis (PubMed:28334956). Involved in the regulation of microtubule polymerization (PubMed:28334956). {ECO:0000269\|PubMed:10602478, ECO:0000269\|PubMed:11687967, ECO:0000269\|PubMed:14998490, ECO:0000269\|PubMed:16428445, ECO:0000269\|PubMed:17906697, ECO:0000269\|PubMed:28334956}.
Q86TV6	TTC7B	S657	ochoa	Tetratricopeptide repeat protein 7B (TPR repeat protein 7B) (Tetratricopeptide repeat protein 7-like-1) (TPR repeat protein 7-like-1)	Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and HYCC1, via direct interactions (PubMed:26571211). {ECO:0000269\|PubMed:23229899, ECO:0000269\|PubMed:26571211}.
Q86U70	LDB1	S308	ochoa	LIM domain-binding protein 1 (LDB-1) (Carboxyl-terminal LIM domain-binding protein 2) (CLIM-2) (LIM domain-binding factor CLIM2) (hLdb1) (Nuclear LIM interactor)	Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state. {ECO:0000250\|UniProtKB:P70662}.
Q86U70	LDB1	S332	ochoa	LIM domain-binding protein 1 (LDB-1) (Carboxyl-terminal LIM domain-binding protein 2) (CLIM-2) (LIM domain-binding factor CLIM2) (hLdb1) (Nuclear LIM interactor)	Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state. {ECO:0000250\|UniProtKB:P70662}.
Q86UE4	MTDH	S347	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q86UE4	MTDH	S357	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q86UE8	TLK2	S38	ochoa	Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:20016786, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:29955062, ECO:0000269\|PubMed:33323470, ECO:0000269\|PubMed:35136069, ECO:0000269\|PubMed:9427565}.
Q86UE8	TLK2	S41	ochoa	Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:20016786, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:29955062, ECO:0000269\|PubMed:33323470, ECO:0000269\|PubMed:35136069, ECO:0000269\|PubMed:9427565}.
Q86UE8	TLK2	S44	ochoa	Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:20016786, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:29955062, ECO:0000269\|PubMed:33323470, ECO:0000269\|PubMed:35136069, ECO:0000269\|PubMed:9427565}.
Q86UE8	TLK2	S117	ochoa	Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:20016786, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:29955062, ECO:0000269\|PubMed:33323470, ECO:0000269\|PubMed:35136069, ECO:0000269\|PubMed:9427565}.
Q86UP2	KTN1	S1319	ochoa	Kinectin (CG-1 antigen) (Kinesin receptor)	Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin.
Q86US8	SMG6	S870	ochoa	Telomerase-binding protein EST1A (EC 3.1.-.-) (Ever shorter telomeres 1A) (hEST1A) (Nonsense mediated mRNA decay factor SMG6) (Smg-6 homolog) (hSmg5/7a)	Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (PubMed:19179534). May have a general role in telomere regulation (PubMed:12676087, PubMed:12699629). Promotes in vitro the ability of TERT to elongate telomeres (PubMed:12676087, PubMed:12699629). Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization (PubMed:12676087, PubMed:12699629). Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER) (PubMed:12676087, PubMed:12699629). {ECO:0000269\|PubMed:12676087, ECO:0000269\|PubMed:12699629, ECO:0000269\|PubMed:19179534}.; FUNCTION: Plays a role in nonsense-mediated mRNA decay (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). {ECO:0000269\|PubMed:17053788, ECO:0000269\|PubMed:18974281, ECO:0000269\|PubMed:19060897, ECO:0000269\|PubMed:20930030}.
Q86UU0	BCL9L	S997	ochoa	B-cell CLL/lymphoma 9-like protein (B-cell lymphoma 9-like protein) (BCL9-like protein) (Protein BCL9-2)	Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity). {ECO:0000250}.
Q86UU1	PHLDB1	S539	ochoa	Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha)	None
Q86UU1	PHLDB1	S984	ochoa	Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha)	None
Q86V15	CASZ1	S747	ochoa	Zinc finger protein castor homolog 1 (Castor-related protein) (Putative survival-related protein) (Zinc finger protein 693)	Transcriptional activator (PubMed:23639441, PubMed:27693370). Involved in vascular assembly and morphogenesis through direct transcriptional regulation of EGFL7 (PubMed:23639441). {ECO:0000269\|PubMed:23639441, ECO:0000269\|PubMed:27693370}.
Q86V15	CASZ1	S750	ochoa	Zinc finger protein castor homolog 1 (Castor-related protein) (Putative survival-related protein) (Zinc finger protein 693)	Transcriptional activator (PubMed:23639441, PubMed:27693370). Involved in vascular assembly and morphogenesis through direct transcriptional regulation of EGFL7 (PubMed:23639441). {ECO:0000269\|PubMed:23639441, ECO:0000269\|PubMed:27693370}.
Q86V48	LUZP1	S518	ochoa	Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin)	F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250\|UniProtKB:Q8R4U7, ECO:0000269\|PubMed:30990684, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:38009294, ECO:0000269\|PubMed:38832964}.
Q86V48	LUZP1	S579	ochoa	Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin)	F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250\|UniProtKB:Q8R4U7, ECO:0000269\|PubMed:30990684, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:38009294, ECO:0000269\|PubMed:38832964}.
Q86VP3	PACS2	S337	ochoa	Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein)	Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:15692567}.
Q86VP3	PACS2	S343	ochoa	Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein)	Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:15692567}.
Q86VP3	PACS2	S694	ochoa	Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein)	Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:15692567}.
Q86WB0	ZC3HC1	S62	ochoa	Zinc finger C3HC-type protein 1 (Nuclear-interacting partner of ALK) (hNIPA) (Nuclear-interacting partner of anaplastic lymphoma kinase)	Required for proper positioning of a substantial amount of TPR at the nuclear basket (NB) through interaction with TPR. {ECO:0000269\|PubMed:34440706}.
Q86WB0	ZC3HC1	S344	ochoa\|psp	Zinc finger C3HC-type protein 1 (Nuclear-interacting partner of ALK) (hNIPA) (Nuclear-interacting partner of anaplastic lymphoma kinase)	Required for proper positioning of a substantial amount of TPR at the nuclear basket (NB) through interaction with TPR. {ECO:0000269\|PubMed:34440706}.
Q86X10	RALGAPB	S726	ochoa	Ral GTPase-activating protein subunit beta (p170)	Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.
Q86X10	RALGAPB	S729	ochoa	Ral GTPase-activating protein subunit beta (p170)	Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.
Q86X29	LSR	S371	ochoa	Lipolysis-stimulated lipoprotein receptor (Angulin-1)	Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (By similarity). {ECO:0000250\|UniProtKB:Q99KG5, ECO:0000250\|UniProtKB:Q9WU74}.
Q86X51	EZHIP	S468	ochoa	EZH inhibitory protein	Inhibits PRC2/EED-EZH1 and PRC2/EED-EZH2 complex function by inhibiting EZH1/EZH2 methyltransferase activity, thereby causing down-regulation of histone H3 trimethylation on 'Lys-27' (H3K27me3) (PubMed:29909548, PubMed:30923826, PubMed:31086175, PubMed:31451685). Probably inhibits methyltransferase activity by limiting the stimulatory effect of cofactors such as AEBP2 and JARID2 (PubMed:30923826). Inhibits H3K27me3 deposition during spermatogenesis and oogenesis (By similarity). {ECO:0000250\|UniProtKB:B1B0V2, ECO:0000269\|PubMed:29909548, ECO:0000269\|PubMed:30923826, ECO:0000269\|PubMed:31086175, ECO:0000269\|PubMed:31451685}.
Q86XK3	SFR1	S42	ochoa	Swi5-dependent recombination DNA repair protein 1 homolog (Meiosis protein 5 homolog)	Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination (PubMed:21252223). Acts as a transcriptional modulator for ESR1 (PubMed:23874500). {ECO:0000269\|PubMed:21252223, ECO:0000269\|PubMed:23874500}.
Q86XZ4	SPATS2	S120	ochoa	Spermatogenesis-associated serine-rich protein 2 (Serine-rich spermatocytes and round spermatid 59 kDa protein) (p59scr)	None
Q86Y01	DTX1	S195	ochoa	E3 ubiquitin-protein ligase DTX1 (EC 2.3.2.27) (Protein deltex-1) (Deltex1) (hDTX1) (RING-type E3 ubiquitin transferase DTX1)	Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1. {ECO:0000250, ECO:0000269\|PubMed:11564735, ECO:0000269\|PubMed:11869684, ECO:0000269\|PubMed:9590294}.
Q86YD5	LDLRAD3	S305	ochoa	Low-density lipoprotein receptor class A domain-containing protein 3 (LDLR class A domain-containing protein 3)	May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (PubMed:26854353). {ECO:0000250, ECO:0000269\|PubMed:26854353}.; FUNCTION: (Microbial infection) Acts as a receptor for Venezuelan equine encephalitis virus. {ECO:0000269\|PubMed:33208938, ECO:0000269\|PubMed:34646020, ECO:0000269\|PubMed:34646021}.
Q86YD5	LDLRAD3	S310	ochoa	Low-density lipoprotein receptor class A domain-containing protein 3 (LDLR class A domain-containing protein 3)	May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (PubMed:26854353). {ECO:0000250, ECO:0000269\|PubMed:26854353}.; FUNCTION: (Microbial infection) Acts as a receptor for Venezuelan equine encephalitis virus. {ECO:0000269\|PubMed:33208938, ECO:0000269\|PubMed:34646020, ECO:0000269\|PubMed:34646021}.
Q86YN6	PPARGC1B	S390	ochoa	Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PGC-1-beta) (PPAR-gamma coactivator 1-beta) (PPARGC-1-beta) (PGC-1-related estrogen receptor alpha coactivator)	Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. {ECO:0000269\|PubMed:11854298, ECO:0000269\|PubMed:12678921, ECO:0000269\|PubMed:15546003, ECO:0000269\|PubMed:23836911}.
Q86YP4	GATAD2A	S343	ochoa	Transcriptional repressor p66-alpha (Hp66alpha) (GATA zinc finger domain-containing protein 2A)	Transcriptional repressor (PubMed:12183469, PubMed:16415179). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179). Efficient repression requires the presence of GATAD2B (PubMed:16415179). {ECO:0000269\|PubMed:12183469, ECO:0000269\|PubMed:16415179, ECO:0000269\|PubMed:16428440, ECO:0000269\|PubMed:28977666}.
Q86YP4	GATAD2A	S554	ochoa	Transcriptional repressor p66-alpha (Hp66alpha) (GATA zinc finger domain-containing protein 2A)	Transcriptional repressor (PubMed:12183469, PubMed:16415179). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179). Efficient repression requires the presence of GATAD2B (PubMed:16415179). {ECO:0000269\|PubMed:12183469, ECO:0000269\|PubMed:16415179, ECO:0000269\|PubMed:16428440, ECO:0000269\|PubMed:28977666}.
Q86YS7	C2CD5	S301	ochoa	C2 domain-containing protein 5 (C2 domain-containing phosphoprotein of 138 kDa)	Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. {ECO:0000269\|PubMed:21907143}.
Q86YV0	RASAL3	S170	ochoa	RAS protein activator like-3	Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250\|UniProtKB:Q8C2K5}.
Q86YV5	PRAG1	S743	ochoa	Inactive tyrosine-protein kinase PRAG1 (PEAK1-related kinase-activating pseudokinase 1) (Pragmin) (Sugen kinase 223) (SgK223)	Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (By similarity). {ECO:0000250\|UniProtKB:D3ZMK9, ECO:0000250\|UniProtKB:Q571I4}.
Q86YV5	PRAG1	S850	ochoa	Inactive tyrosine-protein kinase PRAG1 (PEAK1-related kinase-activating pseudokinase 1) (Pragmin) (Sugen kinase 223) (SgK223)	Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (By similarity). {ECO:0000250\|UniProtKB:D3ZMK9, ECO:0000250\|UniProtKB:Q571I4}.
Q86YW5	TREML1	S211	ochoa	Trem-like transcript 1 protein (TLT-1) (Triggering receptor expressed on myeloid cells-like protein 1)	Cell surface receptor that may play a role in the innate and adaptive immune response. {ECO:0000269\|PubMed:15128762}.
Q8IU85	CAMK1D	S337	ochoa	Calcium/calmodulin-dependent protein kinase type 1D (EC 2.7.11.17) (CaM kinase I delta) (CaM kinase ID) (CaM-KI delta) (CaMKI delta) (CaMKID) (CaMKI-like protein kinase) (CKLiK)	Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta. {ECO:0000269\|PubMed:11050006, ECO:0000269\|PubMed:15840691, ECO:0000269\|PubMed:16324104, ECO:0000269\|PubMed:17056143}.
Q8IUC4	RHPN2	S604	ochoa	Rhophilin-2 (76 kDa RhoB effector protein) (GTP-Rho-binding protein 2) (p76RBE)	Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity. {ECO:0000269\|PubMed:12221077}.
Q8IUD2	ERC1	S116	ochoa	ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (Rab6-interacting protein 2)	Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269\|PubMed:15218148}.
Q8IUE0	TGIF2LY	S19	ochoa	Homeobox protein TGIF2LY (TGF-beta-induced transcription factor 2-like protein) (TGFB-induced factor 2-like protein, Y-linked) (TGIF-like on the Y)	May have a transcription role in testis. May act as a competitor/regulator of TGIF2LX.
Q8IUE0	TGIF2LY	S25	ochoa	Homeobox protein TGIF2LY (TGF-beta-induced transcription factor 2-like protein) (TGFB-induced factor 2-like protein, Y-linked) (TGIF-like on the Y)	May have a transcription role in testis. May act as a competitor/regulator of TGIF2LX.
Q8IUE1	TGIF2LX	S19	ochoa	Homeobox protein TGIF2LX (TGF-beta-induced transcription factor 2-like protein) (TGFB-induced factor 2-like protein, X-linked) (TGIF-like on the X)	May have a transcription role in testis.
Q8IUE1	TGIF2LX	S25	ochoa	Homeobox protein TGIF2LX (TGF-beta-induced transcription factor 2-like protein) (TGFB-induced factor 2-like protein, X-linked) (TGIF-like on the X)	May have a transcription role in testis.
Q8IV31	TMEM139	S155	ochoa	Transmembrane protein 139	May be involved in cellular trafficking of proteins such as SLC4A1. {ECO:0000305\|PubMed:26049106}.
Q8IV36	HID1	S679	ochoa	Protein HID1 (Down-regulated in multiple cancers 1) (HID1 domain-containing protein) (Protein hid-1 homolog)	May play an important role in the development of cancers in a broad range of tissues. {ECO:0000269\|PubMed:11281419}.
Q8IV48	ERI1	S62	ochoa	3'-5' exoribonuclease 1 (EC 3.1.13.1) (3'-5' exonuclease ERI1) (Eri-1 homolog) (Histone mRNA 3'-end-specific exoribonuclease) (Histone mRNA 3'-exonuclease 1) (Protein 3'hExo) (HEXO)	RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication (PubMed:14536070, PubMed:16912046, PubMed:17135487, PubMed:37352860). A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient 3'-end histone mRNA exonuclease activity and degradation of RNA substrates (PubMed:14536070, PubMed:16912046, PubMed:17135487). Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi) (PubMed:14961122). Required for binding the 5'-ACCCA-3' sequence present in stem-loop structure (PubMed:14536070, PubMed:16912046). Able to bind other mRNAs (PubMed:14536070, PubMed:16912046). Required for 5.8S rRNA 3'-end processing (PubMed:37352860). Also binds to 5.8s ribosomal RNA (By similarity). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs (PubMed:14536070, PubMed:16912046, PubMed:17135487). In vitro, does not have sequence specificity (PubMed:17135487). In vitro, has weak DNA exonuclease activity (PubMed:17135487). In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (PubMed:17135487). ERI1-mediated RNA metabolism plays a key role in chondrogenesis (PubMed:37352860). {ECO:0000250\|UniProtKB:Q7TMF2, ECO:0000269\|PubMed:14536070, ECO:0000269\|PubMed:14961122, ECO:0000269\|PubMed:16912046, ECO:0000269\|PubMed:17135487, ECO:0000269\|PubMed:37352860}.
Q8IVF2	AHNAK2	S4425	ochoa	Protein AHNAK2	None
Q8IVH2	FOXP4	S448	ochoa	Forkhead box protein P4 (Fork head-related protein-like A)	Transcriptional repressor that represses lung-specific expression. {ECO:0000250}.
Q8IVL1	NAV2	S2468	ochoa	Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)	Possesses 3' to 5' helicase activity and exonuclease activity. Involved in neuronal development, specifically in the development of different sensory organs. {ECO:0000269\|PubMed:12214280, ECO:0000269\|PubMed:15158073}.
Q8IVT2	MISP	S84	ochoa	Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein)	Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. {ECO:0000269\|PubMed:23509069, ECO:0000269\|PubMed:23574715}.
Q8IVT2	MISP	S284	ochoa	Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein)	Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. {ECO:0000269\|PubMed:23509069, ECO:0000269\|PubMed:23574715}.
Q8IVT2	MISP	S479	ochoa	Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein)	Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. {ECO:0000269\|PubMed:23509069, ECO:0000269\|PubMed:23574715}.
Q8IWB9	TEX2	S146	ochoa	Testis-expressed protein 2 (Transmembrane protein 96)	During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000269\|PubMed:28011845}.
Q8IWB9	TEX2	S176	ochoa	Testis-expressed protein 2 (Transmembrane protein 96)	During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000269\|PubMed:28011845}.
Q8IWC1	MAP7D3	S530	ochoa	MAP7 domain-containing protein 3	Promotes the assembly and stability of microtubules. {ECO:0000269\|PubMed:22142902, ECO:0000269\|PubMed:24927501}.
Q8IWX8	CHERP	S823	ochoa	Calcium homeostasis endoplasmic reticulum protein (ERPROT 213-21) (SR-related CTD-associated factor 6)	Involved in calcium homeostasis, growth and proliferation. {ECO:0000269\|PubMed:10794731, ECO:0000269\|PubMed:12656674}.
Q8IWX8	CHERP	S828	ochoa	Calcium homeostasis endoplasmic reticulum protein (ERPROT 213-21) (SR-related CTD-associated factor 6)	Involved in calcium homeostasis, growth and proliferation. {ECO:0000269\|PubMed:10794731, ECO:0000269\|PubMed:12656674}.
Q8IWZ3	ANKHD1	S2287	ochoa	Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK)	May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269\|PubMed:16098192}.
Q8IWZ3	ANKHD1	S2297	ochoa	Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK)	May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269\|PubMed:16098192}.
Q8IWZ3	ANKHD1	S2299	ochoa	Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK)	May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269\|PubMed:16098192}.
Q8IWZ8	SUGP1	S491	ochoa	SURP and G-patch domain-containing protein 1 (RNA-binding protein RBP) (Splicing factor 4)	Plays a role in pre-mRNA splicing.
Q8IXI1	RHOT2	S331	ochoa	Mitochondrial Rho GTPase 2 (MIRO-2) (hMiro-2) (EC 3.6.5.-) (Ras homolog gene family member T2)	Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking (PubMed:16630562, PubMed:22396657, PubMed:30513825). Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (PubMed:22396657). Can hydrolyze GTP (By similarity). Can hydrolyze ATP and UTP (PubMed:30513825). {ECO:0000250\|UniProtKB:Q8IXI2, ECO:0000269\|PubMed:16630562, ECO:0000269\|PubMed:22396657, ECO:0000269\|PubMed:30513825}.
Q8IXJ9	ASXL1	S509	ochoa	Polycomb group protein ASXL1 (Additional sex combs-like protein 1)	Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG) (PubMed:16606617). Acts as a coactivator of RARA and RXRA through association with NCOA1 (PubMed:16606617). Acts as a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (PubMed:20436459, PubMed:30664650, PubMed:36180891). Acts as a sensor of N(6)-methyladenine methylation on DNA (6mA): recognizes and binds 6mA DNA, leading to its ubiquitination and degradation by TRIP12, thereby inactivating the PR-DUB complex and regulating Polycomb silencing (PubMed:30982744). The PR-DUB complex is an epigenetic regulator of gene expression and acts as a transcriptional coactivator, affecting genes involved in development, cell communication, signaling, cell proliferation and cell viability (PubMed:30664650, PubMed:36180891). ASXL1, ASXL2 and ASXL3 function redundantly in the PR-DUB complex (By similarity) (PubMed:30664650). The ASXL proteins are essential for chromatin recruitment and transcriptional activation of associated genes (By similarity). ASXL1 and ASXL2 are important for BAP1 protein stability (PubMed:30664650). Together with BAP1, negatively regulates epithelial-mesenchymal transition (EMT) of trophoblast stem cells during placental development by regulating genes involved in epithelial cell integrity, cell adhesion and cytoskeletal organization (PubMed:34170818). {ECO:0000250\|UniProtKB:P59598, ECO:0000269\|PubMed:16606617, ECO:0000269\|PubMed:20436459, ECO:0000269\|PubMed:30664650, ECO:0000269\|PubMed:30982744, ECO:0000269\|PubMed:34170818, ECO:0000269\|PubMed:36180891}.
Q8IXT5	RBM12B	S107	ochoa	RNA-binding protein 12B (RNA-binding motif protein 12B)	None
Q8IY26	PLPP6	S26	ochoa	Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 (EC 3.1.3.-) (EC 3.6.1.-) (EC 3.6.1.68) (Lipid phosphatase-related protein-B) (LPRP-B) (PA-PSP) (Phosphatidic acid phosphatase type 2 domain-containing protein 2) (PPAP2 domain-containing protein 2) (Phospholipid phosphatase 6) (Presqualene diphosphate phosphatase) (Type 1 polyisoprenoid diphosphate phosphatase)	Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269\|PubMed:16464866, ECO:0000269\|PubMed:18930839, ECO:0000269\|PubMed:19220020, ECO:0000269\|PubMed:20110354, ECO:0000269\|PubMed:23568778}.
Q8IY57	YAF2	S155	ochoa	YY1-associated factor 2	Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. {ECO:0000269\|PubMed:11593398, ECO:0000269\|PubMed:12706874, ECO:0000269\|PubMed:9016636}.
Q8IY63	AMOTL1	S793	ochoa\|psp	Angiomotin-like protein 1	Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. {ECO:0000269\|PubMed:22362771}.
Q8IYB1	MB21D2	S439	ochoa	Nucleotidyltransferase MB21D2 (EC 2.7.7.-) (Mab-21 domain-containing protein 2) (hMB21D2)	Probable nucleotidyltransferase that catalyzes the formation of cyclic dinucleotide second messenger in response to some unknown stimulus. {ECO:0000305\|PubMed:34261127}.
Q8IYB1	MB21D2	S442	ochoa	Nucleotidyltransferase MB21D2 (EC 2.7.7.-) (Mab-21 domain-containing protein 2) (hMB21D2)	Probable nucleotidyltransferase that catalyzes the formation of cyclic dinucleotide second messenger in response to some unknown stimulus. {ECO:0000305\|PubMed:34261127}.
Q8IYJ3	SYTL1	S243	ochoa	Synaptotagmin-like protein 1 (Exophilin-7) (Protein JFC1)	May play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11278853, ECO:0000269\|PubMed:18266782}.
Q8IYJ3	SYTL1	S244	ochoa	Synaptotagmin-like protein 1 (Exophilin-7) (Protein JFC1)	May play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11278853, ECO:0000269\|PubMed:18266782}.
Q8IZ21	PHACTR4	S182	ochoa	Phosphatase and actin regulator 4	Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). {ECO:0000250}.
Q8IZ21	PHACTR4	S449	ochoa	Phosphatase and actin regulator 4	Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). {ECO:0000250}.
Q8IZH2	XRN1	S1645	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8IZH2	XRN1	S1651	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8IZH2	XRN1	S1657	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8IZP0	ABI1	S222	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8IZP0	ABI1	S231	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8IZP0	ABI1	S329	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8N0Z3	SPICE1	S320	ochoa	Spindle and centriole-associated protein 1 (Coiled-coil domain-containing protein 52) (Spindle and centriole-associated protein)	Regulator required for centriole duplication, for proper bipolar spindle formation and chromosome congression in mitosis. {ECO:0000269\|PubMed:20736305}.
Q8N108	MIER1	S383	ochoa	Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) (hMi-er1)	Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269\|PubMed:12482978}.
Q8N122	RPTOR	S887	ochoa	Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein)	Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity). {ECO:0000250\|UniProtKB:Q8K4Q0, ECO:0000269\|PubMed:12150925, ECO:0000269\|PubMed:12150926, ECO:0000269\|PubMed:12747827, ECO:0000269\|PubMed:24403073, ECO:0000269\|PubMed:26588989, ECO:0000269\|PubMed:32561715, ECO:0000269\|PubMed:37541260}.
Q8N163	CCAR2	S25	ochoa	Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) (DBIRD complex subunit KIAA1967) (Deleted in breast cancer gene 1 protein) (DBC-1) (DBC.1) (NET35) (p30 DBC)	Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (PubMed:22446626). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (PubMed:18235501, PubMed:18235502, PubMed:23352644). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand-dependent transcriptional activation by nuclear hormone receptors (PubMed:19131338). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (PubMed:23398316). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978). {ECO:0000269\|PubMed:18235501, ECO:0000269\|PubMed:18235502, ECO:0000269\|PubMed:19131338, ECO:0000269\|PubMed:19218236, ECO:0000269\|PubMed:20074560, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:21030595, ECO:0000269\|PubMed:22446626, ECO:0000269\|PubMed:23352644, ECO:0000269\|PubMed:23398316, ECO:0000269\|PubMed:24415752, ECO:0000269\|PubMed:24824780, ECO:0000269\|PubMed:25361978, ECO:0000269\|PubMed:25661920, ECO:0000269\|PubMed:25732823}.
Q8N163	CCAR2	S681	ochoa	Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) (DBIRD complex subunit KIAA1967) (Deleted in breast cancer gene 1 protein) (DBC-1) (DBC.1) (NET35) (p30 DBC)	Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (PubMed:22446626). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (PubMed:18235501, PubMed:18235502, PubMed:23352644). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand-dependent transcriptional activation by nuclear hormone receptors (PubMed:19131338). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (PubMed:23398316). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978). {ECO:0000269\|PubMed:18235501, ECO:0000269\|PubMed:18235502, ECO:0000269\|PubMed:19131338, ECO:0000269\|PubMed:19218236, ECO:0000269\|PubMed:20074560, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:21030595, ECO:0000269\|PubMed:22446626, ECO:0000269\|PubMed:23352644, ECO:0000269\|PubMed:23398316, ECO:0000269\|PubMed:24415752, ECO:0000269\|PubMed:24824780, ECO:0000269\|PubMed:25361978, ECO:0000269\|PubMed:25661920, ECO:0000269\|PubMed:25732823}.
Q8N163	CCAR2	S814	ochoa	Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) (DBIRD complex subunit KIAA1967) (Deleted in breast cancer gene 1 protein) (DBC-1) (DBC.1) (NET35) (p30 DBC)	Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (PubMed:22446626). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (PubMed:18235501, PubMed:18235502, PubMed:23352644). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand-dependent transcriptional activation by nuclear hormone receptors (PubMed:19131338). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (PubMed:23398316). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978). {ECO:0000269\|PubMed:18235501, ECO:0000269\|PubMed:18235502, ECO:0000269\|PubMed:19131338, ECO:0000269\|PubMed:19218236, ECO:0000269\|PubMed:20074560, ECO:0000269\|PubMed:20160719, ECO:0000269\|PubMed:21030595, ECO:0000269\|PubMed:22446626, ECO:0000269\|PubMed:23352644, ECO:0000269\|PubMed:23398316, ECO:0000269\|PubMed:24415752, ECO:0000269\|PubMed:24824780, ECO:0000269\|PubMed:25361978, ECO:0000269\|PubMed:25661920, ECO:0000269\|PubMed:25732823}.
Q8N1F7	NUP93	S72	ochoa	Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93)	Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725). {ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:15703211, ECO:0000269\|PubMed:26878725, ECO:0000269\|PubMed:9348540}.
Q8N1F7	NUP93	S168	ochoa	Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93)	Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725). {ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:15703211, ECO:0000269\|PubMed:26878725, ECO:0000269\|PubMed:9348540}.
Q8N1G2	CMTR1	S37	ochoa	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (hMTr1) (FtsJ methyltransferase domain-containing protein 2) (Interferon-stimulated gene 95 kDa protein) (ISG95)	S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269\|PubMed:18533109, ECO:0000269\|PubMed:20713356, ECO:0000269\|PubMed:21310715}.
Q8N1G2	CMTR1	S46	ochoa	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (hMTr1) (FtsJ methyltransferase domain-containing protein 2) (Interferon-stimulated gene 95 kDa protein) (ISG95)	S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269\|PubMed:18533109, ECO:0000269\|PubMed:20713356, ECO:0000269\|PubMed:21310715}.
Q8N1G2	CMTR1	S55	ochoa	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (hMTr1) (FtsJ methyltransferase domain-containing protein 2) (Interferon-stimulated gene 95 kDa protein) (ISG95)	S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269\|PubMed:18533109, ECO:0000269\|PubMed:20713356, ECO:0000269\|PubMed:21310715}.
Q8N2R8	FAM43A	S389	ochoa	Protein FAM43A	None
Q8N2R8	FAM43A	S392	ochoa	Protein FAM43A	None
Q8N328	PGBD3	S92	ochoa	PiggyBac transposable element-derived protein 3	Binds in vitro to PGBD3-related transposable elements, called MER85s; these non-autonomous 140 bp elements are characterized by the presence of PGBD3 terminal inverted repeats and the absence of internal transposase ORF. {ECO:0000269\|PubMed:22483866}.
Q8N350	CBARP	S328	ochoa	Voltage-dependent calcium channel beta subunit-associated regulatory protein	Negatively regulates voltage-gated calcium channels by preventing the interaction between their alpha and beta subunits. Thereby, negatively regulates calcium channels activity at the plasma membrane and indirectly inhibits calcium-regulated exocytosis. {ECO:0000250\|UniProtKB:Q66L44}.
Q8N3F8	MICALL1	S516	ochoa	MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13)	Lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, acts as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation (PubMed:19864458, PubMed:20801876, PubMed:23596323, PubMed:34100897). Involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking (PubMed:21795389). Alternatively, regulates slow endocytic recycling of endocytosed proteins back to the plasma membrane (PubMed:19864458). Also involved in cargo protein delivery to the plasma membrane (PubMed:34100897). Plays a role in ciliogenesis coordination, recruits EHD1 to primary cilium where it is anchored to the centriole through interaction with tubulins (PubMed:31615969). May indirectly play a role in neurite outgrowth (By similarity). {ECO:0000250\|UniProtKB:Q8BGT6, ECO:0000269\|PubMed:19864458, ECO:0000269\|PubMed:20801876, ECO:0000269\|PubMed:21795389, ECO:0000269\|PubMed:23596323, ECO:0000269\|PubMed:31615969, ECO:0000269\|PubMed:34100897}.
Q8N3F8	MICALL1	S559	ochoa	MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13)	Lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, acts as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation (PubMed:19864458, PubMed:20801876, PubMed:23596323, PubMed:34100897). Involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking (PubMed:21795389). Alternatively, regulates slow endocytic recycling of endocytosed proteins back to the plasma membrane (PubMed:19864458). Also involved in cargo protein delivery to the plasma membrane (PubMed:34100897). Plays a role in ciliogenesis coordination, recruits EHD1 to primary cilium where it is anchored to the centriole through interaction with tubulins (PubMed:31615969). May indirectly play a role in neurite outgrowth (By similarity). {ECO:0000250\|UniProtKB:Q8BGT6, ECO:0000269\|PubMed:19864458, ECO:0000269\|PubMed:20801876, ECO:0000269\|PubMed:21795389, ECO:0000269\|PubMed:23596323, ECO:0000269\|PubMed:31615969, ECO:0000269\|PubMed:34100897}.
Q8N3U4	STAG2	S1064	ochoa	Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2)	Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269\|PubMed:12034751}.
Q8N3V7	SYNPO	S591	ochoa	Synaptopodin	Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.
Q8N3X1	FNBP4	S435	ochoa	Formin-binding protein 4 (Formin-binding protein 30)	None
Q8N3X1	FNBP4	S438	ochoa	Formin-binding protein 4 (Formin-binding protein 30)	None
Q8N4S9	MARVELD2	S146	ochoa	MARVEL domain-containing protein 2 (Tricellulin)	Plays a role in the formation of tricellular tight junctions and of epithelial barriers (By similarity). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti (PubMed:17186462). {ECO:0000250\|UniProtKB:Q3UZP0, ECO:0000269\|PubMed:17186462}.
Q8N4X5	AFAP1L2	S309	ochoa	Actin filament-associated protein 1-like 2 (AFAP1-like protein 2)	May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation. {ECO:0000269\|PubMed:17412687}.
Q8N568	DCLK2	S347	ochoa	Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin domain-containing protein 3B) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2)	Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity). {ECO:0000250}.
Q8N5G2	MACO1	S337	ochoa	Macoilin (Macoilin-1) (Transmembrane protein 57)	Plays a role in the regulation of neuronal activity. {ECO:0000269\|PubMed:21589894}.
Q8N5I9	NOPCHAP1	S20	ochoa	NOP protein chaperone 1	Client-loading PAQosome/R2TP complex cofactor that selects NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP) assembly. Acts as a bridge between NOP58 and the R2TP complex via RUVBL1:RUVBL2. {ECO:0000269\|PubMed:33367824}.
Q8N5I9	NOPCHAP1	S21	ochoa	NOP protein chaperone 1	Client-loading PAQosome/R2TP complex cofactor that selects NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP) assembly. Acts as a bridge between NOP58 and the R2TP complex via RUVBL1:RUVBL2. {ECO:0000269\|PubMed:33367824}.
Q8N612	FHIP1B	S596	ochoa	FHF complex subunit HOOK-interacting protein 1B (FHIP1B) (FTS- and Hook-interacting protein) (FHIP)	Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). {ECO:0000269\|PubMed:18799622, ECO:0000269\|PubMed:32073997}.
Q8N684	CPSF7	S197	ochoa	Cleavage and polyadenylation specificity factor subunit 7 (Cleavage and polyadenylation specificity factor 59 kDa subunit) (CPSF 59 kDa subunit) (Cleavage factor Im complex 59 kDa subunit) (CFIm59) (Pre-mRNA cleavage factor Im 59 kDa subunit)	Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:17024186, PubMed:29276085, PubMed:8626397). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:17024186, PubMed:8626397). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF7 activates directly the mRNA 3'-processing machinery (PubMed:29276085). Binds to pA signals in RNA substrates (PubMed:17024186, PubMed:8626397). {ECO:0000269\|PubMed:17024186, ECO:0000269\|PubMed:20695905, ECO:0000269\|PubMed:23187700, ECO:0000269\|PubMed:29276085, ECO:0000269\|PubMed:8626397}.
Q8N699	MYCT1	S115	ochoa	Myc target protein 1 (Myc target in myeloid cells protein 1)	May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability, and inhibition of hematopoietic differentiation (By similarity). {ECO:0000250}.
Q8N699	MYCT1	S141	ochoa	Myc target protein 1 (Myc target in myeloid cells protein 1)	May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability, and inhibition of hematopoietic differentiation (By similarity). {ECO:0000250}.
Q8N699	MYCT1	S155	ochoa	Myc target protein 1 (Myc target in myeloid cells protein 1)	May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability, and inhibition of hematopoietic differentiation (By similarity). {ECO:0000250}.
Q8N6H7	ARFGAP2	S340	ochoa	ADP-ribosylation factor GTPase-activating protein 2 (ARF GAP 2) (GTPase-activating protein ZNF289) (Zinc finger protein 289)	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269\|PubMed:17760859}.
Q8N6H7	ARFGAP2	S419	ochoa	ADP-ribosylation factor GTPase-activating protein 2 (ARF GAP 2) (GTPase-activating protein ZNF289) (Zinc finger protein 289)	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269\|PubMed:17760859}.
Q8N6T3	ARFGAP1	S361	ochoa	ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)	GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). {ECO:0000250}.
Q8N8S7	ENAH	S537	ochoa	Protein enabled homolog	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11696321, ECO:0000269\|PubMed:18158903}.
Q8N8V4	ANKS4B	S189	ochoa	Ankyrin repeat and SAM domain-containing protein 4B (Harmonin-interacting ankyrin repeat-containing protein) (Harp)	As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (PubMed:26812018). May play a role in cellular response to endoplasmic reticulum stress (By similarity). {ECO:0000250\|UniProtKB:Q8K3X6, ECO:0000269\|PubMed:26812018}.
Q8N9U0	TC2N	S174	ochoa	Tandem C2 domains nuclear protein (Membrane targeting tandem C2 domain-containing protein 1) (Tandem C2 protein in nucleus) (Tac2-N)	None
Q8N9U0	TC2N	S211	ochoa	Tandem C2 domains nuclear protein (Membrane targeting tandem C2 domain-containing protein 1) (Tandem C2 protein in nucleus) (Tac2-N)	None
Q8NAN2	MIGA1	S147	ochoa	Mitoguardin 1 (Protein FAM73A)	Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD. {ECO:0000269\|PubMed:26711011}.
Q8NB78	KDM1B	S26	ochoa	Lysine-specific histone demethylase 2 (EC 1.14.99.66) (Flavin-containing amine oxidase domain-containing protein 1) (Lysine-specific histone demethylase 1B)	Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to achieve such activity, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes (PubMed:30970244). {ECO:0000269\|PubMed:23260659, ECO:0000269\|PubMed:23357850, ECO:0000269\|PubMed:30970244}.
Q8NBF6	AVL9	S329	ochoa	Late secretory pathway protein AVL9 homolog	Functions in cell migration. {ECO:0000269\|PubMed:22595670}.
Q8NC44	RETREG2	S138	ochoa	Reticulophagy regulator 2	Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress (PubMed:34338405). When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins (PubMed:34338405). Required for collagen quality control in a LIR motif-independent manner (By similarity). {ECO:0000250\|UniProtKB:Q6NS82, ECO:0000269\|PubMed:34338405}.
Q8NC51	SERBP1	S203	ochoa\|psp	SERPINE1 mRNA-binding protein 1 (PAI1 RNA-binding protein 1) (PAI-RBP1) (Plasminogen activator inhibitor 1 RNA-binding protein)	Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). {ECO:0000250\|UniProtKB:Q9CY58, ECO:0000269\|PubMed:11001948, ECO:0000269\|PubMed:28695742, ECO:0000269\|PubMed:36691768}.
Q8NC51	SERBP1	S205	ochoa	SERPINE1 mRNA-binding protein 1 (PAI1 RNA-binding protein 1) (PAI-RBP1) (Plasminogen activator inhibitor 1 RNA-binding protein)	Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). {ECO:0000250\|UniProtKB:Q9CY58, ECO:0000269\|PubMed:11001948, ECO:0000269\|PubMed:28695742, ECO:0000269\|PubMed:36691768}.
Q8NC51	SERBP1	S208	ochoa	SERPINE1 mRNA-binding protein 1 (PAI1 RNA-binding protein 1) (PAI-RBP1) (Plasminogen activator inhibitor 1 RNA-binding protein)	Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). {ECO:0000250\|UniProtKB:Q9CY58, ECO:0000269\|PubMed:11001948, ECO:0000269\|PubMed:28695742, ECO:0000269\|PubMed:36691768}.
Q8NC74	RBBP8NL	S196	ochoa	RBBP8 N-terminal-like protein	None
Q8NCD3	HJURP	S563	ochoa	Holliday junction recognition protein (14-3-3-associated AKT substrate) (Fetal liver-expressing gene 1 protein) (Up-regulated in lung cancer 9)	Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions. {ECO:0000269\|PubMed:19410544, ECO:0000269\|PubMed:19410545}.
Q8NCE2	MTMR14	S518	ochoa	Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR14 (EC 3.1.3.95) (HCV NS5A-transactivated protein 4 splice variant A-binding protein 1) (NS5ATP4ABP1) (Myotubularin-related protein 14) (Phosphatidylinositol-3-phosphate phosphatase) (hJumpy)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate. {ECO:0000269\|PubMed:17008356}.
Q8NCN4	RNF169	S374	ochoa	E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169)	Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269\|PubMed:22492721, ECO:0000269\|PubMed:22733822, ECO:0000269\|PubMed:22742833, ECO:0000269\|PubMed:30104380, ECO:0000269\|PubMed:30773093}.
Q8NCN4	RNF169	S409	ochoa	E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169)	Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269\|PubMed:22492721, ECO:0000269\|PubMed:22733822, ECO:0000269\|PubMed:22742833, ECO:0000269\|PubMed:30104380, ECO:0000269\|PubMed:30773093}.
Q8ND24	RNF214	S21	ochoa	RING finger protein 214	None
Q8ND24	RNF214	S25	ochoa	RING finger protein 214	None
Q8ND24	RNF214	S53	ochoa	RING finger protein 214	None
Q8ND83	SLAIN1	S246	ochoa	SLAIN motif-containing protein 1	Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269\|PubMed:21646404}.
Q8ND83	SLAIN1	S253	ochoa	SLAIN motif-containing protein 1	Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269\|PubMed:21646404}.
Q8NDI1	EHBP1	S177	ochoa	EH domain-binding protein 1	May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (PubMed:14676205, PubMed:27552051). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity). {ECO:0000250\|UniProtKB:Q69ZW3, ECO:0000269\|PubMed:14676205, ECO:0000305\|PubMed:27552051}.
Q8NDI1	EHBP1	S666	ochoa	EH domain-binding protein 1	May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (PubMed:14676205, PubMed:27552051). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity). {ECO:0000250\|UniProtKB:Q69ZW3, ECO:0000269\|PubMed:14676205, ECO:0000305\|PubMed:27552051}.
Q8NDT2	RBM15B	S237	ochoa	Putative RNA-binding protein 15B (One-twenty two protein 3) (HsOTT3) (HuOTT3) (RNA-binding motif protein 15B)	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:27602518). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA splicing (PubMed:21044963). Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1 (PubMed:19586903). {ECO:0000269\|PubMed:19586903, ECO:0000269\|PubMed:21044963, ECO:0000269\|PubMed:27602518, ECO:0000305\|PubMed:16129689}.
Q8NDV7	TNRC6A	S678	ochoa	Trinucleotide repeat-containing gene 6A protein (CAG repeat protein 26) (EMSY interactor protein) (GW182 autoantigen) (Protein GW1) (Glycine-tryptophan protein of 182 kDa)	Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent repression of translation and for siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As a scaffolding protein, associates with argonaute proteins bound to partially complementary mRNAs, and can simultaneously recruit CCR4-NOT and PAN deadenylase complexes. {ECO:0000269\|PubMed:16284622, ECO:0000269\|PubMed:16284623, ECO:0000269\|PubMed:17596515, ECO:0000269\|PubMed:17671087, ECO:0000269\|PubMed:19056672, ECO:0000269\|PubMed:19304925}.
Q8NDX5	PHC3	S304	ochoa	Polyhomeotic-like protein 3 (Early development regulatory protein 3) (Homolog of polyhomeotic 3) (hPH3)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269\|PubMed:12167701}.
Q8NDX5	PHC3	S661	ochoa	Polyhomeotic-like protein 3 (Early development regulatory protein 3) (Homolog of polyhomeotic 3) (hPH3)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269\|PubMed:12167701}.
Q8NEM7	SUPT20H	S391	ochoa	Transcription factor SPT20 homolog (p38-interacting protein) (p38IP)	Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail (By similarity). Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000250, ECO:0000269\|PubMed:19893488}.
Q8NEM7	SUPT20H	S434	ochoa	Transcription factor SPT20 homolog (p38-interacting protein) (p38IP)	Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail (By similarity). Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000250, ECO:0000269\|PubMed:19893488}.
Q8NEY1	NAV1	S312	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8NEY1	NAV1	S654	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8NEY1	NAV1	S1187	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8NEY1	NAV1	S1271	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8NEY8	PPHLN1	S153	ochoa	Periphilin-1 (CDC7 expression repressor) (CR) (Gastric cancer antigen Ga50)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269\|PubMed:15474462, ECO:0000269\|PubMed:17963697, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:30487602, ECO:0000305\|PubMed:12853457}.
Q8NEY8	PPHLN1	S161	ochoa	Periphilin-1 (CDC7 expression repressor) (CR) (Gastric cancer antigen Ga50)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269\|PubMed:15474462, ECO:0000269\|PubMed:17963697, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:30487602, ECO:0000305\|PubMed:12853457}.
Q8NEY8	PPHLN1	S213	ochoa	Periphilin-1 (CDC7 expression repressor) (CR) (Gastric cancer antigen Ga50)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269\|PubMed:15474462, ECO:0000269\|PubMed:17963697, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:30487602, ECO:0000305\|PubMed:12853457}.
Q8NEZ2	VPS37A	S18	ochoa	Vacuolar protein sorting-associated protein 37A (hVps37A) (ESCRT-I complex subunit VPS37A) (Hepatocellular carcinoma-related protein 1)	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269\|PubMed:15240819}.
Q8NEZ4	KMT2C	S119	ochoa	Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.364) (Homologous to ALR protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 3)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:22266653, PubMed:24081332, PubMed:25561738). Likely plays a redundant role with KMT2D in enriching H3K4me1 mark on primed and active enhancer elements (PubMed:24081332). {ECO:0000269\|PubMed:22266653, ECO:0000269\|PubMed:24081332, ECO:0000269\|PubMed:25561738}.
Q8NF91	SYNE1	S8670	ochoa	Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)	Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus-centrosome attachment and nuclear migration in neural progenitors implicating LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes; SYNE1 and SYNE2 may act redundantly. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250\|UniProtKB:Q6ZWR6, ECO:0000269\|PubMed:11792814, ECO:0000269\|PubMed:18396275}.
Q8NF91	SYNE1	S8671	ochoa	Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)	Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus-centrosome attachment and nuclear migration in neural progenitors implicating LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes; SYNE1 and SYNE2 may act redundantly. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250\|UniProtKB:Q6ZWR6, ECO:0000269\|PubMed:11792814, ECO:0000269\|PubMed:18396275}.
Q8NF99	ZNF397	S242	ochoa	Zinc finger protein 397 (Zinc finger and SCAN domain-containing protein 15) (Zinc finger protein 47)	Isoform 3 acts as a DNA-dependent transcriptional repressor. {ECO:0000269\|PubMed:12801647}.
Q8NF99	ZNF397	S244	ochoa	Zinc finger protein 397 (Zinc finger and SCAN domain-containing protein 15) (Zinc finger protein 47)	Isoform 3 acts as a DNA-dependent transcriptional repressor. {ECO:0000269\|PubMed:12801647}.
Q8NFC6	BOD1L1	S1101	ochoa	Biorientation of chromosomes in cell division protein 1-like 1	Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2-dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM (PubMed:26166705, PubMed:29937342). Does not regulate spindle orientation (PubMed:26166705). {ECO:0000269\|PubMed:26166705, ECO:0000269\|PubMed:29937342}.
Q8NFC6	BOD1L1	S1286	ochoa	Biorientation of chromosomes in cell division protein 1-like 1	Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2-dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM (PubMed:26166705, PubMed:29937342). Does not regulate spindle orientation (PubMed:26166705). {ECO:0000269\|PubMed:26166705, ECO:0000269\|PubMed:29937342}.
Q8NFC6	BOD1L1	S1710	ochoa	Biorientation of chromosomes in cell division protein 1-like 1	Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2-dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM (PubMed:26166705, PubMed:29937342). Does not regulate spindle orientation (PubMed:26166705). {ECO:0000269\|PubMed:26166705, ECO:0000269\|PubMed:29937342}.
Q8NFH3	NUP43	S315	ochoa	Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) (p42)	Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269\|PubMed:17363900}.
Q8NFH5	NUP35	S105	ochoa	Nucleoporin NUP35 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53)	Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC. {ECO:0000269\|PubMed:15703211}.
Q8NHG8	ZNRF2	S113	ochoa	E3 ubiquitin-protein ligase ZNRF2 (EC 2.3.2.27) (Protein Ells2) (RING finger protein 202) (RING-type E3 ubiquitin transferase ZNRF2) (Zinc/RING finger protein 2)	E3 ubiquitin-protein ligase that plays a role in the establishment and maintenance of neuronal transmission and plasticity. Ubiquitinates the Na(+)/K(+) ATPase alpha-1 subunit/ATP1A1 and thereby influences its endocytosis and/or degradation (PubMed:22797923). Acts also as a positive regulator of mTORC1 activation by amino acids, which functions upstream of the V-ATPase and of Rag-GTPases (PubMed:27244671). In turn, phosphorylation by mTOR leads to its inhibition via targeting to the cytosol allowing a self-regulating feedback mechanism (PubMed:27244671). {ECO:0000269\|PubMed:14561866, ECO:0000269\|PubMed:22797923, ECO:0000269\|PubMed:27244671}.
Q8NHM5	KDM2B	S480	ochoa	Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)	Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (PubMed:16362057, PubMed:17994099). May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex (Probable). {ECO:0000269\|PubMed:16362057, ECO:0000269\|PubMed:17994099, ECO:0000269\|PubMed:26237645, ECO:0000305}.
Q8NHM5	KDM2B	S483	ochoa	Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)	Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (PubMed:16362057, PubMed:17994099). May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex (Probable). {ECO:0000269\|PubMed:16362057, ECO:0000269\|PubMed:17994099, ECO:0000269\|PubMed:26237645, ECO:0000305}.
Q8NHV4	NEDD1	S338	psp	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NHV4	NEDD1	S411	ochoa\|psp	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NHV4	NEDD1	S525	ochoa	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NHV4	NEDD1	S574	psp	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NI08	NCOA7	S179	ochoa	Nuclear receptor coactivator 7 (140 kDa estrogen receptor-associated protein) (Estrogen nuclear receptor coactivator 1)	Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269\|PubMed:11971969}.
Q8NI27	THOC2	S1215	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8NI27	THOC2	S1217	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8TAA9	VANGL1	S17	ochoa	Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1)	None
Q8TAE6	PPP1R14C	S42	ochoa	Protein phosphatase 1 regulatory subunit 14C (Kinase-enhanced PP1 inhibitor) (PKC-potentiated PP1 inhibitory protein) (Serologically defined breast cancer antigen NY-BR-81)	Inhibitor of the PP1 regulatory subunit PPP1CA.
Q8TAE6	PPP1R14C	S43	ochoa	Protein phosphatase 1 regulatory subunit 14C (Kinase-enhanced PP1 inhibitor) (PKC-potentiated PP1 inhibitory protein) (Serologically defined breast cancer antigen NY-BR-81)	Inhibitor of the PP1 regulatory subunit PPP1CA.
Q8TB45	DEPTOR	S244	ochoa\|psp	DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6)	Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269\|PubMed:19446321, ECO:0000269\|PubMed:22017875, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:22017877, ECO:0000269\|PubMed:25936805, ECO:0000269\|PubMed:29382726, ECO:0000269\|PubMed:34519268, ECO:0000269\|PubMed:34519269}.
Q8TB45	DEPTOR	S286	ochoa\|psp	DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6)	Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269\|PubMed:19446321, ECO:0000269\|PubMed:22017875, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:22017877, ECO:0000269\|PubMed:25936805, ECO:0000269\|PubMed:29382726, ECO:0000269\|PubMed:34519268, ECO:0000269\|PubMed:34519269}.
Q8TB45	DEPTOR	S293	ochoa\|psp	DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6)	Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269\|PubMed:19446321, ECO:0000269\|PubMed:22017875, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:22017877, ECO:0000269\|PubMed:25936805, ECO:0000269\|PubMed:29382726, ECO:0000269\|PubMed:34519268, ECO:0000269\|PubMed:34519269}.
Q8TB72	PUM2	S93	ochoa	Pumilio homolog 2 (Pumilio-2)	Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000269\|PubMed:18776931, ECO:0000269\|PubMed:21397187, ECO:0000269\|PubMed:22345517, ECO:0000269\|PubMed:22955276, ECO:0000269\|PubMed:25340845, ECO:0000269\|PubMed:25349211, ECO:0000269\|PubMed:26724866, ECO:0000269\|PubMed:28431233}.
Q8TBB5	KLHDC4	S68	ochoa	Kelch domain-containing protein 4	None
Q8TBC3	SHKBP1	S637	ochoa	SH3KBP1-binding protein 1 (SETA-binding protein 1)	Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation. {ECO:0000250\|UniProtKB:Q6P7W2}.
Q8TBZ3	WDR20	S438	ochoa	WD repeat-containing protein 20 (Protein DMR)	Regulator of deubiquitinating complexes. Activates deubiquitinating activity of complexes containing USP12 (PubMed:20147737, PubMed:27373336). Anchors at the base of the ubiquitin-contacting loop of USP12 and remotely modulates the catalytic center of the enzyme (PubMed:27373336). Regulates shuttling of the USP12 deubiquitinase complex between the plasma membrane, cytoplasm and nucleus (PubMed:30466959). {ECO:0000269\|PubMed:20147737, ECO:0000269\|PubMed:27373336, ECO:0000269\|PubMed:30466959}.
Q8TCN5	ZNF507	S410	ochoa	Zinc finger protein 507	May be involved in transcriptional regulation.
Q8TCN5	ZNF507	S890	ochoa	Zinc finger protein 507	May be involved in transcriptional regulation.
Q8TD19	NEK9	S741	ochoa	Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) (NimA-related kinase 8) (Nek8)	Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817, PubMed:26522158). {ECO:0000269\|PubMed:11864968, ECO:0000269\|PubMed:12101123, ECO:0000269\|PubMed:12840024, ECO:0000269\|PubMed:14660563, ECO:0000269\|PubMed:19941817, ECO:0000269\|PubMed:26522158}.
Q8TDB6	DTX3L	S551	ochoa	E3 ubiquitin-protein ligase DTX3L (EC 2.3.2.27) (B-lymphoma- and BAL-associated protein) (Protein deltex-3-like) (RING-type E3 ubiquitin transferase DTX3L) (Rhysin-2) (Rhysin2)	E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses (PubMed:12670957, PubMed:19818714, PubMed:23230272, PubMed:26479788). Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4 (PubMed:28525742). In response to DNA damage, mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1) (PubMed:19818714). The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me) (PubMed:19818714). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). By monoubiquitinating histone H2B H2BC9/H2BJ and thereby promoting chromatin remodeling, positively regulates STAT1-dependent interferon-stimulated gene transcription and thus STAT1-mediated control of viral replication (PubMed:26479788). Independently of its catalytic activity, promotes the sorting of chemokine receptor CXCR4 from early endosome to lysosome following CXCL12 stimulation by reducing E3 ligase ITCH activity and thus ITCH-mediated ubiquitination of endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (PubMed:24790097). In addition, required for the recruitment of HGS and STAM to early endosomes (PubMed:24790097). In association with PARP9, plays a role in antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases and thus promoting their proteasomal-mediated degradation (PubMed:26479788). {ECO:0000269\|PubMed:12670957, ECO:0000269\|PubMed:19818714, ECO:0000269\|PubMed:23230272, ECO:0000269\|PubMed:24790097, ECO:0000269\|PubMed:26479788, ECO:0000269\|PubMed:28525742}.
Q8TDJ6	DMXL2	S959	ochoa	DmX-like protein 2 (Rabconnectin-3)	May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763). Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity). {ECO:0000250\|UniProtKB:Q8BPN8, ECO:0000269\|PubMed:11809763}.
Q8TDJ6	DMXL2	S1149	ochoa	DmX-like protein 2 (Rabconnectin-3)	May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763). Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity). {ECO:0000250\|UniProtKB:Q8BPN8, ECO:0000269\|PubMed:11809763}.
Q8TDY2	RB1CC1	S650	ochoa	RB1-inducible coiled-coil protein 1 (FAK family kinase-interacting protein of 200 kDa) (FIP200)	Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). {ECO:0000250\|UniProtKB:Q9ESK9, ECO:0000269\|PubMed:10769033, ECO:0000269\|PubMed:12095676, ECO:0000269\|PubMed:12163359, ECO:0000269\|PubMed:12221124, ECO:0000269\|PubMed:14533007, ECO:0000269\|PubMed:21775823, ECO:0000269\|PubMed:23392225}.
Q8TDY2	RB1CC1	S653	ochoa	RB1-inducible coiled-coil protein 1 (FAK family kinase-interacting protein of 200 kDa) (FIP200)	Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). {ECO:0000250\|UniProtKB:Q9ESK9, ECO:0000269\|PubMed:10769033, ECO:0000269\|PubMed:12095676, ECO:0000269\|PubMed:12163359, ECO:0000269\|PubMed:12221124, ECO:0000269\|PubMed:14533007, ECO:0000269\|PubMed:21775823, ECO:0000269\|PubMed:23392225}.
Q8TDY4	ASAP3	S868	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 (Development and differentiation-enhancing factor-like 1) (Protein up-regulated in liver cancer 1)	Promotes cell proliferation. {ECO:0000269\|PubMed:14654939}.
Q8TE76	MORC4	S538	ochoa	MORC family CW-type zinc finger protein 4 (Zinc finger CW-type coiled-coil domain protein 2) (Zinc finger CW-type domain protein 4)	Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034). {ECO:0000269\|PubMed:26933034}.
Q8TED9	AFAP1L1	S149	ochoa	Actin filament-associated protein 1-like 1 (AFAP1-like protein 1)	May be involved in podosome and invadosome formation. {ECO:0000269\|PubMed:21333378}.
Q8TEK3	DOT1L	S1065	ochoa	Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (DOT1-like protein) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4)	Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones (PubMed:12123582). Binds to DNA (PubMed:12628190). {ECO:0000269\|PubMed:12123582, ECO:0000269\|PubMed:12628190}.
Q8TEQ0	SNX29	S450	ochoa	Sorting nexin-29 (RUN domain-containing protein 2A)	None
Q8TEU7	RAPGEF6	S1076	ochoa	Rap guanine nucleotide exchange factor 6 (PDZ domain-containing guanine nucleotide exchange factor 2) (PDZ-GEF2) (RA-GEF-2)	Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP. {ECO:0000269\|PubMed:11524421, ECO:0000269\|PubMed:12581858}.
Q8TEW0	PARD3	S158	ochoa	Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)	Adapter protein involved in asymmetrical cell division and cell polarization processes (PubMed:10954424, PubMed:27925688). Seems to play a central role in the formation of epithelial tight junctions (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:10934474). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (PubMed:19812038, PubMed:27925688). {ECO:0000250\|UniProtKB:Q99NH2, ECO:0000250\|UniProtKB:Q9Z340, ECO:0000269\|PubMed:10934474, ECO:0000269\|PubMed:10954424, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:27925688}.
Q8TEW0	PARD3	S386	ochoa	Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)	Adapter protein involved in asymmetrical cell division and cell polarization processes (PubMed:10954424, PubMed:27925688). Seems to play a central role in the formation of epithelial tight junctions (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:10934474). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (PubMed:19812038, PubMed:27925688). {ECO:0000250\|UniProtKB:Q99NH2, ECO:0000250\|UniProtKB:Q9Z340, ECO:0000269\|PubMed:10934474, ECO:0000269\|PubMed:10954424, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:27925688}.
Q8TEW0	PARD3	S809	ochoa	Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)	Adapter protein involved in asymmetrical cell division and cell polarization processes (PubMed:10954424, PubMed:27925688). Seems to play a central role in the formation of epithelial tight junctions (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:10934474). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (PubMed:19812038, PubMed:27925688). {ECO:0000250\|UniProtKB:Q99NH2, ECO:0000250\|UniProtKB:Q9Z340, ECO:0000269\|PubMed:10934474, ECO:0000269\|PubMed:10954424, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:27925688}.
Q8TEW0	PARD3	S973	ochoa	Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)	Adapter protein involved in asymmetrical cell division and cell polarization processes (PubMed:10954424, PubMed:27925688). Seems to play a central role in the formation of epithelial tight junctions (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:10934474). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (PubMed:19812038, PubMed:27925688). {ECO:0000250\|UniProtKB:Q99NH2, ECO:0000250\|UniProtKB:Q9Z340, ECO:0000269\|PubMed:10934474, ECO:0000269\|PubMed:10954424, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:27925688}.
Q8TEW8	PARD3B	S344	ochoa	Partitioning defective 3 homolog B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein) (PAR3-beta) (Partitioning defective 3-like protein) (PAR3-L protein)	Putative adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions.
Q8TF72	SHROOM3	S976	ochoa	Protein Shroom3 (Shroom-related protein) (hShrmL)	Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers (By similarity). Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity). {ECO:0000250\|UniProtKB:Q27IV2, ECO:0000250\|UniProtKB:Q9QXN0}.
Q8TF76	HASPIN	S185	psp	Serine/threonine-protein kinase haspin (EC 2.7.11.1) (Germ cell-specific gene 2 protein) (H-haspin) (Haploid germ cell-specific nuclear protein kinase)	Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle. {ECO:0000269\|PubMed:11228240, ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:17084365, ECO:0000269\|PubMed:20705812, ECO:0000269\|PubMed:20929775}.
Q8WU20	FRS2	S161	ochoa	Fibroblast growth factor receptor substrate 2 (FGFR substrate 2) (FGFR-signaling adaptor SNT) (Suc1-associated neurotrophic factor target 1) (SNT-1)	Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1. {ECO:0000269\|PubMed:12974390, ECO:0000269\|PubMed:21765395}.
Q8WU79	SMAP2	S222	ochoa	Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like)	GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity). {ECO:0000250}.
Q8WU79	SMAP2	S225	ochoa	Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like)	GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity). {ECO:0000250}.
Q8WUB8	PHF10	S67	ochoa	PHD finger protein 10 (BRG1-associated factor 45a) (BAF45a) (XAP135)	Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.
Q8WUB8	PHF10	S327	ochoa	PHD finger protein 10 (BRG1-associated factor 45a) (BAF45a) (XAP135)	Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.
Q8WUI4	HDAC7	S493	ochoa	Histone deacetylase 7 (HD7) (EC 3.5.1.98) (Histone deacetylase 7A) (HD7a) (Protein deacetylase HDAC7) (EC 3.5.1.-)	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (By similarity). During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene (PubMed:12239305). Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). Also acetylates non-histone proteins, such as ALKBH5 (PubMed:37369679). {ECO:0000250\|UniProtKB:Q8C2B3, ECO:0000269\|PubMed:12239305, ECO:0000269\|PubMed:17360565, ECO:0000269\|PubMed:28167758, ECO:0000269\|PubMed:37369679}.
Q8WUM0	NUP133	S33	ochoa	Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133)	Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269\|PubMed:11684705, ECO:0000269\|PubMed:30179222}.
Q8WUM0	NUP133	S50	ochoa\|psp	Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133)	Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269\|PubMed:11684705, ECO:0000269\|PubMed:30179222}.
Q8WUM0	NUP133	S499	ochoa	Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133)	Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269\|PubMed:11684705, ECO:0000269\|PubMed:30179222}.
Q8WUZ0	BCL7C	S106	ochoa	B-cell CLL/lymphoma 7 protein family member C	May play an anti-apoptotic role. {ECO:0000250}.
Q8WV28	BLNK	S225	ochoa	B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65)	Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis. {ECO:0000269\|PubMed:10583958, ECO:0000269\|PubMed:15270728, ECO:0000269\|PubMed:16912232, ECO:0000269\|PubMed:9697839}.
Q8WVB6	CHTF18	S871	ochoa	Chromosome transmission fidelity protein 18 homolog (hCTF18) (CHL12)	Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. Interacts with and stimulates DNA polymerase POLH. During DNA repair synthesis, involved in loading DNA polymerase POLE at the sites of local damage (PubMed:20227374). {ECO:0000269\|PubMed:12766176, ECO:0000269\|PubMed:12930902, ECO:0000269\|PubMed:17545166, ECO:0000269\|PubMed:20227374}.
Q8WVM7	STAG1	S1068	ochoa	Cohesin subunit SA-1 (SCC3 homolog 1) (Stromal antigen 1)	Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Q8WVV4	POF1B	S82	ochoa	Protein POF1B (Premature ovarian failure protein 1B)	Plays a key role in the organization of epithelial monolayers by regulating the actin cytoskeleton. May be involved in ovary development. {ECO:0000269\|PubMed:16773570, ECO:0000269\|PubMed:21940798}.
Q8WWI1	LMO7	S252	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S255	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S263	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S873	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S879	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S994	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S997	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1018	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1026	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1516	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1570	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1599	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1601	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWM7	ATXN2L	S396	ochoa	Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein)	Involved in the regulation of stress granule and P-body formation. {ECO:0000269\|PubMed:23209657}.
Q8WWM7	ATXN2L	S430	ochoa	Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein)	Involved in the regulation of stress granule and P-body formation. {ECO:0000269\|PubMed:23209657}.
Q8WWM7	ATXN2L	S604	ochoa	Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein)	Involved in the regulation of stress granule and P-body formation. {ECO:0000269\|PubMed:23209657}.
Q8WWQ0	PHIP	S142	ochoa	PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11)	Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269\|PubMed:12242307, ECO:0000269\|PubMed:21834987}.
Q8WWQ0	PHIP	S677	ochoa	PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11)	Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269\|PubMed:12242307, ECO:0000269\|PubMed:21834987}.
Q8WWQ0	PHIP	S683	ochoa	PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11)	Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269\|PubMed:12242307, ECO:0000269\|PubMed:21834987}.
Q8WWQ0	PHIP	S1479	ochoa	PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11)	Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269\|PubMed:12242307, ECO:0000269\|PubMed:21834987}.
Q8WWY3	PRPF31	S451	ochoa	U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (Serologically defined breast cancer antigen NY-BR-99) (U4/U6 snRNP 61 kDa protein) (Protein 61K) (hPrp31)	Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11867543, PubMed:20118938, PubMed:28781166). Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:11867543). {ECO:0000269\|PubMed:11867543, ECO:0000269\|PubMed:20118938, ECO:0000269\|PubMed:28781166}.
Q8WX93	PALLD	S760	ochoa	Palladin (SIH002) (Sarcoma antigen NY-SAR-77)	Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci. {ECO:0000269\|PubMed:11598191, ECO:0000269\|PubMed:15147863, ECO:0000269\|PubMed:17537434}.
Q8WX93	PALLD	S763	ochoa	Palladin (SIH002) (Sarcoma antigen NY-SAR-77)	Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci. {ECO:0000269\|PubMed:11598191, ECO:0000269\|PubMed:15147863, ECO:0000269\|PubMed:17537434}.
Q8WXE0	CASKIN2	S409	ochoa	Caskin-2 (CASK-interacting protein 2)	None
Q8WXE0	CASKIN2	S412	ochoa	Caskin-2 (CASK-interacting protein 2)	None
Q8WXE0	CASKIN2	S711	ochoa	Caskin-2 (CASK-interacting protein 2)	None
Q8WXG6	MADD	S707	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S708	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S709	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S824	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S836	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S839	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S936	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S1198	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXI7	MUC16	S9553	ochoa	Mucin-16 (MUC-16) (Ovarian cancer-related tumor marker CA125) (CA-125) (Ovarian carcinoma antigen CA125)	Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. {ECO:0000250}.
Q8WXI9	GATAD2B	S135	ochoa	Transcriptional repressor p66-beta (GATA zinc finger domain-containing protein 2B) (p66/p68)	Transcriptional repressor (PubMed:12183469, PubMed:16415179). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Enhances MBD2-mediated repression (PubMed:12183469, PubMed:16415179). Efficient repression requires the presence of GATAD2A (PubMed:16415179). Targets MBD3 to discrete loci in the nucleus (PubMed:11756549). May play a role in synapse development (PubMed:23644463). {ECO:0000269\|PubMed:11756549, ECO:0000269\|PubMed:12183469, ECO:0000269\|PubMed:16415179, ECO:0000269\|PubMed:16428440, ECO:0000269\|PubMed:23644463, ECO:0000269\|PubMed:28977666}.
Q8WY36	BBX	S183	ochoa	HMG box transcription factor BBX (Bobby sox homolog) (HMG box-containing protein 2)	Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269\|PubMed:11680820}.
Q8WY36	BBX	S649	ochoa	HMG box transcription factor BBX (Bobby sox homolog) (HMG box-containing protein 2)	Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269\|PubMed:11680820}.
Q8WYB5	KAT6B	S527	ochoa	Histone acetyltransferase KAT6B (EC 2.3.1.48) (Histone acetyltransferase MOZ2) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4) (MYST-4) (Monocytic leukemia zinc finger protein-related factor)	Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269\|PubMed:10497217, ECO:0000269\|PubMed:11965546, ECO:0000269\|PubMed:16387653}.
Q8WYL5	SSH1	S943	ochoa	Protein phosphatase Slingshot homolog 1 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 1) (SSH-1L) (hSSH-1L)	Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269\|PubMed:11832213, ECO:0000269\|PubMed:12684437, ECO:0000269\|PubMed:12807904, ECO:0000269\|PubMed:14531860, ECO:0000269\|PubMed:14645219, ECO:0000269\|PubMed:15056216, ECO:0000269\|PubMed:15159416, ECO:0000269\|PubMed:15660133, ECO:0000269\|PubMed:15671020, ECO:0000269\|PubMed:16230460}.
Q8WYP5	AHCTF1	S1160	ochoa	Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1)	Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269\|PubMed:17098863, ECO:0000269\|PubMed:17235358}.
Q8WYP5	AHCTF1	S1914	ochoa	Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1)	Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269\|PubMed:17098863, ECO:0000269\|PubMed:17235358}.
Q8WYQ5	DGCR8	S383	ochoa	Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8)	Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs (PubMed:26027739, PubMed:26748718). The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994). Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998). Involved in the silencing of embryonic stem cell self-renewal (By similarity). Also plays a role in DNA repair by promoting the recruitment of RNF168 to RNF8 and MDC1 at DNA double-strand breaks and subsequently the clearance of DNA breaks (PubMed:34188037). {ECO:0000250\|UniProtKB:Q9EQM6, ECO:0000269\|PubMed:15531877, ECO:0000269\|PubMed:15574589, ECO:0000269\|PubMed:15589161, ECO:0000269\|PubMed:16751099, ECO:0000269\|PubMed:16906129, ECO:0000269\|PubMed:16963499, ECO:0000269\|PubMed:17159994, ECO:0000269\|PubMed:25799998, ECO:0000269\|PubMed:26027739, ECO:0000269\|PubMed:26748718}.
Q8WZ73	RFFL	S36	ochoa	E3 ubiquitin-protein ligase rififylin (EC 2.3.2.27) (Caspase regulator CARP2) (Caspases-8 and -10-associated RING finger protein 2) (CARP-2) (FYVE-RING finger protein Sakura) (Fring) (RING finger and FYVE-like domain-containing protein 1) (RING finger protein 189) (RING finger protein 34-like) (RING-type E3 ubiquitin transferase rififylin)	E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269\|PubMed:15069192, ECO:0000269\|PubMed:17121812, ECO:0000269\|PubMed:18382127, ECO:0000269\|PubMed:18450452, ECO:0000269\|PubMed:22609986}.
Q8WZ75	ROBO4	S663	ochoa	Roundabout homolog 4 (Magic roundabout)	Receptor for Slit proteins, at least for SLIT2, and seems to be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins (By similarity). Involved in the maintenance of endothelial barrier organization and function (PubMed:30455415). {ECO:0000250, ECO:0000269\|PubMed:30455415}.
Q92545	TMEM131	S1342	ochoa	Transmembrane protein 131 (Protein RW1)	Collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII (PubMed:32095531). May play a role in the immune response to viral infection. {ECO:0000250, ECO:0000269\|PubMed:32095531}.
Q92545	TMEM131	S1627	ochoa	Transmembrane protein 131 (Protein RW1)	Collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII (PubMed:32095531). May play a role in the immune response to viral infection. {ECO:0000250, ECO:0000269\|PubMed:32095531}.
Q92574	TSC1	S282	ochoa	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92574	TSC1	S511	ochoa\|psp	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92574	TSC1	S521	ochoa	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92574	TSC1	S1046	ochoa	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92585	MAML1	S344	ochoa	Mastermind-like protein 1 (Mam-1)	Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions. {ECO:0000269\|PubMed:11101851, ECO:0000269\|PubMed:11390662, ECO:0000269\|PubMed:12050117, ECO:0000269\|PubMed:15546612, ECO:0000269\|PubMed:17317671}.
Q92597	NDRG1	S336	ochoa	Protein NDRG1 (Differentiation-related gene 1 protein) (DRG-1) (N-myc downstream-regulated gene 1 protein) (Nickel-specific induction protein Cap43) (Reducing agents and tunicamycin-responsive protein) (RTP) (Rit42)	Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy. {ECO:0000269\|PubMed:15247272, ECO:0000269\|PubMed:15377670, ECO:0000269\|PubMed:17786215, ECO:0000269\|PubMed:9766676}.
Q92609	TBC1D5	S544	ochoa	TBC1 domain family member 5	May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269\|PubMed:19531583, ECO:0000269\|PubMed:20923837, ECO:0000269\|PubMed:22354992, ECO:0000269\|PubMed:24603492, ECO:0000305\|PubMed:19531583, ECO:0000305\|PubMed:22354992, ECO:0000305\|PubMed:24603492}.
Q92609	TBC1D5	S564	ochoa	TBC1 domain family member 5	May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269\|PubMed:19531583, ECO:0000269\|PubMed:20923837, ECO:0000269\|PubMed:22354992, ECO:0000269\|PubMed:24603492, ECO:0000305\|PubMed:19531583, ECO:0000305\|PubMed:22354992, ECO:0000305\|PubMed:24603492}.
Q92609	TBC1D5	S732	ochoa	TBC1 domain family member 5	May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269\|PubMed:19531583, ECO:0000269\|PubMed:20923837, ECO:0000269\|PubMed:22354992, ECO:0000269\|PubMed:24603492, ECO:0000305\|PubMed:19531583, ECO:0000305\|PubMed:22354992, ECO:0000305\|PubMed:24603492}.
Q92610	ZNF592	S1027	ochoa	Zinc finger protein 592	May be involved in transcriptional regulation. {ECO:0000269\|PubMed:20531441}.
Q92613	JADE3	S572	ochoa	Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16)	Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. {ECO:0000269\|PubMed:16387653}.
Q92614	MYO18A	S157	ochoa	Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)	May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250\|UniProtKB:Q9JMH9, ECO:0000269\|PubMed:16087679, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:19837035, ECO:0000269\|PubMed:21123169, ECO:0000269\|PubMed:23345592, ECO:0000269\|PubMed:25965346, ECO:0000269\|PubMed:27467939}.
Q92614	MYO18A	S1076	ochoa	Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)	May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250\|UniProtKB:Q9JMH9, ECO:0000269\|PubMed:16087679, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:19837035, ECO:0000269\|PubMed:21123169, ECO:0000269\|PubMed:23345592, ECO:0000269\|PubMed:25965346, ECO:0000269\|PubMed:27467939}.
Q92619	ARHGAP45	S99	ochoa	Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1 (mHag HA-1)]	Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity. {ECO:0000269\|PubMed:24086303}.; FUNCTION: Precursor of the histocompatibility antigen HA-1. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. Specifically, mismatching for mHag HA-1 which is recognized as immunodominant, is shown to be associated with the development of severe GVHD after HLA-identical BMT. HA-1 is presented to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte (CTL) reactivity against hematologic malignancies after treatment by HLA-identical allogenic BMT. It induces cell recognition and lysis by CTL. {ECO:0000269\|PubMed:12601144, ECO:0000269\|PubMed:8260714, ECO:0000269\|PubMed:8532022, ECO:0000269\|PubMed:9798702}.
Q92619	ARHGAP45	S629	ochoa	Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1 (mHag HA-1)]	Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity. {ECO:0000269\|PubMed:24086303}.; FUNCTION: Precursor of the histocompatibility antigen HA-1. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. Specifically, mismatching for mHag HA-1 which is recognized as immunodominant, is shown to be associated with the development of severe GVHD after HLA-identical BMT. HA-1 is presented to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte (CTL) reactivity against hematologic malignancies after treatment by HLA-identical allogenic BMT. It induces cell recognition and lysis by CTL. {ECO:0000269\|PubMed:12601144, ECO:0000269\|PubMed:8260714, ECO:0000269\|PubMed:8532022, ECO:0000269\|PubMed:9798702}.
Q92622	RUBCN	S416	ochoa	Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (Rubicon) (Beclin-1 associated RUN domain containing protein) (Baron)	Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation (PubMed:20974968, PubMed:21062745). {ECO:0000269\|PubMed:20974968, ECO:0000269\|PubMed:21062745}.; FUNCTION: Involved in regulation of pathogen-specific host defense of activated macrophages. Following bacterial infection promotes NADH oxidase activity by association with CYBA thereby affecting TLR2 signaling and probably other TLR-NOX pathways. Stabilizes the CYBA:CYBB NADPH oxidase heterodimer, increases its association with TLR2 and its phagosome trafficking to induce antimicrobial burst of ROS and production of inflammatory cytokines (PubMed:22423966). Following fungal or viral infection (implicating CLEC7A (dectin-1)-mediated myeloid cell activation or RIGI-dependent sensing of RNA viruses) negatively regulates pro-inflammatory cytokine production by association with CARD9 and sequestering it from signaling complexes (PubMed:22423967). {ECO:0000269\|PubMed:22423966, ECO:0000269\|PubMed:22423967}.
Q92625	ANKS1A	S628	ochoa	Ankyrin repeat and SAM domain-containing protein 1A (Odin)	Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity). {ECO:0000250, ECO:0000269\|PubMed:17875921}.
Q92625	ANKS1A	S649	ochoa	Ankyrin repeat and SAM domain-containing protein 1A (Odin)	Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity). {ECO:0000250, ECO:0000269\|PubMed:17875921}.
Q92628	KIAA0232	S164	ochoa	Uncharacterized protein KIAA0232	None
Q92633	LPAR1	S347	ochoa	Lysophosphatidic acid receptor 1 (LPA receptor 1) (LPA-1) (Lysophosphatidic acid receptor Edg-2)	Receptor for lysophosphatidic acid (LPA) (PubMed:19306925, PubMed:25025571, PubMed:26091040, PubMed:9070858). Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:26091040). Signaling triggers an increase of cytoplasmic Ca(2+) levels (PubMed:19656035, PubMed:19733258, PubMed:26091040). Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:19306925). Signaling mediates activation of down-stream MAP kinases (By similarity). Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:26091040). Promotes the activation of Rho and the formation of actin stress fibers (PubMed:26091040). Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (By similarity). Through its function as LPA receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:18066075, PubMed:19656035, PubMed:19733258). Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to LPA (By similarity). Inhibits the intracellular ciliogenesis pathway in response to LPA and through AKT1 activation (PubMed:31204173). Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain (By similarity). {ECO:0000250\|UniProtKB:P61793, ECO:0000269\|PubMed:18066075, ECO:0000269\|PubMed:19306925, ECO:0000269\|PubMed:19656035, ECO:0000269\|PubMed:19733258, ECO:0000269\|PubMed:25025571, ECO:0000269\|PubMed:26091040, ECO:0000269\|PubMed:31204173, ECO:0000269\|PubMed:9070858, ECO:0000305\|PubMed:11093753, ECO:0000305\|PubMed:9069262}.
Q92667	AKAP1	S450	ochoa	A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 149 kDa) (AKAP 149) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84)	Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (PubMed:31522117). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity). {ECO:0000250\|UniProtKB:O08715, ECO:0000269\|PubMed:31522117}.
Q92736	RYR2	S2814	psp	Ryanodine receptor 2 (RYR-2) (RyR2) (hRYR-2) (Cardiac muscle ryanodine receptor) (Cardiac muscle ryanodine receptor-calcium release channel) (Type 2 ryanodine receptor)	Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) cytosolic levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development. {ECO:0000269\|PubMed:10830164, ECO:0000269\|PubMed:17984046, ECO:0000269\|PubMed:20056922, ECO:0000269\|PubMed:27733687, ECO:0000269\|PubMed:33536282}.
Q92766	RREB1	S42	ochoa	Ras-responsive element-binding protein 1 (RREB-1) (Finger protein in nuclear bodies) (Raf-responsive zinc finger protein LZ321) (Zinc finger motif enhancer-binding protein 1) (Zep-1)	Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters (PubMed:10390538, PubMed:15067362, PubMed:17550981, PubMed:8816445, PubMed:9305772). Represses the angiotensinogen gene (PubMed:15067362). Negatively regulates the transcriptional activity of AR (PubMed:17550981). Potentiates the transcriptional activity of NEUROD1 (PubMed:12482979). Promotes brown adipocyte differentiation (By similarity). May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression (PubMed:8816445). {ECO:0000250\|UniProtKB:Q3UH06, ECO:0000269\|PubMed:10390538, ECO:0000269\|PubMed:12482979, ECO:0000269\|PubMed:15067362, ECO:0000269\|PubMed:17550981, ECO:0000269\|PubMed:8816445, ECO:0000269\|PubMed:9305772}.
Q92805	GOLGA1	S36	ochoa	Golgin subfamily A member 1 (Golgin-97)	Involved in vesicular trafficking at the Golgi apparatus level. Involved in endosome-to-Golgi trafficking. Mechanistically, captures transport vesicles arriving from endosomes via the protein TBC1D23 (PubMed:29084197, PubMed:38552021). Recognized vesicles are then tethered to the trans-Golgi before subsequent SNARE engagement and vesicle fusion. Selectively regulates E-cadherin transport from the trans-Golgi network in tubulovesicular carriers (PubMed:34969853). {ECO:0000269\|PubMed:29084197, ECO:0000269\|PubMed:34969853, ECO:0000269\|PubMed:38552021}.; FUNCTION: (Microbial infection) Plays an important role in poxvirus morphogenesis. Translocates into the viral factories where it may transport the membrane fragments and associated protein factors important for virus maturation to the sites of virion assembly. {ECO:0000269\|PubMed:17276477}.
Q92859	NEO1	S1220	ochoa	Neogenin (Immunoglobulin superfamily DCC subclass member 2)	Multi-functional cell surface receptor regulating cell adhesion in many diverse developmental processes, including neural tube and mammary gland formation, myogenesis and angiogenesis. Receptor for members of the BMP, netrin, and repulsive guidance molecule (RGM) families. Netrin-Neogenin interactions result in a chemoattractive axon guidance response and cell-cell adhesion, the interaction between NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response. {ECO:0000269\|PubMed:21149453}.
Q92925	SMARCD2	S211	ochoa	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 (60 kDa BRG-1/Brm-associated factor subunit B) (BRG1-associated factor 60B) (BAF60B)	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:22952240, PubMed:26601204). Critical regulator of myeloid differentiation, controlling granulocytopoiesis and the expression of genes involved in neutrophil granule formation (PubMed:28369036). {ECO:0000269\|PubMed:28369036, ECO:0000303\|PubMed:22952240, ECO:0000303\|PubMed:26601204}.
Q92934	BAD	S124	ochoa\|psp	Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-2-like protein 8) (Bcl2-L-8) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)	Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. {ECO:0000250}.
Q92945	KHSRP	S131	ochoa	Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (p75)	Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs. {ECO:0000250, ECO:0000269\|PubMed:11003644, ECO:0000269\|PubMed:8940189, ECO:0000269\|PubMed:9136930}.
Q92974	ARHGEF2	S127	ochoa	Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40)	Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250\|UniProtKB:Q60875, ECO:0000250\|UniProtKB:Q865S3, ECO:0000269\|PubMed:19043560, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:28453519, ECO:0000269\|PubMed:9857026}.
Q92994	BRF1	S442	ochoa	Transcription factor IIIB 90 kDa subunit (TFIIIB90) (hTFIIIB90) (B-related factor 1) (BRF-1) (hBRF) (TAF3B2) (TATA box-binding protein-associated factor, RNA polymerase III, subunit 2)	General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.
Q92994	BRF1	S553	ochoa	Transcription factor IIIB 90 kDa subunit (TFIIIB90) (hTFIIIB90) (B-related factor 1) (BRF-1) (hBRF) (TAF3B2) (TATA box-binding protein-associated factor, RNA polymerase III, subunit 2)	General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.
Q92997	DVL3	S208	ochoa\|psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S209	ochoa\|psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S570	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S573	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S576	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S611	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S639	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S642	ochoa\|psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q93052	LPP	S151	ochoa	Lipoma-preferred partner (LIM domain-containing preferred translocation partner in lipoma)	May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. {ECO:0000269\|PubMed:10637295}.
Q93052	LPP	S246	ochoa	Lipoma-preferred partner (LIM domain-containing preferred translocation partner in lipoma)	May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. {ECO:0000269\|PubMed:10637295}.
Q969R5	L3MBTL2	S73	ochoa	Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2)	Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. {ECO:0000269\|PubMed:19233876}.
Q969R5	L3MBTL2	S79	ochoa	Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2)	Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. {ECO:0000269\|PubMed:19233876}.
Q969R5	L3MBTL2	S85	ochoa	Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2)	Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. {ECO:0000269\|PubMed:19233876}.
Q969T4	UBE2E3	S20	ochoa	Ubiquitin-conjugating enzyme E2 E3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme E3) (UbcH9) (Ubiquitin carrier protein E3) (Ubiquitin-conjugating enzyme E2-23 kDa) (Ubiquitin-protein ligase E3)	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. {ECO:0000269\|PubMed:10343118, ECO:0000269\|PubMed:20061386, ECO:0000269\|PubMed:27237050}.
Q969V6	MRTFA	S139	ochoa	Myocardin-related transcription factor A (MRTF-A) (MKL/myocardin-like protein 1) (Megakaryoblastic leukemia 1 protein) (Megakaryocytic acute leukemia protein)	Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:26224645). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex. Activity is also regulated by filamentous actin (F-actin) in the nucleus. {ECO:0000250\|UniProtKB:Q8K4J6, ECO:0000269\|PubMed:26224645}.
Q96A57	TMEM230	S20	ochoa	Transmembrane protein 230	Involved in trafficking and recycling of synaptic vesicles. {ECO:0000269\|PubMed:27270108}.
Q96AC1	FERMT2	S181	ochoa\|psp	Fermitin family homolog 2 (Kindlin-2) (Mitogen-inducible gene 2 protein) (MIG-2) (Pleckstrin homology domain-containing family C member 1) (PH domain-containing family C member 1)	Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling. {ECO:0000269\|PubMed:12679033, ECO:0000269\|PubMed:18458155, ECO:0000269\|PubMed:21325030, ECO:0000269\|PubMed:22030399, ECO:0000269\|PubMed:22078565, ECO:0000269\|PubMed:22699938}.
Q96AC1	FERMT2	S186	psp	Fermitin family homolog 2 (Kindlin-2) (Mitogen-inducible gene 2 protein) (MIG-2) (Pleckstrin homology domain-containing family C member 1) (PH domain-containing family C member 1)	Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling. {ECO:0000269\|PubMed:12679033, ECO:0000269\|PubMed:18458155, ECO:0000269\|PubMed:21325030, ECO:0000269\|PubMed:22030399, ECO:0000269\|PubMed:22078565, ECO:0000269\|PubMed:22699938}.
Q96AY2	EME1	S117	ochoa	Structure-specific endonuclease subunit EME1 (Crossover junction endonuclease EME1) (Essential meiotic structure-specific endonuclease 1) (MMS4 homolog) (hMMS4)	Non-catalytic subunit of the structure-specific, heterodimeric DNA endonuclease MUS81-EME1 which is involved in the maintenance of genome stability. In the complex, EME1 is required for DNA cleavage, participating in DNA recognition and bending (PubMed:12686547, PubMed:12721304, PubMed:14617801, PubMed:17289582, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). MUS81-EME1 cleaves 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24733841, PubMed:35290797). Active during prometaphase, MUS81-EME1 resolves mitotic recombination intermediates, including Holliday junctions, which form during homologous recombination (PubMed:14617801, PubMed:24813886). {ECO:0000269\|PubMed:12686547, ECO:0000269\|PubMed:12721304, ECO:0000269\|PubMed:14617801, ECO:0000269\|PubMed:17289582, ECO:0000269\|PubMed:24733841, ECO:0000269\|PubMed:24813886, ECO:0000269\|PubMed:35290797, ECO:0000269\|PubMed:39015284}.
Q96B97	SH3KBP1	S85	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96B97	SH3KBP1	S189	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96B97	SH3KBP1	S509	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96BR9	ZBTB8A	S167	ochoa	Zinc finger and BTB domain-containing protein 8A (BTB/POZ and zinc-finger domain-containing factor) (BTB/POZ and zinc-finger domains factor on chromosome 1) (BOZ-F1)	May be involved in transcriptional regulation.
Q96BT3	CENPT	S403	ochoa	Centromere protein T (CENP-T) (Interphase centromere complex protein 22)	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000269\|PubMed:16716197, ECO:0000269\|PubMed:21529714, ECO:0000269\|PubMed:21695110}.
Q96BY6	DOCK10	S1298	ochoa	Dedicator of cytokinesis protein 10 (Zizimin-3)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic spine morphogenesis in Purkinje cells and in hippocampal neurons, via a CDC42-mediated pathway. Sustains B-cell lymphopoiesis in secondary lymphoid tissues and regulates FCER2/CD23 expression. {ECO:0000250\|UniProtKB:Q8BZN6}.
Q96BY9	SARAF	S314	ochoa	Store-operated calcium entry-associated regulatory factor (SARAF) (SOCE-associated regulatory factor) (HBV X-transactivated gene 3 protein) (HBV XAg-transactivated protein 3) (Protein FOAP-7) (Transmembrane protein 66)	Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions. {ECO:0000269\|PubMed:22464749}.
Q96C24	SYTL4	S217	ochoa	Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin)	Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). {ECO:0000250}.
Q96CV9	OPTN	S177	ochoa\|psp	Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)	Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269\|PubMed:11834836, ECO:0000269\|PubMed:15837803, ECO:0000269\|PubMed:20085643, ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:21617041, ECO:0000269\|PubMed:22854040, ECO:0000269\|PubMed:27534431, ECO:0000269\|PubMed:27538435}.; FUNCTION: (Microbial infection) May constitute a cellular target for various viruses, such as adenovirus E3 14.7 or Bluetongue virus, to inhibit innate immune response (PubMed:27538435, PubMed:9488477). During RNA virus infection, such as that of Sendai virus, negatively regulates the induction of IFNB1 (PubMed:20174559). {ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:27538435, ECO:0000269\|PubMed:9488477}.
Q96CV9	OPTN	S519	ochoa	Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)	Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269\|PubMed:11834836, ECO:0000269\|PubMed:15837803, ECO:0000269\|PubMed:20085643, ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:21617041, ECO:0000269\|PubMed:22854040, ECO:0000269\|PubMed:27534431, ECO:0000269\|PubMed:27538435}.; FUNCTION: (Microbial infection) May constitute a cellular target for various viruses, such as adenovirus E3 14.7 or Bluetongue virus, to inhibit innate immune response (PubMed:27538435, PubMed:9488477). During RNA virus infection, such as that of Sendai virus, negatively regulates the induction of IFNB1 (PubMed:20174559). {ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:27538435, ECO:0000269\|PubMed:9488477}.
Q96CW1	AP2M1	S240	ochoa	AP-2 complex subunit mu (AP-2 mu chain) (Adaptin-mu2) (Adaptor protein complex AP-2 subunit mu) (Adaptor-related protein complex 2 subunit mu) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (HA2 50 kDa subunit) (Plasma membrane adaptor AP-2 50 kDa protein)	Component of the adaptor protein complex 2 (AP-2) (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis (PubMed:16581796). AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway (PubMed:19033387). During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2 (PubMed:11877457). The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (PubMed:11877457). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). {ECO:0000250\|UniProtKB:P84092, ECO:0000269\|PubMed:11877457, ECO:0000269\|PubMed:12694563, ECO:0000269\|PubMed:12952941, ECO:0000269\|PubMed:14745134, ECO:0000269\|PubMed:14985334, ECO:0000269\|PubMed:15473838, ECO:0000269\|PubMed:16581796, ECO:0000269\|PubMed:19033387, ECO:0000269\|PubMed:23676497, ECO:0000269\|PubMed:31104773}.
Q96CX2	KCTD12	S204	ochoa	BTB/POZ domain-containing protein KCTD12 (Pfetin) (Predominantly fetal expressed T1 domain)	Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity). {ECO:0000250}.
Q96D46	NMD3	S468	ochoa	60S ribosomal export protein NMD3 (hNMD3)	Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269\|PubMed:12724356, ECO:0000269\|PubMed:12773398}.
Q96DR7	ARHGEF26	S329	ochoa	Rho guanine nucleotide exchange factor 26 (SH3 domain-containing guanine exchange factor)	Activates RhoG GTPase by promoting the exchange of GDP by GTP. Required for the formation of membrane ruffles during macropinocytosis. Required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB, which induces cytoskeleton rearrangements and promotes bacterial entry. {ECO:0000269\|PubMed:15133129, ECO:0000269\|PubMed:17074883, ECO:0000269\|PubMed:17875742}.
Q96DY7	MTBP	S545	ochoa	Mdm2-binding protein (hMTBP)	Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells (By similarity). May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. {ECO:0000250, ECO:0000269\|PubMed:15632057}.
Q96E39	RBMXL1	S314	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96E39	RBMXL1	S329	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96E39	RBMXL1	S332	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96EB6	SIRT1	S545	ochoa	NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]	NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17290224, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21947282, PubMed:22274616, PubMed:22918831, PubMed:24415752, PubMed:24824780, PubMed:29681526, PubMed:29765047, PubMed:30409912). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (PubMed:15469825). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (PubMed:14976264, PubMed:14980222, PubMed:15152190). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (PubMed:15205477). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (By similarity). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (PubMed:21504832). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:19188449). Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (PubMed:20375098). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (By similarity). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (PubMed:18004385, PubMed:21504832). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (PubMed:18004385, PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672523, PubMed:12006491, PubMed:22542455). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (By similarity). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (PubMed:19364925, PubMed:21807113). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (PubMed:14976264, PubMed:14980222, PubMed:21841822). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (PubMed:15126506). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (PubMed:15152190). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17283066, PubMed:17620057, PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15692560). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (PubMed:12535671). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (PubMed:17505061). Represses HNF1A-mediated transcription (By similarity). Required for the repression of ESRRG by CREBZF (PubMed:19690166). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (PubMed:20817729, PubMed:29765047). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (By similarity). Deacetylates p300/EP300 and PRMT1 (By similarity). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:21701047). Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (PubMed:17290224, PubMed:20817729). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (PubMed:15205477, PubMed:16998810, PubMed:17334224, PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (PubMed:15205477, PubMed:17334224, PubMed:20097625). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (PubMed:32538779). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (PubMed:19934257). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (PubMed:32034146). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (PubMed:21775285). Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (PubMed:18687677, PubMed:20203304). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (PubMed:21890893). Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (PubMed:22274616). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (By similarity). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (By similarity). Protects cardiomyocytes against palmitate-induced apoptosis (By similarity). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (By similarity). Involved in the regulation of centrosome duplication: deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (PubMed:31722219). Deacetylates NDC80/HEC1 (PubMed:30409912). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein delactylation, depropionylation and decrotonylation (PubMed:28497810, PubMed:38512451). Mediates depropionylation of Osterix (SP7) (By similarity). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (PubMed:28497810). Mediates protein delactylation of TEAD1 and YAP1 (PubMed:38512451). {ECO:0000250\|UniProtKB:Q923E4, ECO:0000269\|PubMed:11672523, ECO:0000269\|PubMed:12006491, ECO:0000269\|PubMed:12535671, ECO:0000269\|PubMed:14976264, ECO:0000269\|PubMed:14980222, ECO:0000269\|PubMed:15126506, ECO:0000269\|PubMed:15152190, ECO:0000269\|PubMed:15205477, ECO:0000269\|PubMed:15469825, ECO:0000269\|PubMed:15692560, ECO:0000269\|PubMed:16079181, ECO:0000269\|PubMed:16166628, ECO:0000269\|PubMed:16892051, ECO:0000269\|PubMed:16998810, ECO:0000269\|PubMed:17283066, ECO:0000269\|PubMed:17290224, ECO:0000269\|PubMed:17334224, ECO:0000269\|PubMed:17505061, ECO:0000269\|PubMed:17612497, ECO:0000269\|PubMed:17620057, ECO:0000269\|PubMed:17936707, ECO:0000269\|PubMed:18203716, ECO:0000269\|PubMed:18296641, ECO:0000269\|PubMed:18485871, ECO:0000269\|PubMed:18662546, ECO:0000269\|PubMed:18687677, ECO:0000269\|PubMed:19188449, ECO:0000269\|PubMed:19220062, ECO:0000269\|PubMed:19364925, ECO:0000269\|PubMed:19690166, ECO:0000269\|PubMed:19934257, ECO:0000269\|PubMed:20097625, ECO:0000269\|PubMed:20100829, ECO:0000269\|PubMed:20203304, ECO:0000269\|PubMed:20375098, ECO:0000269\|PubMed:20620956, ECO:0000269\|PubMed:20670893, ECO:0000269\|PubMed:20817729, ECO:0000269\|PubMed:20955178, ECO:0000269\|PubMed:21149730, ECO:0000269\|PubMed:21245319, ECO:0000269\|PubMed:21471201, ECO:0000269\|PubMed:21504832, ECO:0000269\|PubMed:21555002, ECO:0000269\|PubMed:21698133, ECO:0000269\|PubMed:21701047, ECO:0000269\|PubMed:21775285, ECO:0000269\|PubMed:21807113, ECO:0000269\|PubMed:21841822, ECO:0000269\|PubMed:21890893, ECO:0000269\|PubMed:21947282, ECO:0000269\|PubMed:22274616, ECO:0000269\|PubMed:22542455, ECO:0000269\|PubMed:22918831, ECO:0000269\|PubMed:23142079, ECO:0000269\|PubMed:24415752, ECO:0000269\|PubMed:24824780, ECO:0000269\|PubMed:28497810, ECO:0000269\|PubMed:29681526, ECO:0000269\|PubMed:29765047, ECO:0000269\|PubMed:30193097, ECO:0000269\|PubMed:30409912, ECO:0000269\|PubMed:31722219, ECO:0000269\|PubMed:32034146, ECO:0000269\|PubMed:32538779, ECO:0000269\|PubMed:38512451}.; FUNCTION: [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. {ECO:0000269\|PubMed:20975832}.; FUNCTION: [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000269\|PubMed:21987377}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. {ECO:0000269\|PubMed:18329615}.
Q96EY5	MVB12A	S208	ochoa	Multivesicular body subunit 12A (CIN85/CD2AP family-binding protein) (ESCRT-I complex subunit MVB12A) (Protein FAM125A)	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down-regulation of EGF receptor. {ECO:0000269\|PubMed:16895919}.
Q96F45	ZNF503	S234	ochoa	Zinc finger protein 503	May function as a transcriptional repressor. {ECO:0000250}.
Q96F45	ZNF503	S237	ochoa	Zinc finger protein 503	May function as a transcriptional repressor. {ECO:0000250}.
Q96FA3	PELI1	S82	psp	E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (Pellino-related intracellular-signaling molecule) (RING-type E3 ubiquitin transferase pellino homolog 1)	E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:12496252, PubMed:17675297, PubMed:29883609, PubMed:30952868). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6 (PubMed:12496252, PubMed:17675297). Acts as a positive regulator of inflammatory response in microglia through activation of NF-kappa-B and MAP kinase (By similarity). Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (PubMed:12496252, PubMed:17675297). Conjugates 'Lys-63'-linked ubiquitin chains to the adapter protein ASC/PYCARD, which in turn is crucial for NLRP3 inflammasome activation (PubMed:34706239). Mediates 'Lys-48'-linked polyubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation; preferentially recognizes and mediates the degradation of the 'Thr-182' phosphorylated form of RIPK3 (PubMed:29883609). Negatively regulates necroptosis by reducing RIPK3 expression (PubMed:29883609). Mediates 'Lys-63'-linked ubiquitination of RIPK1 (PubMed:29883609). Following phosphorylation by ATM, catalyzes 'Lys-63'-linked ubiquitination of NBN, promoting DNA repair via homologous recombination (PubMed:30952868). Negatively regulates activation of the metabolic mTORC1 signaling pathway by mediating 'Lys-63'-linked ubiquitination of mTORC1-inhibitory protein TSC1 and thereby promoting TSC1/TSC2 complex stability (PubMed:33215753). {ECO:0000250\|UniProtKB:Q8C669, ECO:0000269\|PubMed:12496252, ECO:0000269\|PubMed:17675297, ECO:0000269\|PubMed:29883609, ECO:0000269\|PubMed:30952868, ECO:0000269\|PubMed:33215753}.
Q96FF9	CDCA5	S164	ochoa\|psp	Sororin (Cell division cycle-associated protein 5) (p35)	Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair. {ECO:0000269\|PubMed:15837422, ECO:0000269\|PubMed:17349791, ECO:0000269\|PubMed:21111234}.
Q96FS4	SIPA1	S845	ochoa	Signal-induced proliferation-associated protein 1 (Sipa-1) (GTPase-activating protein Spa-1) (p130 SPA-1)	GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting them to the putatively inactive GDP-bound state (PubMed:9346962). Affects cell cycle progression (By similarity). {ECO:0000250\|UniProtKB:P46062, ECO:0000269\|PubMed:9346962}.
Q96G01	BICD1	S616	ochoa	Protein bicaudal D homolog 1 (Bic-D 1)	Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.
Q96GX5	MASTL	S376	ochoa	Serine/threonine-protein kinase greatwall (GW) (GWL) (hGWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L)	Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance (PubMed:19680222). Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively (PubMed:38123684). ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high (PubMed:20818157). Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation. {ECO:0000269\|PubMed:12890928, ECO:0000269\|PubMed:19680222, ECO:0000269\|PubMed:19793917, ECO:0000269\|PubMed:20538976, ECO:0000269\|PubMed:20818157, ECO:0000269\|PubMed:38123684}.
Q96H79	ZC3HAV1L	S263	ochoa	Zinc finger CCCH-type antiviral protein 1-like	None
Q96HA1	POM121	S351	ochoa	Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
Q96HB5	CCDC120	S302	ochoa	Coiled-coil domain-containing protein 120	Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth. {ECO:0000269\|PubMed:25326380}.
Q96HC4	PDLIM5	S217	ochoa	PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein)	May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation. {ECO:0000250\|UniProtKB:Q62920}.
Q96HC4	PDLIM5	S319	ochoa	PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein)	May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation. {ECO:0000250\|UniProtKB:Q62920}.
Q96HC4	PDLIM5	S383	ochoa	PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein)	May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation. {ECO:0000250\|UniProtKB:Q62920}.
Q96HC4	PDLIM5	S385	ochoa	PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein)	May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation. {ECO:0000250\|UniProtKB:Q62920}.
Q96HN2	AHCYL2	S155	psp	Adenosylhomocysteinase 3 (AdoHcyase 3) (EC 3.13.2.1) (IP(3)Rs binding protein released with IP(3) 2) (IRBIT2) (Long-IRBIT) (S-adenosyl-L-homocysteine hydrolase 3) (S-adenosylhomocysteine hydrolase-like protein 2)	May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (PubMed:19220705). {ECO:0000250\|UniProtKB:A6QLP2, ECO:0000269\|PubMed:19220705}.
Q96HN2	AHCYL2	S158	psp	Adenosylhomocysteinase 3 (AdoHcyase 3) (EC 3.13.2.1) (IP(3)Rs binding protein released with IP(3) 2) (IRBIT2) (Long-IRBIT) (S-adenosyl-L-homocysteine hydrolase 3) (S-adenosylhomocysteine hydrolase-like protein 2)	May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (PubMed:19220705). {ECO:0000250\|UniProtKB:A6QLP2, ECO:0000269\|PubMed:19220705}.
Q96J84	KIRREL1	S645	ochoa	Kin of IRRE-like protein 1 (Kin of irregular chiasm-like protein 1) (Nephrin-like protein 1)	Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (PubMed:31472902). It is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity). {ECO:0000250, ECO:0000269\|PubMed:31472902}.
Q96JB2	COG3	S533	ochoa	Conserved oligomeric Golgi complex subunit 3 (COG complex subunit 3) (Component of oligomeric Golgi complex 3) (Vesicle-docking protein SEC34 homolog) (p94)	Involved in ER-Golgi transport (PubMed:11929878). Also involved in retrograde (Golgi to ER) transport (PubMed:37711075). {ECO:0000269\|PubMed:11929878, ECO:0000269\|PubMed:37711075}.
Q96JE7	SEC16B	S173	ochoa	Protein transport protein Sec16B (Leucine zipper transcription regulator 2) (Regucalcin gene promoter region-related protein p117) (RGPR-p117) (SEC16 homolog B)	Plays a role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17192411, PubMed:21768384, PubMed:22355596). Involved in peroxisome biogenesis. Regulates the transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER to peroxisomes (PubMed:21768384). {ECO:0000269\|PubMed:17192411, ECO:0000269\|PubMed:21768384, ECO:0000303\|PubMed:22355596}.
Q96JG6	VPS50	S552	ochoa	Syndetin (Coiled-coil domain-containing protein 132) (EARP/GARPII complex subunit VPS50)	Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). {ECO:0000269\|PubMed:25799061}.
Q96JH8	RADIL	S963	ochoa	Ras-associating and dilute domain-containing protein	Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development. {ECO:0000269\|PubMed:17704304}.
Q96JI7	SPG11	S1961	ochoa	Spatacsin (Colorectal carcinoma-associated protein) (Spastic paraplegia 11 protein)	May play a role in neurite plasticity by maintaining cytoskeleton stability and regulating synaptic vesicle transport. {ECO:0000269\|PubMed:24794856}.
Q96JK2	DCAF5	S651	ochoa	DDB1- and CUL4-associated factor 5 (Breakpoint cluster region protein 2) (BCRP2) (WD repeat-containing protein 22)	Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin-protein ligase complex (CRL4) (PubMed:29691401, PubMed:30442713). The complex CRL4-DCAF5 is involved in the ubiquitination of a set of methylated non-histone proteins, including SOX2, DNMT1 and E2F1 (PubMed:29691401, PubMed:30442713). {ECO:0000269\|PubMed:16949367, ECO:0000269\|PubMed:16964240, ECO:0000269\|PubMed:29691401, ECO:0000269\|PubMed:30442713}.
Q96JM3	CHAMP1	S468	ochoa	Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)	Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269\|PubMed:21063390}.
Q96JM3	CHAMP1	S482	ochoa	Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)	Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269\|PubMed:21063390}.
Q96JQ2	CLMN	S157	ochoa	Calmin (Calponin-like transmembrane domain protein)	None
Q96JQ2	CLMN	S927	ochoa	Calmin (Calponin-like transmembrane domain protein)	None
Q96JY6	PDLIM2	S127	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96JY6	PDLIM2	S143	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96JY6	PDLIM2	S203	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96JY6	PDLIM2	S209	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96K76	USP47	S903	ochoa	Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47)	Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level. {ECO:0000269\|PubMed:19966869, ECO:0000269\|PubMed:21362556}.
Q96KP1	EXOC2	S422	ochoa	Exocyst complex component 2 (Exocyst complex component Sec5)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269\|PubMed:12459492, ECO:0000269\|PubMed:32639540}.
Q96KP1	EXOC2	S432	ochoa	Exocyst complex component 2 (Exocyst complex component Sec5)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269\|PubMed:12459492, ECO:0000269\|PubMed:32639540}.
Q96KR1	ZFR	S481	ochoa	Zinc finger RNA-binding protein (hZFR) (M-phase phosphoprotein homolog)	Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA (By similarity). {ECO:0000250}.
Q96LR5	UBE2E2	S19	ochoa	Ubiquitin-conjugating enzyme E2 E2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme E2) (UbcH8) (Ubiquitin carrier protein E2) (Ubiquitin-protein ligase E2)	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000269\|PubMed:20061386, ECO:0000269\|PubMed:20133869, ECO:0000269\|PubMed:27237050, ECO:0000269\|PubMed:9371400}.
Q96LZ7	RMDN2	S143	ochoa	Regulator of microtubule dynamics protein 2 (RMD-2) (hRMD-2) (Protein FAM82A1)	None
Q96MG7	NSMCE3	S57	ochoa	Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (Hepatocellular carcinoma-associated protein 4) (MAGE-G1 antigen) (Melanoma-associated antigen G1) (Necdin-like protein 2)	Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination (PubMed:20864041, PubMed:27427983). The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (PubMed:20864041). May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest (By similarity). {ECO:0000250\|UniProtKB:Q9CPR8, ECO:0000269\|PubMed:20864041, ECO:0000269\|PubMed:27427983}.
Q96MU7	YTHDC1	S152	ochoa	YTH domain-containing protein 1 (Splicing factor YT521) (YT521-B)	Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). {ECO:0000250\|UniProtKB:E9Q5K9, ECO:0000269\|PubMed:20167602, ECO:0000269\|PubMed:25242552, ECO:0000269\|PubMed:26318451, ECO:0000269\|PubMed:26876937, ECO:0000269\|PubMed:27602518, ECO:0000269\|PubMed:28984244, ECO:0000269\|PubMed:32663306}.
Q96MU7	YTHDC1	S326	ochoa	YTH domain-containing protein 1 (Splicing factor YT521) (YT521-B)	Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). {ECO:0000250\|UniProtKB:E9Q5K9, ECO:0000269\|PubMed:20167602, ECO:0000269\|PubMed:25242552, ECO:0000269\|PubMed:26318451, ECO:0000269\|PubMed:26876937, ECO:0000269\|PubMed:27602518, ECO:0000269\|PubMed:28984244, ECO:0000269\|PubMed:32663306}.
Q96N66	MBOAT7	S291	ochoa	Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7 (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (Bladder and breast carcinoma-overexpressed gene 1 protein) (Leukocyte receptor cluster member 4) (Lysophosphatidylinositol acyltransferase) (LPIAT) (Lyso-PI acyltransferase) (Lysophospholipid acyltransferase 7) (LPLAT 7) (Membrane-bound O-acyltransferase domain-containing protein 7) (O-acyltransferase domain-containing protein 7) (h-mboa-7)	Acyltransferase which catalyzes the transfer of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (PubMed:18094042, PubMed:18772128). Prefers arachidonoyl-CoA as the acyl donor, thus contributing to the regulation of free levels arachidonic acid in cell (PubMed:18094042, PubMed:18772128). In liver, participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation (PubMed:32253259). {ECO:0000269\|PubMed:18094042, ECO:0000269\|PubMed:18772128, ECO:0000269\|PubMed:32253259}.
Q96N67	DOCK7	S888	ochoa	Dedicator of cytokinesis protein 7	Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250\|UniProtKB:Q8R1A4, ECO:0000269\|PubMed:16982419, ECO:0000269\|PubMed:29467281}.
Q96N67	DOCK7	S970	ochoa	Dedicator of cytokinesis protein 7	Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250\|UniProtKB:Q8R1A4, ECO:0000269\|PubMed:16982419, ECO:0000269\|PubMed:29467281}.
Q96N67	DOCK7	S1438	ochoa	Dedicator of cytokinesis protein 7	Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250\|UniProtKB:Q8R1A4, ECO:0000269\|PubMed:16982419, ECO:0000269\|PubMed:29467281}.
Q96NE9	FRMD6	S391	ochoa	FERM domain-containing protein 6 (Willin)	None
Q96NE9	FRMD6	S512	ochoa	FERM domain-containing protein 6 (Willin)	None
Q96NU1	SAMD11	S646	ochoa	Sterile alpha motif domain-containing protein 11 (SAM domain-containing protein 11)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, essential for establishing rod photoreceptor cell identity and function by silencing nonrod gene expression in developing rod photoreceptor cells. {ECO:0000250\|UniProtKB:Q1RNF8}.
Q96NY7	CLIC6	S299	ochoa	Chloride intracellular channel protein 6 (Glutaredoxin-like oxidoreductase CLIC6) (EC 1.8.-.-) (Parchorin)	In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor (By similarity). Can insert into membranes and form voltage-dependent chloride-selective channels. The channel opens upon membrane depolarization at positive voltages and closes at negative membrane voltages (PubMed:37838179). May play a critical role in water-secreting cells, possibly through the regulation of chloride ion transport (By similarity). {ECO:0000250\|UniProtKB:Q9N2G5, ECO:0000250\|UniProtKB:Q9Y696, ECO:0000269\|PubMed:37838179}.
Q96NY9	MUS81	S101	ochoa	Structure-specific endonuclease subunit MUS81 (EC 3.1.22.-) (Crossover junction endonuclease MUS81) (MUS81 endonuclease homolog)	Catalytic subunit of two functionally distinct, structure-specific, heterodimeric DNA endonucleases MUS81-EME1 and MUS81-EME2 that are involved in the maintenance of genome stability (PubMed:11741546, PubMed:12374758, PubMed:12686547, PubMed:12721304, PubMed:24371268, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). Both endonucleases have essentially the same substrate specificity though MUS81-EME2 is more active than its MUS81-EME1 counterpart. Both cleave 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24371268, PubMed:24733841, PubMed:35290797). MUS81-EME2 which is active during the replication of DNA is more specifically involved in replication fork processing (PubMed:24813886). Replication forks frequently encounter obstacles to their passage, including DNA base lesions, DNA interstrand cross-links, difficult-to-replicate sequences, transcription bubbles, or tightly bound proteins. One mechanism for the restart of a stalled replication fork involves nucleolytic cleavage mediated by the MUS81-EME2 endonuclease. By acting upon the stalled fork, MUS81-EME2 generates a DNA double-strand break (DSB) that can be repaired by homologous recombination, leading to the restoration of an active fork (PubMed:24813886). MUS81-EME2 could also function in telomere maintenance (PubMed:24813886). MUS81-EME1, on the other hand, is active later in the cell cycle and functions in the resolution of mitotic recombination intermediates including the Holliday junctions, the four-way DNA intermediates that form during homologous recombination (PubMed:11741546, PubMed:12374758, PubMed:14617801, PubMed:15805243, PubMed:24813886). {ECO:0000269\|PubMed:11741546, ECO:0000269\|PubMed:12374758, ECO:0000269\|PubMed:12686547, ECO:0000269\|PubMed:12721304, ECO:0000269\|PubMed:14617801, ECO:0000269\|PubMed:15805243, ECO:0000269\|PubMed:24371268, ECO:0000269\|PubMed:24733841, ECO:0000269\|PubMed:24813886, ECO:0000269\|PubMed:35290797, ECO:0000269\|PubMed:39015284}.
Q96PC5	MIA2	S1243	ochoa	Melanoma inhibitory activity protein 2 (MIA protein 2) (CTAGE family member 5 ER export factor) (Cutaneous T-cell lymphoma-associated antigen 5) (Meningioma-expressed antigen 6/11)	Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum (PubMed:21525241, PubMed:25202031, PubMed:27138255, PubMed:27170179). Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum (PubMed:27138255). Thereby, may play a role in cholesterol and triglyceride homeostasis (By similarity). Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites (PubMed:21525241, PubMed:25202031, PubMed:27170179). {ECO:0000250\|UniProtKB:Q91ZV0, ECO:0000269\|PubMed:21525241, ECO:0000269\|PubMed:25202031, ECO:0000269\|PubMed:27138255, ECO:0000269\|PubMed:27170179}.
Q96PD2	DCBLD2	S606	ochoa	Discoidin, CUB and LCCL domain-containing protein 2 (CUB, LCCL and coagulation factor V/VIII-homology domains protein 1) (Endothelial and smooth muscle cell-derived neuropilin-like protein)	None
Q96PE1	ADGRA2	S1122	ochoa	Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (Tumor endothelial marker 5)	Endothelial receptor which functions together with RECK to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:28289266, PubMed:30026314). Plays a key role in Wnt7-specific responses, such as endothelial cell sprouting and migration in the forebrain and neural tube, and establishment of the blood-brain barrier (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (PubMed:30026314). ADGRA2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly (PubMed:30026314). Binds to the glycosaminoglycans heparin, heparin sulfate, chondroitin sulfate and dermatan sulfate (PubMed:16982628). {ECO:0000250\|UniProtKB:Q91ZV8, ECO:0000269\|PubMed:16982628, ECO:0000269\|PubMed:28289266, ECO:0000269\|PubMed:30026314}.
Q96PE2	ARHGEF17	S469	ochoa	Rho guanine nucleotide exchange factor 17 (164 kDa Rho-specific guanine-nucleotide exchange factor) (p164-RhoGEF) (p164RhoGEF) (Tumor endothelial marker 4)	Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPases. {ECO:0000269\|PubMed:12071859}.
Q96PN7	TRERF1	S762	ochoa	Transcriptional-regulating factor 1 (Breast cancer anti-estrogen resistance 2) (Transcriptional-regulating protein 132) (Zinc finger protein rapa) (Zinc finger transcription factor TReP-132)	Binds DNA and activates transcription of CYP11A1. Interaction with CREBBP and EP300 results in a synergistic transcriptional activation of CYP11A1. {ECO:0000269\|PubMed:11349124, ECO:0000269\|PubMed:16371131}.
Q96PU4	UHRF2	S673	ochoa	E3 ubiquitin-protein ligase UHRF2 (EC 2.3.2.27) (Np95/ICBP90-like RING finger protein) (Np95-like RING finger protein) (Nuclear protein 97) (Nuclear zinc finger protein Np97) (RING finger protein 107) (RING-type E3 ubiquitin transferase UHRF2) (Ubiquitin-like PHD and RING finger domain-containing protein 2) (Ubiquitin-like-containing PHD and RING finger domains protein 2)	E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:23404503, PubMed:27743347, PubMed:29506131). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:24813944, PubMed:27129234). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Also ubiquitinates PCNP leading to its degradation by the proteasome (PubMed:12176013, PubMed:14741369). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation (PubMed:29923055). Also promotes DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395). {ECO:0000250\|UniProtKB:Q7TMI3, ECO:0000269\|PubMed:12176013, ECO:0000269\|PubMed:14741369, ECO:0000269\|PubMed:15178429, ECO:0000269\|PubMed:15361834, ECO:0000269\|PubMed:21952639, ECO:0000269\|PubMed:23404503, ECO:0000269\|PubMed:24813944, ECO:0000269\|PubMed:27129234, ECO:0000269\|PubMed:27743347, ECO:0000269\|PubMed:29506131, ECO:0000269\|PubMed:29923055, ECO:0000269\|PubMed:30335751, ECO:0000269\|PubMed:33848395}.
Q96Q15	SMG1	S3576	ochoa	Serine/threonine-protein kinase SMG1 (SMG-1) (hSMG-1) (EC 2.7.11.1) (Lambda/iota protein kinase C-interacting protein) (Lambda-interacting protein) (Nonsense mediated mRNA decay-associated PI3K-related kinase SMG1)	Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. {ECO:0000269\|PubMed:11331269, ECO:0000269\|PubMed:11544179, ECO:0000269\|PubMed:15175154, ECO:0000269\|PubMed:16452507}.
Q96QC0	PPP1R10	S597	ochoa	Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (PP1-binding protein of 114 kDa) (Phosphatase 1 nuclear targeting subunit) (p99)	Substrate-recognition component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation (PubMed:39603239, PubMed:39603240). Promoter-proximal pausing by RNA polymerase II is a transcription halt following transcription initiation but prior to elongation, which acts as a checkpoint to control that transcripts are favorably configured for transcriptional elongation (PubMed:39603239, PubMed:39603240). The PNUTS-PP1 complex mediates the release of RNA polymerase II from promoter-proximal region of genes by catalyzing dephosphorylation of proteins involved in transcription, such as AFF4, CDK9, MEPCE, INTS12, NCBP1, POLR2M/GDOWN1 and SUPT6H (PubMed:39603239, PubMed:39603240). The PNUTS-PP1 complex also regulates RNA polymerase II transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription (PubMed:31677974). PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD, promoting RNA polymerase II degradation (PubMed:33264625). The PNUTS-PP1 complex also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity). PNUTS-PP1 complex mediates dephosphorylation of MYC, promoting MYC stability by preventing MYC ubiquitination by the SCF(FBXW7) complex (PubMed:30158517). In addition to acts as a substrate-recognition component, PPP1R10/PNUTS also acts as a nuclear targeting subunit for the PNUTS-PP1 complex (PubMed:9450550). In some context, PPP1R10/PNUTS also acts as an inhibitor of protein phosphatase 1 (PP1) activity by preventing access to substrates, such as RB (PubMed:18360108). {ECO:0000250\|UniProtKB:Q80W00, ECO:0000269\|PubMed:18360108, ECO:0000269\|PubMed:30158517, ECO:0000269\|PubMed:31677974, ECO:0000269\|PubMed:33264625, ECO:0000269\|PubMed:39603239, ECO:0000269\|PubMed:39603240, ECO:0000269\|PubMed:9450550}.
Q96QD8	SLC38A2	S18	ochoa	Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Protein 40-9-1) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)	Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10930503, PubMed:15774260, PubMed:15922329, PubMed:16621798). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (PubMed:10930503, PubMed:15774260). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250\|UniProtKB:Q8CFE6, ECO:0000250\|UniProtKB:Q9JHE5, ECO:0000269\|PubMed:10930503, ECO:0000269\|PubMed:15774260, ECO:0000269\|PubMed:15922329, ECO:0000269\|PubMed:16621798}.
Q96QD8	SLC38A2	S24	ochoa	Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Protein 40-9-1) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)	Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10930503, PubMed:15774260, PubMed:15922329, PubMed:16621798). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (PubMed:10930503, PubMed:15774260). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250\|UniProtKB:Q8CFE6, ECO:0000250\|UniProtKB:Q9JHE5, ECO:0000269\|PubMed:10930503, ECO:0000269\|PubMed:15774260, ECO:0000269\|PubMed:15922329, ECO:0000269\|PubMed:16621798}.
Q96QF0	RAB3IP	S294	ochoa	Rab-3A-interacting protein (Rab3A-interacting protein) (Rabin-3) (Rabin8) (SSX2-interacting protein)	Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B (PubMed:12221131, PubMed:26824392). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:12221131, PubMed:26824392). Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5 (PubMed:20937701, PubMed:26824392). Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface (PubMed:12221131). Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Part of the ciliary targeting complex containing Rab11, ASAP1, RAB3IP and RAB11FIP3 and ARF4 that promotes RAB3IP preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879, PubMed:31204173). {ECO:0000269\|PubMed:12221131, ECO:0000269\|PubMed:20890297, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:25673879, ECO:0000269\|PubMed:26824392, ECO:0000269\|PubMed:31204173}.
Q96QF0	RAB3IP	S296	ochoa	Rab-3A-interacting protein (Rab3A-interacting protein) (Rabin-3) (Rabin8) (SSX2-interacting protein)	Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B (PubMed:12221131, PubMed:26824392). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:12221131, PubMed:26824392). Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5 (PubMed:20937701, PubMed:26824392). Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface (PubMed:12221131). Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Part of the ciliary targeting complex containing Rab11, ASAP1, RAB3IP and RAB11FIP3 and ARF4 that promotes RAB3IP preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879, PubMed:31204173). {ECO:0000269\|PubMed:12221131, ECO:0000269\|PubMed:20890297, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:25673879, ECO:0000269\|PubMed:26824392, ECO:0000269\|PubMed:31204173}.
Q96QT4	TRPM7	S1358	psp	Transient receptor potential cation channel subfamily M member 7 (EC 2.7.11.1) (Channel-kinase 1) (Long transient receptor potential channel 7) (LTrpC-7) (LTrpC7) [Cleaved into: TRPM7 kinase, cleaved form (M7CK); TRPM7 channel, cleaved form]	Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx (PubMed:11385574, PubMed:12887921, PubMed:15485879, PubMed:24316671, PubMed:35561741, PubMed:36027648). Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed:18365021). In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (PubMed:15485879, PubMed:18394644). {ECO:0000250\|UniProtKB:Q923J1, ECO:0000269\|PubMed:11385574, ECO:0000269\|PubMed:12887921, ECO:0000269\|PubMed:15485879, ECO:0000269\|PubMed:18365021, ECO:0000269\|PubMed:18394644, ECO:0000269\|PubMed:24316671, ECO:0000269\|PubMed:35561741, ECO:0000269\|PubMed:36027648}.; FUNCTION: [TRPM7 channel, cleaved form]: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. {ECO:0000250\|UniProtKB:Q923J1}.; FUNCTION: [TRPM7 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development. {ECO:0000250\|UniProtKB:Q923J1}.
Q96QT4	TRPM7	S1396	ochoa	Transient receptor potential cation channel subfamily M member 7 (EC 2.7.11.1) (Channel-kinase 1) (Long transient receptor potential channel 7) (LTrpC-7) (LTrpC7) [Cleaved into: TRPM7 kinase, cleaved form (M7CK); TRPM7 channel, cleaved form]	Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx (PubMed:11385574, PubMed:12887921, PubMed:15485879, PubMed:24316671, PubMed:35561741, PubMed:36027648). Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed:18365021). In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (PubMed:15485879, PubMed:18394644). {ECO:0000250\|UniProtKB:Q923J1, ECO:0000269\|PubMed:11385574, ECO:0000269\|PubMed:12887921, ECO:0000269\|PubMed:15485879, ECO:0000269\|PubMed:18365021, ECO:0000269\|PubMed:18394644, ECO:0000269\|PubMed:24316671, ECO:0000269\|PubMed:35561741, ECO:0000269\|PubMed:36027648}.; FUNCTION: [TRPM7 channel, cleaved form]: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. {ECO:0000250\|UniProtKB:Q923J1}.; FUNCTION: [TRPM7 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development. {ECO:0000250\|UniProtKB:Q923J1}.
Q96QU8	XPO6	S214	ochoa	Exportin-6 (Exp6) (Ran-binding protein 20)	Mediates the nuclear export of actin and profilin-actin complexes in somatic cells. {ECO:0000269\|PubMed:14592989}.
Q96QZ7	MAGI1	S618	ochoa	Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (Atrophin-1-interacting protein 3) (AIP-3) (BAI1-associated protein 1) (BAP-1) (Membrane-associated guanylate kinase inverted 1) (MAGI-1) (Trinucleotide repeat-containing gene 19 protein) (WW domain-containing protein 3) (WWP3)	Plays a role in coupling actin fibers to cell junctions in endothelial cells, via its interaction with AMOTL2 and CDH5 (By similarity). May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:Q6RHR9}.
Q96RE7	NACC1	S130	ochoa	Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B)	Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. {ECO:0000269\|PubMed:17130457, ECO:0000269\|PubMed:17804717}.
Q96RE7	NACC1	S151	ochoa	Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B)	Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. {ECO:0000269\|PubMed:17130457, ECO:0000269\|PubMed:17804717}.
Q96RF0	SNX18	S202	ochoa	Sorting nexin-18 (SH3 and PX domain-containing protein 3B)	Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis (PubMed:18411244, PubMed:20427313, PubMed:21048941, PubMed:22718350). Required for efficient progress through mitosis and cytokinesis (PubMed:22718350). Required for normal formation of the cleavage furrow at the end of mitosis (PubMed:22718350). Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis (PubMed:20427313). Plays a role in macropinocytosis (PubMed:21048941). Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation (PubMed:18411244). Stimulates the GTPase activity of DNM2 (PubMed:20427313). Promotes DNM2 location at the plasma membrane (PubMed:20427313). Together with DNM2, involved in autophagosome assembly by regulating trafficking from recycling endosomes of phospholipid scramblase ATG9A (PubMed:29437695). {ECO:0000269\|PubMed:18411244, ECO:0000269\|PubMed:20427313, ECO:0000269\|PubMed:21048941, ECO:0000269\|PubMed:22718350, ECO:0000269\|PubMed:29437695}.
Q96RG2	PASK	S849	ochoa	PAS domain-containing serine/threonine-protein kinase (PAS-kinase) (PASKIN) (hPASK) (EC 2.7.11.1)	Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. {ECO:0000269\|PubMed:16275910, ECO:0000269\|PubMed:17052199, ECO:0000269\|PubMed:17595531, ECO:0000269\|PubMed:20943661, ECO:0000269\|PubMed:21181396, ECO:0000269\|PubMed:21418524}.
Q96RL1	UIMC1	S204	ochoa	BRCA1-A complex subunit RAP80 (Receptor-associated protein 80) (Retinoid X receptor-interacting protein 110) (Ubiquitin interaction motif-containing protein 1)	Ubiquitin-binding protein (PubMed:24627472). Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070, Ref.38). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1. {ECO:0000269\|PubMed:12080054, ECO:0000269\|PubMed:17525340, ECO:0000269\|PubMed:17525341, ECO:0000269\|PubMed:17525342, ECO:0000269\|PubMed:17621610, ECO:0000269\|PubMed:17643121, ECO:0000269\|PubMed:19015238, ECO:0000269\|PubMed:19202061, ECO:0000269\|PubMed:19261748, ECO:0000269\|PubMed:19328070, ECO:0000269\|PubMed:24627472, ECO:0000269\|Ref.38}.
Q96RT1	ERBIN	S665	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96RT1	ERBIN	S850	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96RT1	ERBIN	S1085	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96RT1	ERBIN	S1112	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96RU2	USP28	S720	psp	Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)	Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells (PubMed:24623306). {ECO:0000269\|PubMed:16901786, ECO:0000269\|PubMed:17558397, ECO:0000269\|PubMed:17873522, ECO:0000269\|PubMed:18662541, ECO:0000269\|PubMed:24623306}.
Q96RY5	CRAMP1	S1201	ochoa	Protein cramped-like (Cramped chromatin regulator homolog 1) (Hematological and neurological expressed 1-like protein)	None
Q96S38	RPS6KC1	S454	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S38	RPS6KC1	S455	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S38	RPS6KC1	S589	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S38	RPS6KC1	S648	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S38	RPS6KC1	S650	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S38	RPS6KC1	S667	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96S59	RANBP9	S176	ochoa	Ran-binding protein 9 (RanBP9) (BPM-L) (BPM90) (Ran-binding protein M) (RanBPM) (RanBP7)	May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Acts as a mediator of cell spreading and actin cytoskeleton rearrangement (PubMed:18710924). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). May be involved in signaling of ITGB2/LFA-1 and other integrins (PubMed:14722085). Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway (PubMed:12147692). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation (PubMed:12361945, PubMed:18222118). Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity (PubMed:15558019). Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA. {ECO:0000269\|PubMed:12147692, ECO:0000269\|PubMed:12361945, ECO:0000269\|PubMed:14500717, ECO:0000269\|PubMed:14722085, ECO:0000269\|PubMed:15381419, ECO:0000269\|PubMed:15558019, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:18710924, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q96S97	MYADM	S22	ochoa	Myeloid-associated differentiation marker (Protein SB135)	None
Q96SD1	DCLRE1C	S655	psp	Protein artemis (EC 3.1.-.-) (DNA cross-link repair 1C protein) (Protein A-SCID) (SNM1 homolog C) (hSNM1C) (SNM1-like protein)	Nuclease involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments (PubMed:11336668, PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs) (PubMed:11336668, PubMed:11955432, PubMed:14744996). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends (PubMed:11336668, PubMed:11955432, PubMed:14744996). These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively (PubMed:11336668, PubMed:11955432, PubMed:14744996). This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC (PubMed:11955432, PubMed:15071507, PubMed:15574326, PubMed:15936993). The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint (PubMed:11955432). Also required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ (PubMed:15456891, PubMed:15468306, PubMed:15574327, PubMed:15811628). {ECO:0000269\|PubMed:11336668, ECO:0000269\|PubMed:11955432, ECO:0000269\|PubMed:12055248, ECO:0000269\|PubMed:14744996, ECO:0000269\|PubMed:15071507, ECO:0000269\|PubMed:15456891, ECO:0000269\|PubMed:15468306, ECO:0000269\|PubMed:15574326, ECO:0000269\|PubMed:15574327, ECO:0000269\|PubMed:15811628, ECO:0000269\|PubMed:15936993}.
Q96SI9	STRBP	S480	ochoa	Spermatid perinuclear RNA-binding protein	Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity). {ECO:0000250}.
Q96SK2	TMEM209	S228	ochoa	Transmembrane protein 209	Nuclear envelope protein which in association with NUP205, may be involved in nuclear transport of various nuclear proteins in addition to MYC. {ECO:0000269\|PubMed:22719065}.
Q96SN8	CDK5RAP2	S1672	ochoa	CDK5 regulatory subunit-associated protein 2 (CDK5 activator-binding protein C48) (Centrosome-associated protein 215)	Potential regulator of CDK5 activity via its interaction with CDK5R1 (PubMed:15164053). Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation (By similarity). Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter (PubMed:19282672). Together with EB1/MAPRE1, may promote microtubule polymerization, bundle formation, growth and dynamics at the plus ends (PubMed:18042621, PubMed:17959831, PubMed:19553473). Regulates centrosomal maturation by recruitment of the gamma-tubulin ring complex (gTuRC) onto centrosomes (PubMed:18042621, PubMed:17959831, PubMed:26485573, PubMed:39321809). In complex with PDE4DIP isoform 13/MMG8/SMYLE, MAPRE1 and AKAP9, contributes to microtubules nucleation and extension from the centrosome to the cell periphery (PubMed:29162697). Required for the recruitment of AKAP9 to centrosomes (PubMed:29162697). Plays a role in neurogenesis (By similarity). {ECO:0000250\|UniProtKB:Q8K389, ECO:0000269\|PubMed:15164053, ECO:0000269\|PubMed:17959831, ECO:0000269\|PubMed:18042621, ECO:0000269\|PubMed:19282672, ECO:0000269\|PubMed:19553473, ECO:0000269\|PubMed:26485573, ECO:0000269\|PubMed:29162697, ECO:0000269\|PubMed:39321809}.
Q96ST2	IWS1	S426	ochoa	Protein IWS1 homolog (IWS1-like protein)	Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. {ECO:0000269\|PubMed:17184735, ECO:0000269\|PubMed:17234882, ECO:0000269\|PubMed:19141475}.
Q96SU4	OSBPL9	S325	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S344	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S348	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96T23	RSF1	S1252	ochoa	Remodeling and spacing factor 1 (Rsf-1) (HBV pX-associated protein 8) (Hepatitis B virus X-associated protein) (p325 subunit of RSF chromatin-remodeling complex)	Regulatory subunit of the ATP-dependent RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:12972596, PubMed:28801535). Binds to core histones together with SMARCA5, and is required for the assembly of regular nucleosome arrays by the RSF-5 ISWI chromatin-remodeling complex (PubMed:12972596). Directly stimulates the ATPase activity of SMARCA1 and SMARCA5 in the RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, respectively (PubMed:28801535). The RSF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the RSF-5 ISWI chromatin-remodeling complex (PubMed:28801535). The complexes do not have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain (PubMed:11788598, PubMed:11944984). {ECO:0000269\|PubMed:11788598, ECO:0000269\|PubMed:11944984, ECO:0000269\|PubMed:12972596, ECO:0000269\|PubMed:28801535}.
Q96T37	RBM15	S109	ochoa	RNA-binding protein 15 (One-twenty two protein 1) (RNA-binding motif protein 15)	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311). {ECO:0000250\|UniProtKB:Q0VBL3, ECO:0000269\|PubMed:17001072, ECO:0000269\|PubMed:19786495, ECO:0000269\|PubMed:26575292, ECO:0000269\|PubMed:27602518, ECO:0000305\|PubMed:11344311}.
Q96T37	RBM15	S680	ochoa	RNA-binding protein 15 (One-twenty two protein 1) (RNA-binding motif protein 15)	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311). {ECO:0000250\|UniProtKB:Q0VBL3, ECO:0000269\|PubMed:17001072, ECO:0000269\|PubMed:19786495, ECO:0000269\|PubMed:26575292, ECO:0000269\|PubMed:27602518, ECO:0000305\|PubMed:11344311}.
Q96T37	RBM15	S878	ochoa	RNA-binding protein 15 (One-twenty two protein 1) (RNA-binding motif protein 15)	RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311). {ECO:0000250\|UniProtKB:Q0VBL3, ECO:0000269\|PubMed:17001072, ECO:0000269\|PubMed:19786495, ECO:0000269\|PubMed:26575292, ECO:0000269\|PubMed:27602518, ECO:0000305\|PubMed:11344311}.
Q96T58	SPEN	S1261	ochoa	Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog)	May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250\|UniProtKB:Q62504, ECO:0000269\|PubMed:11331609, ECO:0000269\|PubMed:12374742}.
Q96T58	SPEN	S2126	ochoa	Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog)	May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250\|UniProtKB:Q62504, ECO:0000269\|PubMed:11331609, ECO:0000269\|PubMed:12374742}.
Q96TC7	RMDN3	S50	ochoa	Regulator of microtubule dynamics protein 3 (RMD-3) (hRMD-3) (Cerebral protein 10) (Protein FAM82A2) (Protein FAM82C) (Protein tyrosine phosphatase-interacting protein 51) (TCPTP-interacting protein 51)	Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. {ECO:0000269\|PubMed:16820967, ECO:0000269\|PubMed:22131369}.
Q99081	TCF12	S49	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	S73	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	S311	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	S354	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	S392	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99442	SEC62	S341	ochoa	Translocation protein SEC62 (Translocation protein 1) (TP-1) (hTP-1)	Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. {ECO:0000269\|PubMed:22375059, ECO:0000269\|PubMed:29719251}.
Q99501	GAS2L1	S358	ochoa\|psp	GAS2-like protein 1 (GAS2-related protein on chromosome 22) (Growth arrest-specific protein 2-like 1)	Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). {ECO:0000269\|PubMed:12584248, ECO:0000269\|PubMed:24706950}.
Q99501	GAS2L1	S361	ochoa	GAS2-like protein 1 (GAS2-related protein on chromosome 22) (Growth arrest-specific protein 2-like 1)	Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). {ECO:0000269\|PubMed:12584248, ECO:0000269\|PubMed:24706950}.
Q99569	PKP4	S83	ochoa	Plakophilin-4 (p0071)	Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques. {ECO:0000269\|PubMed:17115030}.
Q99575	POP1	S736	ochoa	Ribonucleases P/MRP protein subunit POP1 (hPOP1)	Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:8918471). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269\|PubMed:28115465, ECO:0000269\|PubMed:30454648, ECO:0000269\|PubMed:8918471}.
Q99590	SCAF11	S341	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99590	SCAF11	S344	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99590	SCAF11	S802	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99590	SCAF11	S1110	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99640	PKMYT1	S100	ochoa	Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (EC 2.7.11.1) (Myt1 kinase)	Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase specifically when CDK1 is complexed to cyclins (PubMed:10373560, PubMed:10504341, PubMed:9001210, PubMed:9268380). Mediates phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved in Golgi fragmentation (PubMed:9001210, PubMed:9268380). May be involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree, however tyrosine kinase activity is unclear and may be indirect (PubMed:9001210, PubMed:9268380). {ECO:0000269\|PubMed:10373560, ECO:0000269\|PubMed:10504341, ECO:0000269\|PubMed:9001210, ECO:0000269\|PubMed:9268380}.
Q99661	KIF2C	S115	ochoa\|psp	Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK)	In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:21820309). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (PubMed:19060894). Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (PubMed:23891108). {ECO:0000269\|PubMed:19060894, ECO:0000269\|PubMed:21820309, ECO:0000269\|PubMed:23891108}.
Q99661	KIF2C	S187	ochoa	Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK)	In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:21820309). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis (PubMed:19060894). Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (PubMed:23891108). {ECO:0000269\|PubMed:19060894, ECO:0000269\|PubMed:21820309, ECO:0000269\|PubMed:23891108}.
Q99666	RGPD5	S1486	ochoa	RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63)	None
Q99666	RGPD5	S1585	ochoa	RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63)	None
Q99666	RGPD5	S1592	ochoa	RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63)	None
Q99683	MAP3K5	S984	ochoa	Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269\|PubMed:10411906, ECO:0000269\|PubMed:10688666, ECO:0000269\|PubMed:10849426, ECO:0000269\|PubMed:11029458, ECO:0000269\|PubMed:11154276, ECO:0000269\|PubMed:11689443, ECO:0000269\|PubMed:11920685, ECO:0000269\|PubMed:14688258, ECO:0000269\|PubMed:14749717, ECO:0000269\|PubMed:15023544, ECO:0000269\|PubMed:16129676, ECO:0000269\|PubMed:17220297, ECO:0000269\|PubMed:23102700, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:8940179, ECO:0000269\|PubMed:8974401, ECO:0000269\|PubMed:9564042, ECO:0000269\|PubMed:9774977}.
Q99683	MAP3K5	S986	ochoa	Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269\|PubMed:10411906, ECO:0000269\|PubMed:10688666, ECO:0000269\|PubMed:10849426, ECO:0000269\|PubMed:11029458, ECO:0000269\|PubMed:11154276, ECO:0000269\|PubMed:11689443, ECO:0000269\|PubMed:11920685, ECO:0000269\|PubMed:14688258, ECO:0000269\|PubMed:14749717, ECO:0000269\|PubMed:15023544, ECO:0000269\|PubMed:16129676, ECO:0000269\|PubMed:17220297, ECO:0000269\|PubMed:23102700, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:8940179, ECO:0000269\|PubMed:8974401, ECO:0000269\|PubMed:9564042, ECO:0000269\|PubMed:9774977}.
Q99683	MAP3K5	S1234	ochoa	Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269\|PubMed:10411906, ECO:0000269\|PubMed:10688666, ECO:0000269\|PubMed:10849426, ECO:0000269\|PubMed:11029458, ECO:0000269\|PubMed:11154276, ECO:0000269\|PubMed:11689443, ECO:0000269\|PubMed:11920685, ECO:0000269\|PubMed:14688258, ECO:0000269\|PubMed:14749717, ECO:0000269\|PubMed:15023544, ECO:0000269\|PubMed:16129676, ECO:0000269\|PubMed:17220297, ECO:0000269\|PubMed:23102700, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:8940179, ECO:0000269\|PubMed:8974401, ECO:0000269\|PubMed:9564042, ECO:0000269\|PubMed:9774977}.
Q99684	GFI1	S26	ochoa	Zinc finger protein Gfi-1 (Growth factor independent protein 1) (Zinc finger protein 163)	Transcription repressor essential for hematopoiesis (PubMed:11060035, PubMed:17197705, PubMed:17646546, PubMed:18805794, PubMed:19164764, PubMed:20190815, PubMed:8754800). Functions in a cell-context and development-specific manner (PubMed:11060035, PubMed:17197705, PubMed:17646546, PubMed:18805794, PubMed:19164764, PubMed:20190815, PubMed:8754800). Binds to 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of genes (PubMed:11060035, PubMed:17197705, PubMed:17646546, PubMed:18805794, PubMed:19164764, PubMed:20190815, PubMed:8754800). Component of several complexes, including the EHMT2-GFI1-HDAC1, AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (PubMed:16287849). Regulates neutrophil differentiation, promotes proliferation of lymphoid cells, and is required for granulocyte development (PubMed:12778173). Inhibits SPI1 transcriptional activity at macrophage-specific genes, repressing macrophage differentiation of myeloid progenitor cells and promoting granulocyte commitment (By similarity). Mediates, together with U2AF1L4, the alternative splicing of CD45 and controls T-cell receptor signaling (By similarity). Regulates the endotoxin-mediated Toll-like receptor (TLR) inflammatory response by antagonizing RELA (PubMed:20547752). Cooperates with CBFA2T2 to regulate ITGB1-dependent neurite growth (PubMed:19026687). Controls cell-cycle progression by repressing CDKNIA/p21 transcription in response to TGFB1 via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB promoters (PubMed:16287849). Required for the maintenance of inner ear hair cells (By similarity). In addition to its role in transcription, acts as a substrate adapter for PRMT1 in the DNA damage response: facilitates the recognition of TP53BP1 and MRE11 substrates by PRMT1, promoting their methylation and the DNA damage response (PubMed:29651020). {ECO:0000250\|UniProtKB:P70338, ECO:0000269\|PubMed:11060035, ECO:0000269\|PubMed:12778173, ECO:0000269\|PubMed:16287849, ECO:0000269\|PubMed:17197705, ECO:0000269\|PubMed:17646546, ECO:0000269\|PubMed:18805794, ECO:0000269\|PubMed:19026687, ECO:0000269\|PubMed:19164764, ECO:0000269\|PubMed:20190815, ECO:0000269\|PubMed:20547752, ECO:0000269\|PubMed:29651020, ECO:0000269\|PubMed:8754800}.
Q99698	LYST	S2245	ochoa	Lysosomal-trafficking regulator (Beige homolog)	Adapter protein that regulates and/or fission of intracellular vesicles such as lysosomes (PubMed:11984006, PubMed:25216107). Might regulate trafficking of effectors involved in exocytosis (PubMed:25425525). In cytotoxic T-cells and natural killer (NK) cells, has role in the regulation of size, number and exocytosis of lytic granules (PubMed:26478006). In macrophages and dendritic cells, regulates phagosome maturation by controlling the conversion of early phagosomal compartments into late phagosomes (By similarity). In macrophages and dendritic cells, specifically involved in TLR3- and TLR4-induced production of pro-inflammatory cytokines by regulating the endosomal TLR3- TICAM1/TRIF and TLR4- TICAM1/TRIF signaling pathways (PubMed:27881733). {ECO:0000250\|UniProtKB:P97412, ECO:0000269\|PubMed:11984006, ECO:0000269\|PubMed:25216107, ECO:0000269\|PubMed:25425525, ECO:0000269\|PubMed:26478006, ECO:0000269\|PubMed:27881733}.
Q99700	ATXN2	S213	ochoa	Ataxin-2 (Spinocerebellar ataxia type 2 protein) (Trinucleotide repeat-containing gene 13 protein)	Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269\|PubMed:18602463}.
Q99700	ATXN2	S854	ochoa	Ataxin-2 (Spinocerebellar ataxia type 2 protein) (Trinucleotide repeat-containing gene 13 protein)	Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269\|PubMed:18602463}.
Q99704	DOK1	S316	ochoa	Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok)) (pp62)	DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269\|PubMed:18156175}.
Q99959	PKP2	S294	ochoa	Plakophilin-2	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:25208567). Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (PubMed:23884246). Required to maintain gingival epithelial barrier function (PubMed:34368962). Important component of the desmosome that is also required for localization of desmosome component proteins such as DSC2, DSG2 and JUP to the desmosome cell-cell junction (PubMed:22781308, PubMed:25208567). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (By similarity). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes, via ANK3 stabilization and modulation of SCN5A/Nav1.5 localization to cell-cell junctions (By similarity). Required for mitochondrial function, nuclear envelope integrity and positive regulation of SIRT3 transcription via maintaining DES localization at its nuclear envelope and cell tip anchoring points, and thereby preserving regulation of the transcriptional program (PubMed:35959657). Maintenance of nuclear envelope integrity protects against DNA damage and transcriptional dysregulation of genes, especially those involved in the electron transport chain, thereby preserving mitochondrial function and protecting against superoxide radical anion generation (PubMed:35959657). Binds single-stranded DNA (ssDNA) (PubMed:20613778). May regulate the localization of GJA1 to gap junctions in intercalated disks of the heart (PubMed:18662195). Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297). Acts as a host restriction factor for IAV viral propagation, potentially via disrupting the interaction of IAV polymerase complex proteins (PubMed:28169297). {ECO:0000250\|UniProtKB:F1M7L9, ECO:0000250\|UniProtKB:Q9CQ73, ECO:0000269\|PubMed:18662195, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:22781308, ECO:0000269\|PubMed:23884246, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:28169297, ECO:0000269\|PubMed:34368962, ECO:0000269\|PubMed:35959657}.
Q99961	SH3GL1	S292	ochoa	Endophilin-A2 (EEN fusion partner of MLL) (Endophilin-2) (Extra eleven-nineteen leukemia fusion gene protein) (EEN) (SH3 domain protein 2B) (SH3 domain-containing GRB2-like protein 1)	Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}.
Q9BPU6	DPYSL5	S538	ochoa	Dihydropyrimidinase-related protein 5 (DRP-5) (CRMP3-associated molecule) (CRAM) (Collapsin response mediator protein 5) (CRMP-5) (UNC33-like phosphoprotein 6) (ULIP-6)	Involved in the negative regulation of dendrite outgrowth. {ECO:0000269\|PubMed:33894126}.
Q9BQ52	ELAC2	S205	ochoa	Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Heredity prostate cancer protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2)	Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (PubMed:21593607). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly (PubMed:24703694). {ECO:0000269\|PubMed:21593607, ECO:0000269\|PubMed:24703694}.
Q9BQ89	FAM110A	S244	ochoa	Protein FAM110A	None
Q9BQ89	FAM110A	S249	ochoa	Protein FAM110A	None
Q9BQE3	TUBA1C	S54	ochoa	Tubulin alpha-1C chain (EC 3.6.5.-) (Alpha-tubulin 6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain]	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Q9BQE4	SELENOS	S146	ochoa	Selenoprotein S (SelS) (VCP-interacting membrane protein)	Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination. {ECO:0000269\|PubMed:15215856}.
Q9BQL6	FERMT1	S176	ochoa\|psp	Fermitin family homolog 1 (Kindlerin) (Kindlin syndrome protein) (Kindlin-1) (Unc-112-related protein 1)	Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression. {ECO:0000269\|PubMed:14634021, ECO:0000269\|PubMed:17012746, ECO:0000269\|PubMed:19804783}.
Q9BR39	JPH2	S168	ochoa	Junctophilin-2 (JP-2) (Junctophilin type 2) [Cleaved into: Junctophilin-2 N-terminal fragment (JP2NT)]	[Junctophilin-2]: Membrane-binding protein that provides a structural bridge between the plasma membrane and the sarcoplasmic reticulum and is required for normal excitation-contraction coupling in cardiomyocytes (PubMed:20095964). Provides a structural foundation for functional cross-talk between the cell surface and intracellular Ca(2+) release channels by maintaining the 12-15 nm gap between the sarcolemma and the sarcoplasmic reticulum membranes in the cardiac dyads (By similarity). Necessary for proper intracellular Ca(2+) signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release (By similarity). Contributes to the construction of skeletal muscle triad junctions (By similarity). {ECO:0000250\|UniProtKB:Q9ET78, ECO:0000269\|PubMed:20095964}.; FUNCTION: [Junctophilin-2 N-terminal fragment]: Transcription repressor required to safeguard against the deleterious effects of cardiac stress. Generated following cleavage of the Junctophilin-2 chain by calpain in response to cardiac stress in cardiomyocytes. Following cleavage and release from the membrane, translocates to the nucleus, binds DNA and represses expression of genes implicated in cell growth and differentiation, hypertrophy, inflammation and fibrosis. Modifies the transcription profile and thereby attenuates pathological remodeling in response to cardiac stress. Probably acts by competing with MEF2 transcription factors and TATA-binding proteins. {ECO:0000250\|UniProtKB:Q9ET78}.
Q9BR39	JPH2	S171	ochoa	Junctophilin-2 (JP-2) (Junctophilin type 2) [Cleaved into: Junctophilin-2 N-terminal fragment (JP2NT)]	[Junctophilin-2]: Membrane-binding protein that provides a structural bridge between the plasma membrane and the sarcoplasmic reticulum and is required for normal excitation-contraction coupling in cardiomyocytes (PubMed:20095964). Provides a structural foundation for functional cross-talk between the cell surface and intracellular Ca(2+) release channels by maintaining the 12-15 nm gap between the sarcolemma and the sarcoplasmic reticulum membranes in the cardiac dyads (By similarity). Necessary for proper intracellular Ca(2+) signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release (By similarity). Contributes to the construction of skeletal muscle triad junctions (By similarity). {ECO:0000250\|UniProtKB:Q9ET78, ECO:0000269\|PubMed:20095964}.; FUNCTION: [Junctophilin-2 N-terminal fragment]: Transcription repressor required to safeguard against the deleterious effects of cardiac stress. Generated following cleavage of the Junctophilin-2 chain by calpain in response to cardiac stress in cardiomyocytes. Following cleavage and release from the membrane, translocates to the nucleus, binds DNA and represses expression of genes implicated in cell growth and differentiation, hypertrophy, inflammation and fibrosis. Modifies the transcription profile and thereby attenuates pathological remodeling in response to cardiac stress. Probably acts by competing with MEF2 transcription factors and TATA-binding proteins. {ECO:0000250\|UniProtKB:Q9ET78}.
Q9BRD0	BUD13	S364	ochoa	BUD13 homolog	Involved in pre-mRNA splicing as component of the activated spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000305\|PubMed:33509932}.
Q9BRK4	LZTS2	S105	ochoa	Leucine zipper putative tumor suppressor 2 (hLZTS2) (Protein LAPSER1)	Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. May negatively regulate axonal outgrowth by preventing the formation of microtubule bundles that are necessary for transport within the elongating axon. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin. {ECO:0000255\|HAMAP-Rule:MF_03026, ECO:0000269\|PubMed:17000760, ECO:0000269\|PubMed:17351128, ECO:0000269\|PubMed:17950943, ECO:0000269\|PubMed:18490357}.
Q9BRX2	PELO	S58	ochoa	Protein pelota homolog (hPelota) (Protein Dom34 homolog)	Component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:21448132, PubMed:23667253, PubMed:27543824, PubMed:27863242). In the Pelota-HBS1L complex, PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (PubMed:27543824, PubMed:27863242). Following mRNA extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L complex promotes recruitment of ABCE1, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132, PubMed:32006463). As part of the PINK1-regulated signaling, upon mitochondrial damage is recruited to the ribosome/mRNA-ribonucleoprotein complex associated to mitochondrial outer membrane thereby enabling the recruitment of autophagy receptors and induction of mitophagy (PubMed:29861391). {ECO:0000269\|PubMed:21448132, ECO:0000269\|PubMed:23667253, ECO:0000269\|PubMed:27543824, ECO:0000269\|PubMed:27863242, ECO:0000269\|PubMed:29861391, ECO:0000269\|PubMed:32006463}.
Q9BSJ6	PIMREG	S137	ochoa	Protein PIMREG (CALM-interactor expressed in thymus and spleen) (PICALM-interacting mitotic regulator) (Regulator of chromosome segregation protein 1)	During mitosis, may play a role in the control of metaphase-to-anaphase transition. {ECO:0000269\|PubMed:18757745}.
Q9BSJ6	PIMREG	S201	ochoa	Protein PIMREG (CALM-interactor expressed in thymus and spleen) (PICALM-interacting mitotic regulator) (Regulator of chromosome segregation protein 1)	During mitosis, may play a role in the control of metaphase-to-anaphase transition. {ECO:0000269\|PubMed:18757745}.
Q9BSQ5	CCM2	S251	ochoa	Cerebral cavernous malformations 2 protein (Malcavernin)	Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity). {ECO:0000250}.
Q9BSQ5	CCM2	S289	ochoa	Cerebral cavernous malformations 2 protein (Malcavernin)	Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity). {ECO:0000250}.
Q9BST9	RTKN	S224	ochoa	Rhotekin	Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures. {ECO:0000269\|PubMed:10940294, ECO:0000269\|PubMed:15480428, ECO:0000269\|PubMed:16007136}.
Q9BST9	RTKN	S225	ochoa	Rhotekin	Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures. {ECO:0000269\|PubMed:10940294, ECO:0000269\|PubMed:15480428, ECO:0000269\|PubMed:16007136}.
Q9BSV6	TSEN34	S141	ochoa	tRNA-splicing endonuclease subunit Sen34 (EC 4.6.1.16) (Leukocyte receptor cluster member 5) (tRNA-intron endonuclease Sen34) (HsSen34)	Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. {ECO:0000269\|PubMed:15109492}.
Q9BT25	HAUS8	S139	ochoa\|psp	HAUS augmin-like complex subunit 8 (HEC1/NDC80-interacting centrosome-associated protein 1) (Sarcoma antigen NY-SAR-48)	Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269\|PubMed:18362163, ECO:0000269\|PubMed:19369198, ECO:0000269\|PubMed:19427217}.
Q9BTA9	WAC	S538	ochoa	WW domain-containing adapter protein with coiled-coil	Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1) (PubMed:21329877). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription (PubMed:21329877). Regulates the cell-cycle checkpoint activation in response to DNA damage (PubMed:21329877). Positive regulator of amino acid starvation-induced autophagy (PubMed:22354037). Also acts as a negative regulator of basal autophagy (PubMed:26812014). Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014). May negatively regulate the ubiquitin proteasome pathway (PubMed:21329877). {ECO:0000269\|PubMed:21329877, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:26812014}.
Q9BTC0	DIDO1	S1040	ochoa	Death-inducer obliterator 1 (DIO-1) (hDido1) (Death-associated transcription factor 1) (DATF-1)	Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development. {ECO:0000250, ECO:0000269\|PubMed:16127461}.; FUNCTION: [Isoform 2]: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes. {ECO:0000269\|PubMed:16127461}.
Q9BTE3	MCMBP	S162	ochoa	Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein)	Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion. {ECO:0000269\|PubMed:20090939, ECO:0000269\|PubMed:21196493}.
Q9BTE7	DCUN1D5	S47	ochoa	DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)	Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs) (PubMed:19617556, PubMed:23201271, PubMed:26906416). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (PubMed:23098533, PubMed:24192928). {ECO:0000269\|PubMed:19617556, ECO:0000269\|PubMed:23098533, ECO:0000269\|PubMed:23201271, ECO:0000269\|PubMed:24192928, ECO:0000269\|PubMed:26906416}.
Q9BU76	MMTAG2	S161	ochoa	Multiple myeloma tumor-associated protein 2 (hMMTAG2)	None
Q9BUA3	SPINDOC	S61	ochoa	Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC)	Chromatin protein that stabilizes SPIN1 and enhances its association with histone H3 trimethylated at both 'Lys-4' and 'Lys-9' (H3K4me3K9me3) (PubMed:33574238). Positively regulates poly-ADP-ribosylation in response to DNA damage; acts by facilitating PARP1 ADP-ribosyltransferase activity (PubMed:34737271). {ECO:0000269\|PubMed:33574238, ECO:0000269\|PubMed:34737271}.
Q9BUA3	SPINDOC	S154	ochoa	Spindlin interactor and repressor of chromatin-binding protein (SPIN1-docking protein) (SPIN-DOC)	Chromatin protein that stabilizes SPIN1 and enhances its association with histone H3 trimethylated at both 'Lys-4' and 'Lys-9' (H3K4me3K9me3) (PubMed:33574238). Positively regulates poly-ADP-ribosylation in response to DNA damage; acts by facilitating PARP1 ADP-ribosyltransferase activity (PubMed:34737271). {ECO:0000269\|PubMed:33574238, ECO:0000269\|PubMed:34737271}.
Q9BUH8	BEGAIN	S200	ochoa	Brain-enriched guanylate kinase-associated protein	May sustain the structure of the postsynaptic density (PSD).
Q9BUH8	BEGAIN	S483	ochoa	Brain-enriched guanylate kinase-associated protein	May sustain the structure of the postsynaptic density (PSD).
Q9BUL5	PHF23	S70	ochoa	PHD finger protein 23 (PDH-containing protein JUNE-1)	Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000269\|PubMed:25484098}.
Q9BUL5	PHF23	S153	ochoa	PHD finger protein 23 (PDH-containing protein JUNE-1)	Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000269\|PubMed:25484098}.
Q9BVS4	RIOK2	S489	ochoa	Serine/threonine-protein kinase RIO2 (EC 2.7.11.1) (RIO kinase 2)	Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710). {ECO:0000269\|PubMed:16037817, ECO:0000269\|PubMed:19564402, ECO:0000269\|PubMed:21880710}.
Q9BW04	SARG	S316	ochoa	Specifically androgen-regulated gene protein	Putative androgen-specific receptor. {ECO:0000269\|PubMed:15525603}.
Q9BW04	SARG	S502	ochoa	Specifically androgen-regulated gene protein	Putative androgen-specific receptor. {ECO:0000269\|PubMed:15525603}.
Q9BW04	SARG	S508	ochoa	Specifically androgen-regulated gene protein	Putative androgen-specific receptor. {ECO:0000269\|PubMed:15525603}.
Q9BW71	HIRIP3	S104	ochoa	HIRA-interacting protein 3	Histone chaperone that carries a H2A-H2B histone complex and facilitates its deposition onto chromatin. {ECO:0000269\|PubMed:38334665, ECO:0000269\|PubMed:9710638}.
Q9BWE0	REPIN1	S27	ochoa	DNA-binding protein REPIN1 (60 kDa origin-specific DNA-binding protein) (60 kDa replication initiation region protein) (ATT-binding protein) (DHFR oribeta-binding protein RIP60) (Zinc finger protein 464)	Sequence-specific double-stranded DNA-binding protein (PubMed:10606657, PubMed:11328883, PubMed:2174103, PubMed:2247056, PubMed:8355269). Binds ATT-rich and T-rich DNA sequences and facilitates DNA bending (PubMed:10606657, PubMed:11328883, PubMed:2174103, PubMed:2247056, PubMed:8355269). May regulate the expression of genes involved in cellular fatty acid import, including SCARB1/CD36, and genes involved in lipid droplet formation (By similarity). May regulate the expression of LCN2, and thereby influence iron metabolism and apoptosis-related pathways (By similarity). May regulate the expression of genes involved in glucose transport (By similarity). {ECO:0000250\|UniProtKB:Q5U4E2, ECO:0000269\|PubMed:10606657, ECO:0000269\|PubMed:11328883, ECO:0000269\|PubMed:2174103, ECO:0000269\|PubMed:2247056, ECO:0000269\|PubMed:8355269}.
Q9BWF3	RBM4	S337	ochoa	RNA-binding protein 4 (Lark homolog) (hLark) (RNA-binding motif protein 4) (RNA-binding motif protein 4a)	RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. {ECO:0000269\|PubMed:12628928, ECO:0000269\|PubMed:16260624, ECO:0000269\|PubMed:16777844, ECO:0000269\|PubMed:16934801, ECO:0000269\|PubMed:17284590, ECO:0000269\|PubMed:17932509, ECO:0000269\|PubMed:19801630, ECO:0000269\|PubMed:21343338, ECO:0000269\|PubMed:21518792, ECO:0000269\|PubMed:37548402}.
Q9BX66	SORBS1	S481	ochoa	Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP)	Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity). {ECO:0000250\|UniProtKB:Q62417}.
Q9BX66	SORBS1	S953	ochoa	Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP)	Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity). {ECO:0000250\|UniProtKB:Q62417}.
Q9BXB4	OSBPL11	S48	ochoa	Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11)	Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:23028956, ECO:0000269\|PubMed:39106189}.
Q9BXB4	OSBPL11	S178	ochoa	Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11)	Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:23028956, ECO:0000269\|PubMed:39106189}.
Q9BXB4	OSBPL11	S184	ochoa	Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11)	Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:23028956, ECO:0000269\|PubMed:39106189}.
Q9BXF6	RAB11FIP5	S254	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXF6	RAB11FIP5	S286	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXF6	RAB11FIP5	S365	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXF6	RAB11FIP5	S367	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXF6	RAB11FIP5	S553	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXI6	TBC1D10A	S45	ochoa	TBC1 domain family member 10A (EBP50-PDX interactor of 64 kDa) (EPI64 protein) (Rab27A-GAP-alpha)	GTPase-activating protein (GAP) specific for RAB27A and RAB35 (PubMed:16923811, PubMed:30905672). Does not show GAP activity for RAB2A, RAB3A and RAB4A (PubMed:16923811). {ECO:0000269\|PubMed:16923811, ECO:0000269\|PubMed:30905672}.
Q9BXL7	CARD11	S448	ochoa	Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)	Adapter protein that plays a key role in adaptive immune response by transducing the activation of NF-kappa-B downstream of T-cell receptor (TCR) and B-cell receptor (BCR) engagement (PubMed:11278692, PubMed:11356195, PubMed:12356734). Transduces signals downstream TCR or BCR activation via the formation of a multiprotein complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11356195). Upon activation in response to TCR or BCR triggering, CARD11 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to I-kappa-B kinase (IKK) phosphorylation and degradation, and release of NF-kappa-B proteins for nuclear translocation (PubMed:24074955). Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Promotes linear ubiquitination of BCL10 by promoting the targeting of BCL10 to RNF31/HOIP (PubMed:27777308). Stimulates the phosphorylation of BCL10 (PubMed:11356195). Also activates the TORC1 signaling pathway (PubMed:28628108). {ECO:0000269\|PubMed:11278692, ECO:0000269\|PubMed:11356195, ECO:0000269\|PubMed:12356734, ECO:0000269\|PubMed:17287217, ECO:0000269\|PubMed:24074955, ECO:0000269\|PubMed:27777308, ECO:0000269\|PubMed:28628108}.
Q9BXL7	CARD11	S562	psp	Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)	Adapter protein that plays a key role in adaptive immune response by transducing the activation of NF-kappa-B downstream of T-cell receptor (TCR) and B-cell receptor (BCR) engagement (PubMed:11278692, PubMed:11356195, PubMed:12356734). Transduces signals downstream TCR or BCR activation via the formation of a multiprotein complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11356195). Upon activation in response to TCR or BCR triggering, CARD11 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to I-kappa-B kinase (IKK) phosphorylation and degradation, and release of NF-kappa-B proteins for nuclear translocation (PubMed:24074955). Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Promotes linear ubiquitination of BCL10 by promoting the targeting of BCL10 to RNF31/HOIP (PubMed:27777308). Stimulates the phosphorylation of BCL10 (PubMed:11356195). Also activates the TORC1 signaling pathway (PubMed:28628108). {ECO:0000269\|PubMed:11278692, ECO:0000269\|PubMed:11356195, ECO:0000269\|PubMed:12356734, ECO:0000269\|PubMed:17287217, ECO:0000269\|PubMed:24074955, ECO:0000269\|PubMed:27777308, ECO:0000269\|PubMed:28628108}.
Q9BXW9	FANCD2	S337	ochoa	Fanconi anemia group D2 protein (Protein FACD2)	Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250\|UniProtKB:Q68Y81, ECO:0000269\|PubMed:11239453, ECO:0000269\|PubMed:11239454, ECO:0000269\|PubMed:12086603, ECO:0000269\|PubMed:12239151, ECO:0000269\|PubMed:14517836, ECO:0000269\|PubMed:15115758, ECO:0000269\|PubMed:15314022, ECO:0000269\|PubMed:15377654, ECO:0000269\|PubMed:15454491, ECO:0000269\|PubMed:15650050, ECO:0000269\|PubMed:15661754, ECO:0000269\|PubMed:15671039, ECO:0000269\|PubMed:19465921, ECO:0000269\|PubMed:30335751, ECO:0000269\|PubMed:36385258}.
Q9BXW9	FANCD2	S338	ochoa	Fanconi anemia group D2 protein (Protein FACD2)	Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250\|UniProtKB:Q68Y81, ECO:0000269\|PubMed:11239453, ECO:0000269\|PubMed:11239454, ECO:0000269\|PubMed:12086603, ECO:0000269\|PubMed:12239151, ECO:0000269\|PubMed:14517836, ECO:0000269\|PubMed:15115758, ECO:0000269\|PubMed:15314022, ECO:0000269\|PubMed:15377654, ECO:0000269\|PubMed:15454491, ECO:0000269\|PubMed:15650050, ECO:0000269\|PubMed:15661754, ECO:0000269\|PubMed:15671039, ECO:0000269\|PubMed:19465921, ECO:0000269\|PubMed:30335751, ECO:0000269\|PubMed:36385258}.
Q9BY89	KIAA1671	S1069	ochoa	Uncharacterized protein KIAA1671	None
Q9BY89	KIAA1671	S1230	ochoa	Uncharacterized protein KIAA1671	None
Q9BY89	KIAA1671	S1583	ochoa	Uncharacterized protein KIAA1671	None
Q9BY89	KIAA1671	S1602	ochoa	Uncharacterized protein KIAA1671	None
Q9BY89	KIAA1671	S1608	ochoa	Uncharacterized protein KIAA1671	None
Q9BY89	KIAA1671	S1675	ochoa	Uncharacterized protein KIAA1671	None
Q9BYB0	SHANK3	S1133	ochoa	SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2)	Major scaffold postsynaptic density protein which interacts with multiple proteins and complexes to orchestrate the dendritic spine and synapse formation, maturation and maintenance. Interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and HOMER, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction through the interaction with Arp2/3 and WAVE1 complex as well as the promotion of the F-actin clusters. By way of this control of actin dynamics, participates in the regulation of developing neurons growth cone motility and the NMDA receptor-signaling. Also modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to control the AMPA and metabotropic glutamate receptor-mediated synaptic transmission and plasticity. May be required at an early stage of synapse formation and be inhibited by IGF1 to promote synapse maturation. {ECO:0000269\|PubMed:24132240}.
Q9BZ23	PANK2	S146	ochoa	Pantothenate kinase 2, mitochondrial (hPanK2) (EC 2.7.1.33) (Pantothenic acid kinase 2) [Cleaved into: Pantothenate kinase 2, mitochondrial intermediate form (iPanK2); Pantothenate kinase 2, mitochondrial mature form (mPanK2)]	[Isoform 1]: Mitochondrial isoform that catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis (PubMed:15659606, PubMed:16272150, PubMed:17242360, PubMed:17825826). Required for angiogenic activity of umbilical vein of endothelial cells (HUVEC) (PubMed:30221726). {ECO:0000269\|PubMed:15659606, ECO:0000269\|PubMed:16272150, ECO:0000269\|PubMed:17242360, ECO:0000269\|PubMed:17825826, ECO:0000269\|PubMed:30221726}.; FUNCTION: [Isoform 4]: Cytoplasmic isoform that catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis. {ECO:0000269\|PubMed:16272150}.
Q9BZ29	DOCK9	S1258	ochoa	Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269\|PubMed:12172552, ECO:0000269\|PubMed:19745154}.
Q9BZ29	DOCK9	S1261	ochoa	Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269\|PubMed:12172552, ECO:0000269\|PubMed:19745154}.
Q9BZ29	DOCK9	S1264	ochoa	Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269\|PubMed:12172552, ECO:0000269\|PubMed:19745154}.
Q9BZ29	DOCK9	S1288	ochoa	Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269\|PubMed:12172552, ECO:0000269\|PubMed:19745154}.
Q9BZF1	OSBPL8	S71	ochoa	Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)	Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:17991739, ECO:0000269\|PubMed:21698267, ECO:0000269\|PubMed:26206935}.
Q9BZF1	OSBPL8	S814	ochoa	Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)	Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:17991739, ECO:0000269\|PubMed:21698267, ECO:0000269\|PubMed:26206935}.
Q9BZF3	OSBPL6	S343	ochoa	Oxysterol-binding protein-related protein 6 (ORP-6) (OSBP-related protein 6)	Regulates cellular transport and efflux of cholesterol (PubMed:26941018). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (By similarity). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (By similarity). Weakly binds 25-hydroxycholesterol (PubMed:17428193). {ECO:0000250\|UniProtKB:Q8BXR9, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:26941018}.
Q9BZL6	PRKD2	S203	ochoa	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9BZL6	PRKD2	S206	ochoa	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9BZL6	PRKD2	S242	ochoa	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9BZL6	PRKD2	S244	ochoa\|psp	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9BZL6	PRKD2	S245	ochoa	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9BZQ8	NIBAN1	S602	ochoa\|psp	Protein Niban 1 (Cell growth-inhibiting gene 39 protein) (Protein FAM129A)	Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response (By similarity). {ECO:0000250}.
Q9C040	TRIM2	S102	ochoa	Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING finger protein 86) (RING-type E3 ubiquitin transferase TRIM2)	UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. Plays a role in antiviral immunity and limits New World arenavirus infection independently of its ubiquitin ligase activity (PubMed:24068738). {ECO:0000250\|UniProtKB:Q9ESN6, ECO:0000269\|PubMed:24068738}.
Q9C073	FAM117A	S199	ochoa	Protein FAM117A (C/EBP-induced protein)	None
Q9C0A6	SETD5	S1131	ochoa	Histone-lysine N-methyltransferase SETD5 (EC 2.1.1.359) (EC 2.1.1.367) (SET domain-containing protein 5)	Chromatin regulator required for brain development: acts as a regulator of RNA elongation rate, thereby regulating neural stem cell (NSC) proliferation and synaptic transmission. May act by mediating trimethylation of 'Lys-36' of histone H3 (H3K36me3), which is essential to allow on-time RNA elongation dynamics. Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. The relevance of histone methyltransferase activity is however subject to discussion. {ECO:0000250\|UniProtKB:Q5XJV7}.
Q9C0A6	SETD5	S1144	ochoa	Histone-lysine N-methyltransferase SETD5 (EC 2.1.1.359) (EC 2.1.1.367) (SET domain-containing protein 5)	Chromatin regulator required for brain development: acts as a regulator of RNA elongation rate, thereby regulating neural stem cell (NSC) proliferation and synaptic transmission. May act by mediating trimethylation of 'Lys-36' of histone H3 (H3K36me3), which is essential to allow on-time RNA elongation dynamics. Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. The relevance of histone methyltransferase activity is however subject to discussion. {ECO:0000250\|UniProtKB:Q5XJV7}.
Q9C0B5	ZDHHC5	S345	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S370	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S415	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S428	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S429	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0C2	TNKS1BP1	S435	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S504	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S747	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S857	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S878	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S899	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S1187	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C2	TNKS1BP1	S1558	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0C7	AMBRA1	S1211	ochoa	Activating molecule in BECN1-regulated autophagy protein 1 (DDB1- and CUL4-associated factor 3)	Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy (PubMed:20921139, PubMed:23524951, PubMed:24587252, PubMed:32333458, PubMed:33854232, PubMed:33854235, PubMed:33854239). The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins such as BECN1, CCND1, CCND2, CCND3, ELOC and ULK1 (PubMed:23524951, PubMed:33854232, PubMed:33854235, PubMed:33854239). Acts as an upstream master regulator of the transition from G1 to S cell phase: AMBRA1 specifically recognizes and binds phosphorylated cyclin-D (CCND1, CCND2 and CCND3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation (PubMed:33854232, PubMed:33854235, PubMed:33854239). By controlling the transition from G1 to S phase and cyclin-D degradation, AMBRA1 acts as a tumor suppressor that promotes genomic integrity during DNA replication and counteracts developmental abnormalities and tumor growth (PubMed:33854232, PubMed:33854235, PubMed:33854239). AMBRA1 also regulates the cell cycle by promoting MYC dephosphorylation and degradation independently of the DCX(AMBRA1) complex: acts via interaction with the catalytic subunit of protein phosphatase 2A (PPP2CA), which enhances interaction between PPP2CA and MYC, leading to MYC dephosphorylation and degradation (PubMed:25438055, PubMed:25803737). Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:25499913, PubMed:30166453). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation (PubMed:21358617). In normal conditions, AMBRA1 is tethered to the cytoskeleton via interaction with dyneins DYNLL1 and DYNLL2 (PubMed:20921139). Upon autophagy induction, AMBRA1 is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (PubMed:20921139). The DCX(AMBRA1) complex mediates 'Lys-63'-linked ubiquitination of BECN1, increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity). In collaboration with TRAF6, AMBRA1 mediates 'Lys-63'-linked ubiquitination of ULK1 following autophagy induction, promoting ULK1 stability and kinase activity (PubMed:23524951). Also activates ULK1 via interaction with TRIM32: TRIM32 stimulates ULK1 through unanchored 'Lys-63'-linked polyubiquitin chains (PubMed:31123703). Also acts as an activator of mitophagy via interaction with PRKN and LC3 proteins (MAP1LC3A, MAP1LC3B or MAP1LC3C); possibly by bringing damaged mitochondria onto autophagosomes (PubMed:21753002, PubMed:25215947). Also activates mitophagy by acting as a cofactor for HUWE1; acts by promoting HUWE1-mediated ubiquitination of MFN2 (PubMed:30217973). AMBRA1 is also involved in regulatory T-cells (Treg) differentiation by promoting FOXO3 dephosphorylation independently of the DCX(AMBRA1) complex: acts via interaction with PPP2CA, which enhances interaction between PPP2CA and FOXO3, leading to FOXO3 dephosphorylation and stabilization (PubMed:30513302). May act as a regulator of intracellular trafficking, regulating the localization of active PTK2/FAK and SRC (By similarity). Also involved in transcription regulation by acting as a scaffold for protein complexes at chromatin (By similarity). {ECO:0000250\|UniProtKB:A2AH22, ECO:0000269\|PubMed:20921139, ECO:0000269\|PubMed:21358617, ECO:0000269\|PubMed:21753002, ECO:0000269\|PubMed:23524951, ECO:0000269\|PubMed:24587252, ECO:0000269\|PubMed:25215947, ECO:0000269\|PubMed:25438055, ECO:0000269\|PubMed:25499913, ECO:0000269\|PubMed:25803737, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:30513302, ECO:0000269\|PubMed:31123703, ECO:0000269\|PubMed:32333458, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854235, ECO:0000269\|PubMed:33854239}.
Q9C0C9	UBE2O	S407	ochoa	(E3-independent) E2 ubiquitin-conjugating enzyme (EC 2.3.2.24) (E2/E3 hybrid ubiquitin-protein ligase UBE2O) (Ubiquitin carrier protein O) (Ubiquitin-conjugating enzyme E2 O) (Ubiquitin-conjugating enzyme E2 of 230 kDa) (Ubiquitin-conjugating enzyme E2-230K) (Ubiquitin-protein ligase O)	E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853). {ECO:0000269\|PubMed:23381138, ECO:0000269\|PubMed:23452853, ECO:0000269\|PubMed:23455153, ECO:0000269\|PubMed:24703950}.
Q9C0D5	TANC1	S319	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1665	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1668	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1671	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1684	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1686	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1687	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9GZU3	TMEM39B	S53	ochoa	Transmembrane protein 39B	May protect the cells against DNA damage caused by exposure to the cold-warming stress and facilitates tissue damage repair during the recovery phase. {ECO:0000250\|UniProtKB:Q7ZW11}.
Q9GZV5	WWTR1	S66	ochoa\|psp	WW domain-containing transcription regulator protein 1 (Transcriptional coactivator with PDZ-binding motif)	Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:11118213, PubMed:18227151, PubMed:23911299). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18227151). WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation (PubMed:19010321). In conjunction with YAP1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:18568018). Plays a key role in coupling SMADs to the transcriptional machinery such as the mediator complex (PubMed:18568018). Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition (PubMed:18227151, PubMed:18568018). {ECO:0000269\|PubMed:11118213, ECO:0000269\|PubMed:18227151, ECO:0000269\|PubMed:18568018, ECO:0000269\|PubMed:19010321, ECO:0000269\|PubMed:23911299}.
Q9GZV5	WWTR1	S93	ochoa\|psp	WW domain-containing transcription regulator protein 1 (Transcriptional coactivator with PDZ-binding motif)	Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:11118213, PubMed:18227151, PubMed:23911299). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18227151). WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation (PubMed:19010321). In conjunction with YAP1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:18568018). Plays a key role in coupling SMADs to the transcriptional machinery such as the mediator complex (PubMed:18568018). Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition (PubMed:18227151, PubMed:18568018). {ECO:0000269\|PubMed:11118213, ECO:0000269\|PubMed:18227151, ECO:0000269\|PubMed:18568018, ECO:0000269\|PubMed:19010321, ECO:0000269\|PubMed:23911299}.
Q9GZY8	MFF	S229	ochoa	Mitochondrial fission factor	Plays a role in mitochondrial and peroxisomal fission (PubMed:18353969, PubMed:23530241, PubMed:24196833). Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (PubMed:23530241). May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity). {ECO:0000250\|UniProtKB:Q4KM98, ECO:0000269\|PubMed:18353969, ECO:0000269\|PubMed:23530241, ECO:0000269\|PubMed:24196833}.
Q9H0A0	NAT10	S990	ochoa	RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (N-acetyltransferase 10) (N-acetyltransferase-like protein) (hALP)	RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621, PubMed:35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250\|UniProtKB:P53914, ECO:0000269\|PubMed:14592445, ECO:0000269\|PubMed:17631499, ECO:0000269\|PubMed:18082603, ECO:0000269\|PubMed:19303003, ECO:0000269\|PubMed:25411247, ECO:0000269\|PubMed:25653167, ECO:0000269\|PubMed:26882543, ECO:0000269\|PubMed:27993683, ECO:0000269\|PubMed:30165671, ECO:0000269\|PubMed:30449621, ECO:0000269\|PubMed:31722219, ECO:0000269\|PubMed:34516797, ECO:0000269\|PubMed:35679869}.
Q9H0D6	XRN2	S451	ochoa	5'-3' exoribonuclease 2 (EC 3.1.13.-) (DHM1-like protein) (DHP protein)	Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (PubMed:21700224). {ECO:0000250, ECO:0000269\|PubMed:15565158, ECO:0000269\|PubMed:16648491, ECO:0000269\|PubMed:21700224}.
Q9H0E9	BRD8	S585	ochoa	Bromodomain-containing protein 8 (Skeletal muscle abundant protein) (Skeletal muscle abundant protein 2) (Thyroid hormone receptor coactivating protein of 120 kDa) (TrCP120) (p120)	May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. {ECO:0000269\|PubMed:10517671, ECO:0000269\|PubMed:14966270, ECO:0000269\|PubMed:24463511}.
Q9H0G5	NSRP1	S33	ochoa	Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70)	RNA-binding protein that mediates pre-mRNA alternative splicing regulation. {ECO:0000269\|PubMed:21296756}.
Q9H0G5	NSRP1	S291	ochoa	Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70)	RNA-binding protein that mediates pre-mRNA alternative splicing regulation. {ECO:0000269\|PubMed:21296756}.
Q9H0H5	RACGAP1	S157	ochoa\|psp	Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269\|PubMed:10979956, ECO:0000269\|PubMed:11085985, ECO:0000269\|PubMed:11278976, ECO:0000269\|PubMed:11782313, ECO:0000269\|PubMed:14729465, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16129829, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:18511905, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19468302, ECO:0000269\|PubMed:23235882, ECO:0000269\|PubMed:9497316}.
Q9H0H5	RACGAP1	S170	ochoa\|psp	Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269\|PubMed:10979956, ECO:0000269\|PubMed:11085985, ECO:0000269\|PubMed:11278976, ECO:0000269\|PubMed:11782313, ECO:0000269\|PubMed:14729465, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16129829, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:18511905, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19468302, ECO:0000269\|PubMed:23235882, ECO:0000269\|PubMed:9497316}.
Q9H0H5	RACGAP1	S280	ochoa	Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269\|PubMed:10979956, ECO:0000269\|PubMed:11085985, ECO:0000269\|PubMed:11278976, ECO:0000269\|PubMed:11782313, ECO:0000269\|PubMed:14729465, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16129829, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:18511905, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19468302, ECO:0000269\|PubMed:23235882, ECO:0000269\|PubMed:9497316}.
Q9H0L4	CSTF2T	S563	ochoa	Cleavage stimulation factor subunit 2 tau variant (CF-1 64 kDa subunit tau variant) (Cleavage stimulation factor 64 kDa subunit tau variant) (CSTF 64 kDa subunit tau variant) (TauCstF-64)	May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}.
Q9H165	BCL11A	S453	ochoa	BCL11 transcription factor A (B-cell CLL/lymphoma 11A) (B-cell lymphoma/leukemia 11A) (BCL-11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein homolog) (EVI-9) (Zinc finger protein 856)	Transcription factor (PubMed:16704730, PubMed:29606353). Associated with the BAF SWI/SNF chromatin remodeling complex (PubMed:23644491, PubMed:39607926). Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene (PubMed:29606353, PubMed:39423807). Involved in regulation of the developmental switch from gamma- to beta-globin, probably via direct repression of HBG1; hence indirectly repressing fetal hemoglobin (HbF) level (PubMed:26375765, PubMed:29606353, PubMed:39423807, PubMed:39607926). Involved in brain development (PubMed:27453576). May play a role in hematopoiesis (By similarity). Essential factor in lymphopoiesis required for B-cell formation in fetal liver (By similarity). May function as a modulator of the transcriptional repression activity of NR2F2 (By similarity). {ECO:0000250\|UniProtKB:Q9QYE3, ECO:0000269\|PubMed:16704730, ECO:0000269\|PubMed:23644491, ECO:0000269\|PubMed:29606353, ECO:0000269\|PubMed:39423807, ECO:0000269\|PubMed:39607926, ECO:0000303\|PubMed:26375765, ECO:0000303\|PubMed:27453576}.
Q9H165	BCL11A	S633	ochoa	BCL11 transcription factor A (B-cell CLL/lymphoma 11A) (B-cell lymphoma/leukemia 11A) (BCL-11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein homolog) (EVI-9) (Zinc finger protein 856)	Transcription factor (PubMed:16704730, PubMed:29606353). Associated with the BAF SWI/SNF chromatin remodeling complex (PubMed:23644491, PubMed:39607926). Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene (PubMed:29606353, PubMed:39423807). Involved in regulation of the developmental switch from gamma- to beta-globin, probably via direct repression of HBG1; hence indirectly repressing fetal hemoglobin (HbF) level (PubMed:26375765, PubMed:29606353, PubMed:39423807, PubMed:39607926). Involved in brain development (PubMed:27453576). May play a role in hematopoiesis (By similarity). Essential factor in lymphopoiesis required for B-cell formation in fetal liver (By similarity). May function as a modulator of the transcriptional repression activity of NR2F2 (By similarity). {ECO:0000250\|UniProtKB:Q9QYE3, ECO:0000269\|PubMed:16704730, ECO:0000269\|PubMed:23644491, ECO:0000269\|PubMed:29606353, ECO:0000269\|PubMed:39423807, ECO:0000269\|PubMed:39607926, ECO:0000303\|PubMed:26375765, ECO:0000303\|PubMed:27453576}.
Q9H1A4	ANAPC1	S339	ochoa	Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
Q9H1B7	IRF2BPL	S553	ochoa	Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like)	Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins (PubMed:29374064). Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway (PubMed:29374064). Probably plays a role in the development of the central nervous system and in neuronal maintenance (Probable). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity). {ECO:0000250\|UniProtKB:Q5EIC4, ECO:0000269\|PubMed:29374064, ECO:0000305\|PubMed:17334524, ECO:0000305\|PubMed:29374064, ECO:0000305\|PubMed:30057031}.
Q9H1B7	IRF2BPL	S665	ochoa	Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like)	Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins (PubMed:29374064). Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway (PubMed:29374064). Probably plays a role in the development of the central nervous system and in neuronal maintenance (Probable). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity). {ECO:0000250\|UniProtKB:Q5EIC4, ECO:0000269\|PubMed:29374064, ECO:0000305\|PubMed:17334524, ECO:0000305\|PubMed:29374064, ECO:0000305\|PubMed:30057031}.
Q9H1H9	KIF13A	S1759	ochoa	Kinesin-like protein KIF13A (Kinesin-like protein RBKIN)	Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abscission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269\|PubMed:19841138, ECO:0000269\|PubMed:20208530}.
Q9H1H9	KIF13A	S1760	ochoa	Kinesin-like protein KIF13A (Kinesin-like protein RBKIN)	Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abscission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269\|PubMed:19841138, ECO:0000269\|PubMed:20208530}.
Q9H1I8	ASCC2	S713	ochoa	Activating signal cointegrator 1 complex subunit 2 (ASC-1 complex subunit p100) (Trip4 complex subunit p100)	Ubiquitin-binding protein involved in DNA repair and rescue of stalled ribosomes (PubMed:29144457, PubMed:32099016, PubMed:32579943, PubMed:36302773). Plays a role in DNA damage repair as component of the ASCC complex (PubMed:29144457). Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin chains (PubMed:29144457). Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation (PubMed:12077347). Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation (PubMed:32099016, PubMed:32579943, PubMed:36302773). Specifically recognizes and binds RPS20/uS10 ubiquitinated by ZNF598, promoting recruitment of the RQT (ribosome quality control trigger) complex on stalled ribosomes, followed by disassembly of stalled ribosomes (PubMed:36302773). {ECO:0000269\|PubMed:12077347, ECO:0000269\|PubMed:29144457, ECO:0000269\|PubMed:32099016, ECO:0000269\|PubMed:32579943, ECO:0000269\|PubMed:36302773}.
Q9H1K0	RBSN	S236	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H1K0	RBSN	S238	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H1K0	RBSN	S239	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H1K0	RBSN	S583	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H2E6	SEMA6A	S814	ochoa	Semaphorin-6A (Semaphorin VIA) (Sema VIA) (Semaphorin-6A-1) (SEMA6A-1)	Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation. {ECO:0000250\|UniProtKB:O35464}.; FUNCTION: (Microbial infection) Acts as a receptor for P.sordellii toxin TcsL in the in the vascular endothelium. {ECO:0000269\|PubMed:32302524, ECO:0000269\|PubMed:32589945}.
Q9H2G2	SLK	S347	ochoa\|psp	STE20-like serine/threonine-protein kinase (STE20-like kinase) (hSLK) (EC 2.7.11.1) (CTCL tumor antigen se20-9) (STE20-related serine/threonine-protein kinase) (STE20-related kinase) (Serine/threonine-protein kinase 2)	Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.
Q9H2P0	ADNP	S415	ochoa	Activity-dependent neuroprotector homeobox protein (Activity-dependent neuroprotective protein)	May be involved in transcriptional regulation. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation. Positively modulates WNT-beta-catenin/CTNN1B signaling, acting by regulating phosphorylation of, and thereby stabilizing, CTNNB1. May be required for neural induction and neuronal differentiation. May be involved in erythroid differentiation (By similarity). {ECO:0000250\|UniProtKB:Q9Z103}.
Q9H2X6	HIPK2	S854	ochoa	Homeodomain-interacting protein kinase 2 (hHIPk2) (EC 2.7.11.1)	Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1, ZBTB4 and DAZAP2. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. In response to DNA damage, phosphorylates DAZAP2 which localizes DAZAP2 to the nucleus, reduces interaction of DAZAP2 with HIPK2 and prevents DAZAP2-dependent ubiquitination of HIPK2 by E3 ubiquitin-protein ligase SIAH1 and subsequent proteasomal degradation (PubMed:33591310). Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. {ECO:0000269\|PubMed:11740489, ECO:0000269\|PubMed:11925430, ECO:0000269\|PubMed:12851404, ECO:0000269\|PubMed:12874272, ECO:0000269\|PubMed:14678985, ECO:0000269\|PubMed:17018294, ECO:0000269\|PubMed:17960875, ECO:0000269\|PubMed:18695000, ECO:0000269\|PubMed:18809579, ECO:0000269\|PubMed:19015637, ECO:0000269\|PubMed:19046997, ECO:0000269\|PubMed:19448668, ECO:0000269\|PubMed:20307497, ECO:0000269\|PubMed:20573984, ECO:0000269\|PubMed:20637728, ECO:0000269\|PubMed:20980392, ECO:0000269\|PubMed:21192925, ECO:0000269\|PubMed:22825850, ECO:0000269\|PubMed:33591310}.
Q9H2Y7	ZNF106	S878	ochoa	Zinc finger protein 106 (Zfp-106) (Zinc finger protein 474)	RNA-binding protein. Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA. Essential for maintenance of peripheral motor neuron and skeletal muscle function. Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism. {ECO:0000250\|UniProtKB:O88466}.
Q9H3D4	TP63	S463	ochoa	Tumor protein 63 (p63) (Chronic ulcerative stomatitis protein) (CUSP) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) (p40) (p51)	Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter. {ECO:0000269\|PubMed:11641404, ECO:0000269\|PubMed:12374749, ECO:0000269\|PubMed:12446779, ECO:0000269\|PubMed:12446784, ECO:0000269\|PubMed:20123734, ECO:0000269\|PubMed:22197488, ECO:0000269\|PubMed:9774969}.
Q9H3P7	ACBD3	S321	ochoa	Golgi resident protein GCP60 (Acyl-CoA-binding domain-containing protein 3) (Golgi complex-associated protein 1) (GOCAP1) (Golgi phosphoprotein 1) (GOLPH1) (PBR- and PKA-associated protein 7) (Peripheral benzodiazepine receptor-associated protein PAP7) [Cleaved into: Golgi resident protein GCP60, N-terminally processed]	Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi (PubMed:11590181). Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase (PubMed:27009356). {ECO:0000250\|UniProtKB:Q8BMP6, ECO:0000269\|PubMed:11590181, ECO:0000269\|PubMed:27009356}.; FUNCTION: (Microbial infection) Plays an essential role in Aichi virus RNA replication by recruiting PI4KB at the viral replication sites. {ECO:0000269\|PubMed:22124328, ECO:0000269\|PubMed:22258260, ECO:0000269\|PubMed:27989622}.
Q9H3Q1	CDC42EP4	S80	ochoa\|psp	Cdc42 effector protein 4 (Binder of Rho GTPases 4)	Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Q9H3Q1	CDC42EP4	S315	ochoa	Cdc42 effector protein 4 (Binder of Rho GTPases 4)	Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Q9H3R0	KDM4C	S487	ochoa	Lysine-specific demethylase 4C (EC 1.14.11.66) (Gene amplified in squamous cell carcinoma 1 protein) (GASC-1 protein) (JmjC domain-containing histone demethylation protein 3C) (Jumonji domain-containing protein 2C) ([histone H3]-trimethyl-L-lysine(9) demethylase 4C)	Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000269\|PubMed:16603238, ECO:0000269\|PubMed:28262558}.
Q9H3Y8	PPDPF	S29	ochoa	Pancreatic progenitor cell differentiation and proliferation factor (Exocrine differentiation and proliferation factor)	Probable regulator of exocrine pancreas development. {ECO:0000250}.
Q9H3Y8	PPDPF	S31	ochoa	Pancreatic progenitor cell differentiation and proliferation factor (Exocrine differentiation and proliferation factor)	Probable regulator of exocrine pancreas development. {ECO:0000250}.
Q9H3Y8	PPDPF	S32	ochoa	Pancreatic progenitor cell differentiation and proliferation factor (Exocrine differentiation and proliferation factor)	Probable regulator of exocrine pancreas development. {ECO:0000250}.
Q9H4A3	WNK1	S189	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4A3	WNK1	S1295	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4A3	WNK1	S1308	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4B7	TUBB1	S95	ochoa	Tubulin beta-1 chain	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Q9H4G0	EPB41L1	S678	ochoa	Band 4.1-like protein 1 (Erythrocyte membrane protein band 4.1-like 1) (Neuronal protein 4.1) (4.1N)	May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases.
Q9H4L4	SENP3	S238	ochoa	Sentrin-specific protease 3 (EC 3.4.22.-) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3)	Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:16608850, PubMed:32832608, PubMed:36050397). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8 (PubMed:18946085). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (PubMed:19680224). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation status of ZNF148 (PubMed:18259216). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608). Catalyzes desumoylation of MRE11 (PubMed:36050397). {ECO:0000269\|PubMed:15743823, ECO:0000269\|PubMed:16608850, ECO:0000269\|PubMed:18259216, ECO:0000269\|PubMed:18946085, ECO:0000269\|PubMed:19015314, ECO:0000269\|PubMed:19680224, ECO:0000269\|PubMed:22872859, ECO:0000269\|PubMed:32832608, ECO:0000269\|PubMed:36050397}.
Q9H4L5	OSBPL3	S172	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H4L5	OSBPL3	S309	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H4L5	OSBPL3	S416	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H4M9	EHD1	S355	ochoa	EH domain-containing protein 1 (PAST homolog 1) (hPAST1) (Testilin)	ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes (PubMed:24019528). Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis (PubMed:31615969). Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis (PubMed:25686250). {ECO:0000250\|UniProtKB:Q641Z6, ECO:0000250\|UniProtKB:Q9WVK4, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:17233914, ECO:0000269\|PubMed:20801876, ECO:0000269\|PubMed:24019528, ECO:0000269\|PubMed:25686250, ECO:0000269\|PubMed:31615969}.
Q9H4X1	RGCC	S71	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H4X1	RGCC	S75	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H4X1	RGCC	S97	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H4X1	RGCC	S107	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H5I1	SUV39H2	S388	ochoa	Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.355) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Lysine N-methyltransferase 1B) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2)	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269\|PubMed:14765126}.
Q9H5V7	IKZF5	S318	ochoa	Zinc finger protein Pegasus (Ikaros family zinc finger protein 5)	Transcriptional repressor that binds the core 5'GNNTGTNG-3' DNA consensus sequence (PubMed:10978333, PubMed:31217188). Involved in megakaryocyte differentiation. {ECO:0000269\|PubMed:10978333, ECO:0000269\|PubMed:31217188}.
Q9H694	BICC1	S612	ochoa	Protein bicaudal C homolog 1 (Bic-C)	Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development. {ECO:0000269\|PubMed:21922595}.
Q9H694	BICC1	S803	ochoa	Protein bicaudal C homolog 1 (Bic-C)	Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development. {ECO:0000269\|PubMed:21922595}.
Q9H6F5	CCDC86	S24	ochoa	Coiled-coil domain-containing protein 86 (Cytokine-induced protein with coiled-coil domain)	Required for proper chromosome segregation during mitosis and error-free mitotic progression. {ECO:0000269\|PubMed:36695333}.
Q9H6Q3	SLA2	S19	ochoa	Src-like-adapter 2 (Modulator of antigen receptor signaling) (MARS) (Src-like adapter protein 2) (SLAP-2)	Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269\|PubMed:11696592}.
Q9H6R7	WDCP	S510	ochoa	WD repeat and coiled-coil-containing protein	None
Q9H6R7	WDCP	S535	ochoa	WD repeat and coiled-coil-containing protein	None
Q9H6S0	YTHDC2	S1208	ochoa	3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (YTH domain-containing protein 2) (hYTHDC2)	3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity). {ECO:0000250\|UniProtKB:B2RR83, ECO:0000269\|PubMed:26318451, ECO:0000269\|PubMed:29033321, ECO:0000269\|PubMed:29970596}.
Q9H6S3	EPS8L2	S455	ochoa	Epidermal growth factor receptor kinase substrate 8-like protein 2 (EPS8-like protein 2) (Epidermal growth factor receptor pathway substrate 8-related protein 2) (EPS8-related protein 2)	Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. In the cochlea, is required for stereocilia maintenance in adult hair cells (By similarity). {ECO:0000250\|UniProtKB:Q99K30, ECO:0000269\|PubMed:14565974}.
Q9H6U6	BCAS3	S712	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6U6	BCAS3	S715	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6U6	BCAS3	S877	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6U6	BCAS3	S900	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6W3	RIOX1	S66	ochoa	Ribosomal oxygenase 1 (60S ribosomal protein L8 histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Myc-associated protein with JmjC domain) (Nucleolar protein 66) (hsNO66) (Ribosomal oxygenase NO66) (ROX)	Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (PubMed:23103944). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2) (By similarity). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis (PubMed:23103944). Participates in MYC-induced transcriptional activation (PubMed:17308053). {ECO:0000250\|UniProtKB:Q9JJF3, ECO:0000269\|PubMed:17308053, ECO:0000269\|PubMed:23103944}.
Q9H706	GAREM1	S622	ochoa	GRB2-associated and regulator of MAPK protein 1 (GRB2-associated and regulator of MAPK1)	[Isoform 1]: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation. {ECO:0000269\|PubMed:19509291}.
Q9H7D0	DOCK5	S1781	ochoa	Dedicator of cytokinesis protein 5	Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP (By similarity). Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (PubMed:19004829). {ECO:0000250\|UniProtKB:B2RY04, ECO:0000269\|PubMed:19004829}.
Q9H7N4	SCAF1	S680	ochoa	Splicing factor, arginine/serine-rich 19 (SR-related C-terminal domain-associated factor 1) (SR-related and CTD-associated factor 1) (SR-related-CTD-associated factor) (SCAF) (Serine arginine-rich pre-mRNA splicing factor SR-A1) (SR-A1)	May function in pre-mRNA splicing. {ECO:0000250}.
Q9H7N4	SCAF1	S725	ochoa	Splicing factor, arginine/serine-rich 19 (SR-related C-terminal domain-associated factor 1) (SR-related and CTD-associated factor 1) (SR-related-CTD-associated factor) (SCAF) (Serine arginine-rich pre-mRNA splicing factor SR-A1) (SR-A1)	May function in pre-mRNA splicing. {ECO:0000250}.
Q9H7P6	MVB12B	S207	ochoa	Multivesicular body subunit 12B (ESCRT-I complex subunit MVB12B) (Protein FAM125B)	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies.
Q9H8M5	CNNM2	S749	ochoa	Metal transporter CNNM2 (Ancient conserved domain-containing protein 2) (Cyclin-M2)	Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity). {ECO:0000250\|UniProtKB:Q3TWN3}.
Q9H8V3	ECT2	S889	ochoa	Protein ECT2 (Epithelial cell-transforming sequence 2 oncogene)	Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269\|PubMed:10579713, ECO:0000269\|PubMed:14645260, ECO:0000269\|PubMed:15254234, ECO:0000269\|PubMed:15545273, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16170345, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:16495035, ECO:0000269\|PubMed:19129481, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19617897, ECO:0000269\|PubMed:21189248, ECO:0000269\|PubMed:21373644, ECO:0000269\|PubMed:25068414, ECO:0000269\|PubMed:31888991}.
Q9H8W4	PLEKHF2	S230	ochoa	Pleckstrin homology domain-containing family F member 2 (PH domain-containing family F member 2) (Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains) (EAPF) (PH and FYVE domain-containing protein 2) (Phafin-2) (Phafin2) (Zinc finger FYVE domain-containing protein 18)	May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport. Enhances cellular sensitivity to TNF-induced apoptosis (PubMed:18288467). {ECO:0000269\|PubMed:18288467, ECO:0000269\|PubMed:19995552, ECO:0000269\|PubMed:22816767}.
Q9H910	JPT2	S75	ochoa	Jupiter microtubule associated homolog 2 (Hematological and neurological expressed 1-like protein) (HN1-like protein)	Nicotinic acid adenine dinucleotide phosphate (NAADP) binding protein required for NAADP-evoked intracellular calcium release (PubMed:33758061, PubMed:33758062). Confers NAADP-sensitivity to the two pore channels (TPCs) complex (PubMed:33758061). Enables NAADP to activate Ca(2+) release from the endoplasmic reticulum through ryanodine receptors (PubMed:33758062). {ECO:0000269\|PubMed:33758061, ECO:0000269\|PubMed:33758062}.; FUNCTION: (Microbial infection) Involved in the endolysosomal trafficking of human coronavirus SARS-CoV-2. {ECO:0000269\|PubMed:33758061}.
Q9H992	MARCHF7	S365	ochoa	E3 ubiquitin-protein ligase MARCHF7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING finger protein 177) (RING-type E3 ubiquitin transferase MARCHF7)	E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:16868077). May be involved in T-cell proliferation by regulating LIF secretion (By similarity). May play a role in lysosome homeostasis (PubMed:31270356). Promotes 'Lys-6', 'Lys-11' and 'Lys-63'-linked mixed polyubiquitination on ATG14 leading to the inhibition of autophagy by impairing the interaction between ATG14 and STX7 (PubMed:37632749). Participates in the dopamine-mediated negative regulation of the NLRP3 inflammasome by promoting its uibiquitination and subsequent degradation (PubMed:25594175). {ECO:0000250\|UniProtKB:Q9WV66, ECO:0000269\|PubMed:16868077, ECO:0000269\|PubMed:25594175, ECO:0000269\|PubMed:31270356, ECO:0000269\|PubMed:37632749}.
Q9H9C1	VIPAS39	S130	ochoa	Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction)	Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity). {ECO:0000250\|UniProtKB:Q23288, ECO:0000269\|PubMed:19109425, ECO:0000269\|PubMed:20190753}.
Q9H9E3	COG4	S17	ochoa	Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4)	Required for normal Golgi function (PubMed:19536132, PubMed:30290151). Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 (PubMed:19536132). {ECO:0000269\|PubMed:19536132, ECO:0000269\|PubMed:30290151}.
Q9H9Q4	NHEJ1	S251	psp	Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)	DNA repair protein involved in DNA non-homologous end joining (NHEJ); it is required for double-strand break (DSB) repair and V(D)J recombination and is also involved in telomere maintenance (PubMed:16439204, PubMed:16439205, PubMed:17317666, PubMed:17470781, PubMed:17717001, PubMed:18158905, PubMed:18644470, PubMed:20558749, PubMed:26100018, PubMed:28369633). Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends (PubMed:17470781, PubMed:17717001, PubMed:19056826). Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (PubMed:25670504, PubMed:30250067). May act in concert with XRCC5-XRCC6 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are non-complementary or partially complementary (PubMed:16439204, PubMed:16439205, PubMed:17317666, PubMed:17470781). In some studies, has been shown to associate with XRCC4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed:21768349, PubMed:21775435, PubMed:22228831, PubMed:22287571, PubMed:26100018, PubMed:27437582, PubMed:28500754). Alternatively, it has also been shown that rather than forming filaments, a single NHEJ1 dimer interacts through both head domains with XRCC4 to promote the close alignment of DNA ends (By similarity). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other (PubMed:27437582, PubMed:28500754). The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed:27437582). Binds DNA in a length-dependent manner (PubMed:17317666, PubMed:18158905). {ECO:0000250\|UniProtKB:A0A1L8ENT6, ECO:0000269\|PubMed:16439204, ECO:0000269\|PubMed:16439205, ECO:0000269\|PubMed:17317666, ECO:0000269\|PubMed:17470781, ECO:0000269\|PubMed:17717001, ECO:0000269\|PubMed:18158905, ECO:0000269\|PubMed:18644470, ECO:0000269\|PubMed:19056826, ECO:0000269\|PubMed:20558749, ECO:0000269\|PubMed:21768349, ECO:0000269\|PubMed:21775435, ECO:0000269\|PubMed:22228831, ECO:0000269\|PubMed:22287571, ECO:0000269\|PubMed:25670504, ECO:0000269\|PubMed:26100018, ECO:0000269\|PubMed:27437582, ECO:0000269\|PubMed:28369633, ECO:0000269\|PubMed:28500754, ECO:0000269\|PubMed:30250067}.
Q9HAU0	PLEKHA5	S126	ochoa	Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2)	None
Q9HAU0	PLEKHA5	S132	ochoa	Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2)	None
Q9HAU0	PLEKHA5	S828	ochoa	Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2)	None
Q9HAU0	PLEKHA5	S861	ochoa	Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2)	None
Q9HAU0	PLEKHA5	S1098	ochoa	Pleckstrin homology domain-containing family A member 5 (PH domain-containing family A member 5) (Phosphoinositol 3-phosphate-binding protein 2) (PEPP-2)	None
Q9HB19	PLEKHA2	S320	ochoa	Pleckstrin homology domain-containing family A member 2 (PH domain-containing family A member 2) (Tandem PH domain-containing protein 2) (TAPP-2)	Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity). {ECO:0000250}.
Q9HB20	PLEKHA3	S215	ochoa	Pleckstrin homology domain-containing family A member 3 (PH domain-containing family A member 3) (Phosphatidylinositol-four-phosphate adapter protein 1) (FAPP-1) (Phosphoinositol 4-phosphate adapter protein 1)	Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (PubMed:15107860). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (PubMed:30659099). Binds preferentially to PtdIns(4)P (PubMed:11001876, PubMed:15107860). Negatively regulates APOB secretion from hepatocytes (PubMed:30659099). {ECO:0000269\|PubMed:11001876, ECO:0000269\|PubMed:15107860, ECO:0000269\|PubMed:30659099}.
Q9HB20	PLEKHA3	S221	ochoa	Pleckstrin homology domain-containing family A member 3 (PH domain-containing family A member 3) (Phosphatidylinositol-four-phosphate adapter protein 1) (FAPP-1) (Phosphoinositol 4-phosphate adapter protein 1)	Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (PubMed:15107860). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (PubMed:30659099). Binds preferentially to PtdIns(4)P (PubMed:11001876, PubMed:15107860). Negatively regulates APOB secretion from hepatocytes (PubMed:30659099). {ECO:0000269\|PubMed:11001876, ECO:0000269\|PubMed:15107860, ECO:0000269\|PubMed:30659099}.
Q9HB20	PLEKHA3	S236	ochoa	Pleckstrin homology domain-containing family A member 3 (PH domain-containing family A member 3) (Phosphatidylinositol-four-phosphate adapter protein 1) (FAPP-1) (Phosphoinositol 4-phosphate adapter protein 1)	Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (PubMed:15107860). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (PubMed:30659099). Binds preferentially to PtdIns(4)P (PubMed:11001876, PubMed:15107860). Negatively regulates APOB secretion from hepatocytes (PubMed:30659099). {ECO:0000269\|PubMed:11001876, ECO:0000269\|PubMed:15107860, ECO:0000269\|PubMed:30659099}.
Q9HB20	PLEKHA3	S250	ochoa	Pleckstrin homology domain-containing family A member 3 (PH domain-containing family A member 3) (Phosphatidylinositol-four-phosphate adapter protein 1) (FAPP-1) (Phosphoinositol 4-phosphate adapter protein 1)	Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (PubMed:15107860). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (PubMed:30659099). Binds preferentially to PtdIns(4)P (PubMed:11001876, PubMed:15107860). Negatively regulates APOB secretion from hepatocytes (PubMed:30659099). {ECO:0000269\|PubMed:11001876, ECO:0000269\|PubMed:15107860, ECO:0000269\|PubMed:30659099}.
Q9HB90	RRAGC	S21	ochoa\|psp	Ras-related GTP-binding protein C (Rag C) (RagC) (EC 3.6.5.-) (GTPase-interacting protein 2) (TIB929)	Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade (PubMed:20381137, PubMed:24095279, PubMed:27234373, PubMed:31601708, PubMed:31601764, PubMed:32612235, PubMed:34071043, PubMed:36697823, PubMed:37057673). Forms heterodimeric Rag complexes with RagA/RRAGA or RagB/RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form: RagC/RRAGC is in its active form when GDP-bound RagC/RRAGC forms a complex with GTP-bound RagA/RRAGA (or RagB/RRAGB) and in an inactive form when GTP-bound RagC/RRAGC heterodimerizes with GDP-bound RagA/RRAGA (or RagB/RRAGB) (PubMed:24095279, PubMed:31601708, PubMed:31601764, PubMed:32868926). In its GDP-bound active form, promotes the recruitment of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB (PubMed:20381137, PubMed:24095279, PubMed:27234373, PubMed:32612235, PubMed:36697823). This is a crucial step in the activation of the MTOR signaling cascade by amino acids (PubMed:20381137, PubMed:24095279, PubMed:27234373). Also plays a central role in the non-canonical mTORC1 complex, which acts independently of RHEB and specifically mediates phosphorylation of MiT/TFE factors TFEB and TFE3: GDP-bound RagC/RRAGC mediates recruitment of MiT/TFE factors TFEB and TFE3 (PubMed:32612235, PubMed:36697823). {ECO:0000269\|PubMed:20381137, ECO:0000269\|PubMed:24095279, ECO:0000269\|PubMed:27234373, ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:32612235, ECO:0000269\|PubMed:32868926, ECO:0000269\|PubMed:34071043, ECO:0000269\|PubMed:36697823, ECO:0000269\|PubMed:37057673}.
Q9HBD1	RC3H2	S562	ochoa	Roquin-2 (EC 2.3.2.27) (Membrane-associated nucleic acid-binding protein) (RING finger and CCCH-type zinc finger domain-containing protein 2) (RING finger protein 164) (RING-type E3 ubiquitin transferase Roquin-2)	Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H1, possibly leading to feedback loop regulation (By similarity). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406). Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2B, UBE2D2, UBE2E2, UBE2E3, UBE2G2, UBE2K and UBE2Q2 and produces polyubiquitin chains (PubMed:26489670). Shows the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains (PubMed:26489670). Involved in the ubiquitination of MAP3K5 (PubMed:24448648, PubMed:26489670, PubMed:29186683). Able to interact with double-stranded RNA (dsRNA) (PubMed:26489670). {ECO:0000250\|UniProtKB:P0C090, ECO:0000269\|PubMed:24448648, ECO:0000269\|PubMed:26489670, ECO:0000269\|PubMed:29186683}.
Q9HC35	EML4	S138	ochoa	Echinoderm microtubule-associated protein-like 4 (EMAP-4) (Restrictedly overexpressed proliferation-associated protein) (Ropp 120)	Essential for the formation and stability of microtubules (MTs) (PubMed:16890222, PubMed:31409757). Required for the organization of the mitotic spindle and for the proper attachment of kinetochores to MTs (PubMed:25789526). Promotes the recruitment of NUDC to the mitotic spindle for mitotic progression (PubMed:25789526). {ECO:0000269\|PubMed:16890222, ECO:0000269\|PubMed:25789526, ECO:0000269\|PubMed:31409757}.
Q9HC35	EML4	S144	ochoa\|psp	Echinoderm microtubule-associated protein-like 4 (EMAP-4) (Restrictedly overexpressed proliferation-associated protein) (Ropp 120)	Essential for the formation and stability of microtubules (MTs) (PubMed:16890222, PubMed:31409757). Required for the organization of the mitotic spindle and for the proper attachment of kinetochores to MTs (PubMed:25789526). Promotes the recruitment of NUDC to the mitotic spindle for mitotic progression (PubMed:25789526). {ECO:0000269\|PubMed:16890222, ECO:0000269\|PubMed:25789526, ECO:0000269\|PubMed:31409757}.
Q9HCC9	ZFYVE28	S384	ochoa	Lateral signaling target protein 2 homolog (hLst2) (Zinc finger FYVE domain-containing protein 28)	Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated. {ECO:0000269\|PubMed:19460345}.
Q9HCD6	TANC2	S1452	ochoa	Protein TANC2 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2)	Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines. {ECO:0000269\|PubMed:30021165}.
Q9HCE1	MOV10	S977	ochoa	Helicase MOV-10 (EC 3.6.4.13) (Armitage homolog) (Moloney leukemia virus 10 protein)	5' to 3' RNA helicase that is involved in a number of cellular roles ranging from mRNA metabolism and translation, modulation of viral infectivity, inhibition of retrotransposition, or regulation of synaptic transmission (PubMed:23093941). Plays an important role in innate antiviral immunity by promoting type I interferon production (PubMed:27016603, PubMed:27974568, PubMed:35157734). Mechanistically, specifically uses IKKepsilon/IKBKE as the mediator kinase for IRF3 activation (PubMed:27016603, PubMed:35157734). Blocks HIV-1 virus replication at a post-entry step (PubMed:20215113). Counteracts HIV-1 Vif-mediated degradation of APOBEC3G through its helicase activity by interfering with the ubiquitin-proteasome pathway (PubMed:29258557). Also inhibits hepatitis B virus/HBV replication by interacting with HBV RNA and thereby inhibiting the early step of viral reverse transcription (PubMed:31722967). Contributes to UPF1 mRNA target degradation by translocation along 3' UTRs (PubMed:24726324). Required for microRNA (miRNA)-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (PubMed:16289642, PubMed:17507929, PubMed:22791714). In cooperation with FMR1, regulates miRNA-mediated translational repression by AGO2 (PubMed:25464849). Restricts retrotransposition of long interspersed element-1 (LINE-1) in cooperation with TUT4 and TUT7 counteracting the RNA chaperonne activity of L1RE1 (PubMed:23093941, PubMed:30122351). Facilitates LINE-1 uridylation by TUT4 and TUT7 (PubMed:30122351). Required for embryonic viability and for normal central nervous system development and function. Plays two critical roles in early brain development: suppresses retroelements in the nucleus by directly inhibiting cDNA synthesis, while regulates cytoskeletal mRNAs to influence neurite outgrowth in the cytosol (By similarity). May function as a messenger ribonucleoprotein (mRNP) clearance factor (PubMed:24726324). {ECO:0000250\|UniProtKB:P23249, ECO:0000269\|PubMed:16289642, ECO:0000269\|PubMed:17507929, ECO:0000269\|PubMed:20215113, ECO:0000269\|PubMed:22791714, ECO:0000269\|PubMed:23093941, ECO:0000269\|PubMed:24726324, ECO:0000269\|PubMed:25464849, ECO:0000269\|PubMed:27016603, ECO:0000269\|PubMed:27974568, ECO:0000269\|PubMed:29258557, ECO:0000269\|PubMed:30122351, ECO:0000269\|PubMed:31722967, ECO:0000269\|PubMed:35157734}.; FUNCTION: (Microbial infection) Required for RNA-directed transcription and replication of the human hepatitis delta virus (HDV). Interacts with small capped HDV RNAs derived from genomic hairpin structures that mark the initiation sites of RNA-dependent HDV RNA transcription. {ECO:0000269\|PubMed:18552826}.
Q9HCG8	CWC22	S792	ochoa	Pre-mRNA-splicing factor CWC22 homolog (Nucampholin homolog) (fSAPb)	Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:12226669, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Promotes exon-junction complex (EJC) assembly (PubMed:22959432, PubMed:22961380). Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay. {ECO:0000269\|PubMed:11991638, ECO:0000269\|PubMed:12226669, ECO:0000269\|PubMed:22959432, ECO:0000269\|PubMed:22961380, ECO:0000269\|PubMed:23236153, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000305\|PubMed:33509932}.
Q9HCH5	SYTL2	S466	ochoa	Synaptotagmin-like protein 2 (Breast cancer-associated antigen SGA-72M) (Exophilin-4)	Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon-containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca(2+) while binding to PIP2 is Ca(2+) insensitive. {ECO:0000269\|PubMed:17182843, ECO:0000269\|PubMed:18266782, ECO:0000269\|PubMed:18812475}.
Q9HCH5	SYTL2	S517	ochoa	Synaptotagmin-like protein 2 (Breast cancer-associated antigen SGA-72M) (Exophilin-4)	Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon-containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca(2+) while binding to PIP2 is Ca(2+) insensitive. {ECO:0000269\|PubMed:17182843, ECO:0000269\|PubMed:18266782, ECO:0000269\|PubMed:18812475}.
Q9HCK1	ZDBF2	S539	ochoa	DBF4-type zinc finger-containing protein 2	None
Q9HCM3	KIAA1549	S1418	ochoa	UPF0606 protein KIAA1549	May play a role in photoreceptor function. {ECO:0000269\|PubMed:30120214}.
Q9HCN4	GPN1	S320	ochoa	GPN-loop GTPase 1 (EC 3.6.5.-) (MBD2-interacting protein) (MBDin) (RNAPII-associated protein 4) (XPA-binding protein 1)	Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII) (PubMed:20855544, PubMed:21768307). May act at an RNAP assembly step prior to nuclear import (PubMed:21768307). Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation (PubMed:17643375). May be involved in nuclear localization of XPA (PubMed:11058119). {ECO:0000269\|PubMed:17643375, ECO:0000269\|PubMed:20855544, ECO:0000269\|PubMed:21768307, ECO:0000305\|PubMed:11058119}.
Q9HCU4	CELSR2	S2668	ochoa	Cadherin EGF LAG seven-pass G-type receptor 2 (Cadherin family member 10) (Epidermal growth factor-like protein 2) (EGF-like protein 2) (Flamingo homolog 3) (Multiple epidermal growth factor-like domains protein 3) (Multiple EGF-like domains protein 3)	Receptor that may have an important role in cell/cell signaling during nervous system formation.
Q9HD20	ATP13A1	S905	ochoa	Endoplasmic reticulum transmembrane helix translocase (EC 7.4.2.-) (Endoplasmic reticulum P5A-ATPase)	Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (PubMed:32973005, PubMed:36264797). Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (PubMed:32973005). Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (PubMed:32973005). {ECO:0000269\|PubMed:32973005, ECO:0000269\|PubMed:36264797}.
Q9HD67	MYO10	S968	ochoa	Unconventional myosin-X (Unconventional myosin-10)	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (PubMed:27580874). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. {ECO:0000269\|PubMed:16894163, ECO:0000269\|PubMed:18570893, ECO:0000269\|PubMed:27580874}.; FUNCTION: [Isoform Headless]: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion (By similarity). {ECO:0000250\|UniProtKB:F8VQB6}.
Q9HDC5	JPH1	S168	ochoa	Junctophilin-1 (JP-1) (Junctophilin type 1)	Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Q9HDC5	JPH1	S171	ochoa	Junctophilin-1 (JP-1) (Junctophilin type 1)	Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Q9HDC5	JPH1	S174	ochoa	Junctophilin-1 (JP-1) (Junctophilin type 1)	Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Q9NP61	ARFGAP3	S375	ochoa	ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3)	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269\|PubMed:11172815}.
Q9NP74	PALMD	S370	ochoa	Palmdelphin (Paralemmin-like protein)	None
Q9NPF5	DMAP1	S418	ochoa	DNA methyltransferase 1-associated protein 1 (DNMAP1) (DNMT1-associated protein 1)	Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity. {ECO:0000269\|PubMed:14665632, ECO:0000269\|PubMed:14966270, ECO:0000269\|PubMed:14978102, ECO:0000269\|PubMed:15367675}.
Q9NPI1	BRD7	S47	ochoa	Bromodomain-containing protein 7 (75 kDa bromodomain protein) (Protein CELTIX-1)	Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. {ECO:0000250, ECO:0000269\|PubMed:16265664, ECO:0000269\|PubMed:16475162, ECO:0000269\|PubMed:20215511, ECO:0000269\|PubMed:20228809, ECO:0000269\|PubMed:20660729}.
Q9NPI6	DCP1A	S186	ochoa	mRNA-decapping enzyme 1A (EC 3.6.1.62) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF)	Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:12417715). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12417715). Contributes to the transactivation of target genes after stimulation by TGFB1 (PubMed:11836524). Essential for embryonic development (PubMed:33813271). {ECO:0000269\|PubMed:11836524, ECO:0000269\|PubMed:12417715, ECO:0000269\|PubMed:33813271}.
Q9NQ29	LUC7L	S342	ochoa	Putative RNA-binding protein Luc7-like 1 (Putative SR protein LUC7B1) (SR+89)	May bind to RNA via its Arg/Ser-rich domain. {ECO:0000269\|PubMed:11170747}.
Q9NQ66	PLCB1	S988	ochoa	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-I) (PLC-I) (Phospholipase C-beta-1) (PLC-beta-1)	Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors (PubMed:9188725). Regulates the function of the endothelial barrier. {ECO:0000250\|UniProtKB:Q9Z1B3, ECO:0000269\|PubMed:9188725}.
Q9NQ75	CASS4	S311	ochoa	Cas scaffolding protein family member 4 (HEF-like protein) (HEF1-EFS-p130Cas-like protein) (HEPL)	Docking protein that plays a role in tyrosine kinase-based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading. {ECO:0000269\|PubMed:18256281}.
Q9NQB0	TCF7L2	S185	ochoa	Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (hTCF-4)	Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as a repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. {ECO:0000269\|PubMed:12408868, ECO:0000269\|PubMed:12727872, ECO:0000269\|PubMed:19443654, ECO:0000269\|PubMed:22699938, ECO:0000269\|PubMed:9727977}.
Q9NQS7	INCENP	S208	ochoa	Inner centromere protein	Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules (PubMed:12925766, PubMed:15316025, PubMed:27332895). The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC (PubMed:27332895). Required for localization of CBX5 to mitotic centromeres (PubMed:21346195). Controls the kinetochore localization of BUB1 (PubMed:16760428). {ECO:0000250\|UniProtKB:P53352, ECO:0000269\|PubMed:12925766, ECO:0000269\|PubMed:15316025, ECO:0000269\|PubMed:16760428, ECO:0000269\|PubMed:21346195, ECO:0000269\|PubMed:27332895}.
Q9NQW6	ANLN	S225	ochoa	Anillin	Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269\|PubMed:10931866, ECO:0000269\|PubMed:12479805, ECO:0000269\|PubMed:15496454, ECO:0000269\|PubMed:16040610, ECO:0000269\|PubMed:16357138, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:24676636}.
Q9NQW6	ANLN	S281	ochoa	Anillin	Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269\|PubMed:10931866, ECO:0000269\|PubMed:12479805, ECO:0000269\|PubMed:15496454, ECO:0000269\|PubMed:16040610, ECO:0000269\|PubMed:16357138, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:24676636}.
Q9NQW6	ANLN	S362	ochoa	Anillin	Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269\|PubMed:10931866, ECO:0000269\|PubMed:12479805, ECO:0000269\|PubMed:15496454, ECO:0000269\|PubMed:16040610, ECO:0000269\|PubMed:16357138, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:24676636}.
Q9NQW6	ANLN	S664	ochoa	Anillin	Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269\|PubMed:10931866, ECO:0000269\|PubMed:12479805, ECO:0000269\|PubMed:15496454, ECO:0000269\|PubMed:16040610, ECO:0000269\|PubMed:16357138, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:24676636}.
Q9NQX3	GPHN	S268	ochoa	Gephyrin [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)]	Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Acts as a major instructive molecule at inhibitory synapses, where it also clusters GABA type A receptors (PubMed:25025157, PubMed:26613940). {ECO:0000250\|UniProtKB:Q03555, ECO:0000269\|PubMed:25025157, ECO:0000269\|PubMed:26613940}.; FUNCTION: Also has a catalytic activity and catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. {ECO:0000269\|PubMed:26613940}.
Q9NQX3	GPHN	S283	ochoa	Gephyrin [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)]	Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Acts as a major instructive molecule at inhibitory synapses, where it also clusters GABA type A receptors (PubMed:25025157, PubMed:26613940). {ECO:0000250\|UniProtKB:Q03555, ECO:0000269\|PubMed:25025157, ECO:0000269\|PubMed:26613940}.; FUNCTION: Also has a catalytic activity and catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. {ECO:0000269\|PubMed:26613940}.
Q9NR09	BIRC6	S486	ochoa\|psp	Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6 (EC 2.3.2.24) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (Baculoviral IAP repeat-containing protein 6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON)	Anti-apoptotic protein known as inhibitor of apoptosis (IAP) which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase (PubMed:14765125, PubMed:15200957, PubMed:18329369). Unlike most IAPs, does not contain a RING domain and it is not a RING-type E3 ligase (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Instead acts as a dual E2/E3 enzyme that combines ubiquitin conjugating (E2) and ubiquitin ligase (E3) activities in a single polypeptide (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitination is mediated by a non-canonical E1 ubiquitin activating enzyme UBA6 (PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates CASP3, CASP7 and CASP9 and inhibits their caspase activity; also ubiquitinates their procaspases but to a weaker extent (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates pro-apoptotic factors DIABLO/SMAC and HTRA2 (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). DIABLO/SMAC antagonizes the caspase inhibition activity of BIRC6 by competing for the same binding sites as the caspases (PubMed:18329369, PubMed:36758106). Ubiquitinates the autophagy protein MAP1LC3B; this activity is also inhibited by DIABLO/SMAC (PubMed:36758105). Important regulator for the final stages of cytokinesis (PubMed:18329369). Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification (PubMed:18329369). {ECO:0000269\|PubMed:14765125, ECO:0000269\|PubMed:15200957, ECO:0000269\|PubMed:18329369, ECO:0000269\|PubMed:36758104, ECO:0000269\|PubMed:36758105, ECO:0000269\|PubMed:36758106}.
Q9NR09	BIRC6	S587	ochoa	Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6 (EC 2.3.2.24) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (Baculoviral IAP repeat-containing protein 6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON)	Anti-apoptotic protein known as inhibitor of apoptosis (IAP) which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase (PubMed:14765125, PubMed:15200957, PubMed:18329369). Unlike most IAPs, does not contain a RING domain and it is not a RING-type E3 ligase (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Instead acts as a dual E2/E3 enzyme that combines ubiquitin conjugating (E2) and ubiquitin ligase (E3) activities in a single polypeptide (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitination is mediated by a non-canonical E1 ubiquitin activating enzyme UBA6 (PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates CASP3, CASP7 and CASP9 and inhibits their caspase activity; also ubiquitinates their procaspases but to a weaker extent (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). Ubiquitinates pro-apoptotic factors DIABLO/SMAC and HTRA2 (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). DIABLO/SMAC antagonizes the caspase inhibition activity of BIRC6 by competing for the same binding sites as the caspases (PubMed:18329369, PubMed:36758106). Ubiquitinates the autophagy protein MAP1LC3B; this activity is also inhibited by DIABLO/SMAC (PubMed:36758105). Important regulator for the final stages of cytokinesis (PubMed:18329369). Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification (PubMed:18329369). {ECO:0000269\|PubMed:14765125, ECO:0000269\|PubMed:15200957, ECO:0000269\|PubMed:18329369, ECO:0000269\|PubMed:36758104, ECO:0000269\|PubMed:36758105, ECO:0000269\|PubMed:36758106}.
Q9NR19	ACSS2	S36	ochoa	Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acetyl-CoA synthetase 1) (AceCS1) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme) (Propionate--CoA ligase) (EC 6.2.1.17)	Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:10843999, PubMed:28003429, PubMed:28552616). Acetate is the preferred substrate (PubMed:10843999, PubMed:28003429). Can also utilize propionate with a much lower affinity (By similarity). Nuclear ACSS2 promotes glucose deprivation-induced lysosomal biogenesis and autophagy, tumor cell survival and brain tumorigenesis (PubMed:28552616). Glucose deprivation results in AMPK-mediated phosphorylation of ACSS2 leading to its translocation to the nucleus where it binds to TFEB and locally produces acetyl-CoA for histone acetylation in the promoter regions of TFEB target genes thereby activating their transcription (PubMed:28552616). The regulation of genes associated with autophagy and lysosomal activity through ACSS2 is important for brain tumorigenesis and tumor survival (PubMed:28552616). Acts as a chromatin-bound transcriptional coactivator that up-regulates histone acetylation and expression of neuronal genes (By similarity). Can be recruited to the loci of memory-related neuronal genes to maintain a local acetyl-CoA pool, providing the substrate for histone acetylation and promoting the expression of specific genes, which is essential for maintaining long-term spatial memory (By similarity). {ECO:0000250\|UniProtKB:Q9QXG4, ECO:0000269\|PubMed:10843999, ECO:0000269\|PubMed:28003429, ECO:0000269\|PubMed:28552616}.
Q9NR48	ASH1L	S576	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NR48	ASH1L	S1681	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NR48	ASH1L	S1709	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NR48	ASH1L	S1748	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NR48	ASH1L	S1754	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NRA8	EIF4ENIF1	S687	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRA8	EIF4ENIF1	S693	ochoa\|psp	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRA8	EIF4ENIF1	S752	ochoa\|psp	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRA8	EIF4ENIF1	S757	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRF8	CTPS2	S568	ochoa\|psp	CTP synthase 2 (EC 6.3.4.2) (CTP synthetase 2) (UTP--ammonia ligase 2)	Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. {ECO:0000269\|PubMed:10899599, ECO:0000269\|PubMed:16179339}.
Q9NRY4	ARHGAP35	S1136	ochoa	Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Glucocorticoid receptor repression factor 1) (GRF-1) (Rho GAP p190A) (p190-A)	Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492). This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (PubMed:1894621). {ECO:0000250\|UniProtKB:P81128, ECO:0000250\|UniProtKB:Q91YM2, ECO:0000269\|PubMed:1894621, ECO:0000269\|PubMed:19673492, ECO:0000269\|PubMed:28894085}.
Q9NS37	CREBZF	S22	ochoa	CREB/ATF bZIP transcription factor (Host cell factor-binding transcription factor Zhangfei) (HCF-binding transcription factor Zhangfei)	Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells. {ECO:0000269\|PubMed:10871379, ECO:0000269\|PubMed:15705566}.
Q9NS91	RAD18	S164	ochoa	E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (hHR18) (hRAD18) (RING finger protein 73) (RING-type E3 ubiquitin transferase RAD18)	E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. {ECO:0000269\|PubMed:17108083, ECO:0000269\|PubMed:21659603}.
Q9NSI6	BRWD1	S1481	ochoa	Bromodomain and WD repeat-containing protein 1 (WD repeat-containing protein 9)	May be a transcriptional activator. May be involved in chromatin remodeling (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000250, ECO:0000269\|PubMed:21834987}.
Q9NTI5	PDS5B	S1166	ochoa	Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3)	Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269\|PubMed:10963680, ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19696148}.
Q9NTI5	PDS5B	S1182	ochoa	Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3)	Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269\|PubMed:10963680, ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19696148}.
Q9NUE0	ZDHHC18	S59	ochoa	Palmitoyltransferase ZDHHC18 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 18) (DHHC-18) (Zinc finger DHHC domain-containing protein 18)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK (PubMed:23034182, PubMed:27481942, PubMed:35438208). Acts as a negative regulator of the cGAS-STING pathway be mediating palmitoylation and inactivation of CGAS (PubMed:35438208). May also have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling (PubMed:27481942). {ECO:0000269\|PubMed:23034182, ECO:0000269\|PubMed:27481942, ECO:0000269\|PubMed:35438208}.
Q9NUL3	STAU2	S194	ochoa	Double-stranded RNA-binding protein Staufen homolog 2	RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). {ECO:0000250\|UniProtKB:Q68SB1}.
Q9NUL3	STAU2	S432	ochoa	Double-stranded RNA-binding protein Staufen homolog 2	RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). {ECO:0000250\|UniProtKB:Q68SB1}.
Q9NUQ6	SPATS2L	S369	ochoa	SPATS2-like protein (DNA polymerase-transactivated protein 6) (Stress granule and nucleolar protein) (SGNP)	None
Q9NV58	RNF19A	S288	ochoa	E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.31) (Double ring-finger protein) (Dorfin) (RING finger protein 19A) (p38)	E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection. {ECO:0000269\|PubMed:11237715, ECO:0000269\|PubMed:12145308, ECO:0000269\|PubMed:12750386, ECO:0000269\|PubMed:15456787, ECO:0000269\|PubMed:16513638}.
Q9NV70	EXOC1	S470	ochoa	Exocyst complex component 1 (Exocyst complex component Sec3)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; FUNCTION: (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269\|PubMed:19889084}.
Q9NVE7	PANK4	S393	ochoa	4'-phosphopantetheine phosphatase (EC 3.1.3.-) (Inactive pantothenic acid kinase 4) (hPanK4)	Phosphatase which shows a preference for 4'-phosphopantetheine and its oxidatively damaged forms (sulfonate or S-sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein (PubMed:27322068). May play a role in the physiological regulation of CoA intracellular levels (Probable). {ECO:0000269\|PubMed:27322068, ECO:0000305\|PubMed:27322068}.
Q9NVF7	FBXO28	S344	ochoa	F-box only protein 28	Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}.
Q9NVI1	FANCI	S565	psp	Fanconi anemia group I protein (Protein FACI)	Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites (PubMed:17412408, PubMed:17460694, PubMed:17452773, PubMed:19111657, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (PubMed:19589784). Participates in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:25862789). {ECO:0000250\|UniProtKB:B0I564, ECO:0000269\|PubMed:17412408, ECO:0000269\|PubMed:17452773, ECO:0000269\|PubMed:17460694, ECO:0000269\|PubMed:19111657, ECO:0000269\|PubMed:19589784, ECO:0000269\|PubMed:25862789, ECO:0000269\|PubMed:36385258}.
Q9NVN8	GNL3L	S519	ochoa	Guanine nucleotide-binding protein-like 3-like protein	Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP. {ECO:0000269\|PubMed:16251348, ECO:0000269\|PubMed:17034816, ECO:0000269\|PubMed:19487455, ECO:0000269\|PubMed:21132010}.
Q9NW97	TMEM51	S163	ochoa	Transmembrane protein 51	None
Q9NWQ8	PAG1	S339	ochoa	Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 (Csk-binding protein) (Transmembrane adapter protein PAG) (Transmembrane phosphoprotein Cbp)	Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. {ECO:0000269\|PubMed:10790433}.
Q9NWZ3	IRAK4	S157	ochoa	Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64)	Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. {ECO:0000269\|PubMed:11960013, ECO:0000269\|PubMed:12538665, ECO:0000269\|PubMed:15084582, ECO:0000269\|PubMed:17217339, ECO:0000269\|PubMed:17337443, ECO:0000269\|PubMed:17878374, ECO:0000269\|PubMed:17997719, ECO:0000269\|PubMed:20400509, ECO:0000269\|PubMed:24316379}.
Q9NX63	CHCHD3	S56	ochoa	MICOS complex subunit MIC19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3)	Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (PubMed:25781180, PubMed:32567732, PubMed:33130824). Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:25781180, PubMed:32567732, PubMed:33130824). Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription (PubMed:22567091). {ECO:0000269\|PubMed:22567091, ECO:0000269\|PubMed:25781180, ECO:0000269\|PubMed:32567732, ECO:0000269\|PubMed:33130824}.
Q9NXH8	TOR4A	S87	ochoa	Torsin-4A (Torsin family 4 member A)	None
Q9NXR1	NDE1	S231	ochoa	Nuclear distribution protein nudE homolog 1 (NudE)	Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a postmitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. Acts as a RAB9A/B effector that tethers RAB9-associated late endosomes to the dynein motor for their retrograde transport to the trans-Golgi network (PubMed:34793709). {ECO:0000269\|PubMed:17600710, ECO:0000269\|PubMed:21529752, ECO:0000269\|PubMed:34793709}.
Q9NY27	PPP4R2	S224	ochoa	Serine/threonine-protein phosphatase 4 regulatory subunit 2	Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. {ECO:0000269\|PubMed:10769191, ECO:0000269\|PubMed:12668731, ECO:0000269\|PubMed:18614045, ECO:0000269\|PubMed:20154705}.
Q9NY27	PPP4R2	S226	ochoa	Serine/threonine-protein phosphatase 4 regulatory subunit 2	Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. {ECO:0000269\|PubMed:10769191, ECO:0000269\|PubMed:12668731, ECO:0000269\|PubMed:18614045, ECO:0000269\|PubMed:20154705}.
Q9NY59	SMPD3	S186	ochoa	Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II)	Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). {ECO:0000250\|UniProtKB:O35049, ECO:0000250\|UniProtKB:Q9JJY3, ECO:0000269\|PubMed:10823942, ECO:0000269\|PubMed:14741383, ECO:0000269\|PubMed:15051724}.
Q9NY61	AATF	S61	ochoa	Protein AATF (Apoptosis-antagonizing transcription factor) (Rb-binding protein Che-1)	Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date. {ECO:0000269\|PubMed:12450794, ECO:0000269\|PubMed:12847090, ECO:0000269\|PubMed:14627703, ECO:0000269\|PubMed:15207272, ECO:0000269\|PubMed:34516797}.
Q9NYA4	MTMR4	S616	ochoa	Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4 (EC 3.1.3.95) (FYVE domain-containing dual specificity protein phosphatase 2) (FYVE-DSP2) (Myotubularin-related protein 4) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Zinc finger FYVE domain-containing protein 11)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:11302699, PubMed:16787938, PubMed:20736309, PubMed:27625994, PubMed:29962048, PubMed:30944173). Decreases the levels of phosphatidylinositol 3-phosphate, a phospholipid found in cell membranes where it acts as key regulator of both cell signaling and intracellular membrane traffic, in a subset of endosomal membranes to negatively regulate both endocytic recycling and trafficking and/or maturation of endosomes toward lysosomes (PubMed:16787938, PubMed:20736309, PubMed:29962048). Through phosphatidylinositol 3-phosphate turnover in phagosome membranes regulates phagocytosis and phagosome maturation (PubMed:31543504). By decreasing phosphatidylinositol 3-monophosphate (PI3P) levels in immune cells it can also regulate the innate immune response (PubMed:30944173). Beside its lipid phosphatase activity, can also function as a molecular adapter to regulate midbody abscission during mitotic cytokinesis (PubMed:25659891). Can also negatively regulate TGF-beta and BMP signaling through Smad proteins dephosphorylation and retention in endosomes (PubMed:20061380, PubMed:23150675). {ECO:0000269\|PubMed:11302699, ECO:0000269\|PubMed:16787938, ECO:0000269\|PubMed:20061380, ECO:0000269\|PubMed:20736309, ECO:0000269\|PubMed:23150675, ECO:0000269\|PubMed:25659891, ECO:0000269\|PubMed:27625994, ECO:0000269\|PubMed:29962048, ECO:0000269\|PubMed:30944173, ECO:0000269\|PubMed:31543504}.
Q9NYB0	TERF2IP	S36	ochoa	Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Dopamine receptor-interacting protein 5) (Repressor/activator protein 1 homolog) (RAP1 homolog) (hRap1)	Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. {ECO:0000269\|PubMed:16166375, ECO:0000269\|PubMed:19763083}.
Q9NYB9	ABI2	S233	ochoa	Abl interactor 2 (Abelson interactor 2) (Abi-2) (Abl-binding protein 3) (AblBP3) (Arg-binding protein 1) (ArgBP1)	Regulator of actin cytoskeleton dynamics underlying cell motility and adhesion. Functions as a component of the WAVE complex, which activates actin nucleating machinery Arp2/3 to drive lamellipodia formation (PubMed:21107423). Acts as a regulator and substrate of nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked to cell growth and differentiation. Positively regulates ABL1-mediated phosphorylation of ENAH, which is required for proper polymerization of nucleated actin filaments at the leading edge (PubMed:10498863, PubMed:7590236, PubMed:8649853). Contributes to the regulation of actin assembly at the tips of neuron projections. In particular, controls dendritic spine morphogenesis and may promote dendritic spine specification toward large mushroom-type spines known as repositories of memory in the brain (By similarity). In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that triggers dendrite outgrowth (By similarity). Participates in ocular lens morphogenesis, likely by regulating lamellipodia-driven adherens junction formation at the epithelial cell-secondary lens fiber interface (By similarity). Also required for nascent adherens junction assembly in epithelial cells (PubMed:15572692). {ECO:0000250\|UniProtKB:P62484, ECO:0000269\|PubMed:10498863, ECO:0000269\|PubMed:15572692, ECO:0000269\|PubMed:21107423, ECO:0000269\|PubMed:7590236, ECO:0000269\|PubMed:8649853}.
Q9NYD6	HOXC10	S210	ochoa	Homeobox protein Hox-C10 (Homeobox protein Hox-3I)	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Q9NYF8	BCLAF1	S268	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYF8	BCLAF1	S282	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYF8	BCLAF1	S502	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYF8	BCLAF1	S760	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYF8	BCLAF1	S763	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYI0	PSD3	S1020	ochoa	PH and SEC7 domain-containing protein 3 (Epididymis tissue protein Li 20mP) (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 D) (Exchange factor for ARF6 D) (Hepatocellular carcinoma-associated antigen 67) (Pleckstrin homology and SEC7 domain-containing protein 3)	Guanine nucleotide exchange factor for ARF6. {ECO:0000250}.
Q9NYL2	MAP3K20	S599	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYL2	MAP3K20	S654	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYL2	MAP3K20	S667	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYL2	MAP3K20	S691	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYL2	MAP3K20	S733	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYQ6	CELSR1	S2764	ochoa	Cadherin EGF LAG seven-pass G-type receptor 1 (Cadherin family member 9) (Flamingo homolog 2) (hFmi2)	Receptor that may have an important role in cell/cell signaling during nervous system formation.
Q9NYV4	CDK12	S257	ochoa	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q9NYV4	CDK12	S400	ochoa	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q9NZ52	GGA3	S388	ochoa	ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3)	Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif (PubMed:11301005). Mediates export of the GPCR receptor ADRA2B to the cell surface (PubMed:26811329). nvolved in BACE1 transport and sorting as well as regulation of BACE1 protein levels (PubMed:15615712, PubMed:17553422, PubMed:20484053). Regulates retrograde transport of BACE1 from endosomes to the trans-Golgi network via interaction through the VHS motif and dependent of BACE1 phosphorylation (PubMed:15615712). Modulates BACE1 protein levels independently of the interaction between VHS domain and DXXLL motif through recognition of ubiquitination (PubMed:20484053). Key player in a novel DXXLL-mediated endosomal sorting machinery to the recycling pathway that targets NTRK1 to the plasma membrane (By similarity). {ECO:0000250\|UniProtKB:A0A0G2JV04, ECO:0000269\|PubMed:11301005, ECO:0000269\|PubMed:15615712, ECO:0000269\|PubMed:17553422, ECO:0000269\|PubMed:20484053, ECO:0000269\|PubMed:26811329}.
Q9NZB2	FAM120A	S450	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZB2	FAM120A	S462	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZB2	FAM120A	S513	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZJ0	DTL	S447	ochoa	Denticleless protein homolog (DDB1- and CUL4-associated factor 2) (Lethal(2) denticleless protein homolog) (Retinoic acid-regulated nuclear matrix-associated protein)	Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). {ECO:0000269\|PubMed:16861906, ECO:0000269\|PubMed:16949367, ECO:0000269\|PubMed:16964240, ECO:0000269\|PubMed:17085480, ECO:0000269\|PubMed:18703516, ECO:0000269\|PubMed:18794347, ECO:0000269\|PubMed:18794348, ECO:0000269\|PubMed:19332548, ECO:0000269\|PubMed:20129063, ECO:0000269\|PubMed:23478441, ECO:0000269\|PubMed:23478445, ECO:0000269\|PubMed:23677613, ECO:0000269\|PubMed:26431207, ECO:0000269\|PubMed:27906959}.
Q9NZJ0	DTL	S496	ochoa	Denticleless protein homolog (DDB1- and CUL4-associated factor 2) (Lethal(2) denticleless protein homolog) (Retinoic acid-regulated nuclear matrix-associated protein)	Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). {ECO:0000269\|PubMed:16861906, ECO:0000269\|PubMed:16949367, ECO:0000269\|PubMed:16964240, ECO:0000269\|PubMed:17085480, ECO:0000269\|PubMed:18703516, ECO:0000269\|PubMed:18794347, ECO:0000269\|PubMed:18794348, ECO:0000269\|PubMed:19332548, ECO:0000269\|PubMed:20129063, ECO:0000269\|PubMed:23478441, ECO:0000269\|PubMed:23478445, ECO:0000269\|PubMed:23677613, ECO:0000269\|PubMed:26431207, ECO:0000269\|PubMed:27906959}.
Q9NZJ9	NUDT4	S154	ochoa	Diphosphoinositol polyphosphate phosphohydrolase 2 (DIPP-2) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2) (EC 3.6.1.61) (Nucleoside diphosphate-linked moiety X motif 4) (Nudix motif 4)	Cleaves the beta-phosphate from diphosphoinositol polyphosphates such as PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 (diphosphoinositol tetrakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (PubMed:10777568). Diadenosine polyphosphates, particularly Ap6A (P(1),P(6)-bis(5a-adenosyl) hexaphosphate) and Ap5A (P(1),P(5)-bis(5'-adenosyl) pentaphosphate) are downstream effectors of a signaling cascade that regulates cardiac KATP channels, can also be substrates, although with lower preference than the diphosphoinositol polyphosphates (PubMed:10777568). Can also catalyze the hydrolysis of 5-phosphoribose 1-diphosphate, generating the glycolytic activator ribose 1,5-bisphosphate (PubMed:12370170). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity). {ECO:0000250\|UniProtKB:Q8R2U6, ECO:0000269\|PubMed:10777568, ECO:0000269\|PubMed:12370170}.
Q9NZM3	ITSN2	S222	ochoa	Intersectin-2 (SH3 domain-containing protein 1B) (SH3P18) (SH3P18-like WASP-associated protein)	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:23999003}.
Q9NZM3	ITSN2	S225	ochoa	Intersectin-2 (SH3 domain-containing protein 1B) (SH3P18) (SH3P18-like WASP-associated protein)	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:23999003}.
Q9NZM3	ITSN2	S227	ochoa	Intersectin-2 (SH3 domain-containing protein 1B) (SH3P18) (SH3P18-like WASP-associated protein)	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:23999003}.
Q9NZN5	ARHGEF12	S309	ochoa	Rho guanine nucleotide exchange factor 12 (Leukemia-associated RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. {ECO:0000269\|PubMed:11094164}.
Q9NZN8	CNOT2	S69	ochoa	CCR4-NOT transcription complex subunit 2 (CCR4-associated factor 2)	Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269\|PubMed:14707134, ECO:0000269\|PubMed:16712523, ECO:0000269\|PubMed:21299754, ECO:0000269\|PubMed:22367759}.
Q9P0J7	KCMF1	S225	ochoa	E3 ubiquitin-protein ligase KCMF1 (EC 2.3.2.27) (FGF-induced in gastric cancer) (Potassium channel modulatory factor) (PCMF) (ZZ-type zinc finger-containing protein 1)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and then transfers it to targeted substrates, promoting their degradation by the proteasome (PubMed:15581609, PubMed:25582440, PubMed:34893540, PubMed:37891180, PubMed:38297121). Together with UBR4, component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (PubMed:34893540, PubMed:37891180). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:37891180). Together with UBR4, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy (PubMed:34893540). Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). {ECO:0000269\|PubMed:15581609, ECO:0000269\|PubMed:25582440, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:37891180, ECO:0000269\|PubMed:38297121}.
Q9P0K7	RAI14	S296	ochoa	Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14)	Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250\|UniProtKB:Q5U312}.
Q9P0K7	RAI14	S335	ochoa	Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14)	Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250\|UniProtKB:Q5U312}.
Q9P0U3	SENP1	S163	ochoa	Sentrin-specific protease 1 (EC 3.4.22.-) (Sentrin/SUMO-specific protease SENP1)	Protease that catalyzes two essential functions in the SUMO pathway (PubMed:10652325, PubMed:15199155, PubMed:15487983, PubMed:16253240, PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed:15487983). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:15199155, PubMed:16253240, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). Deconjugates SUMO1 from HIPK2 (PubMed:16253240). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (PubMed:15199155, PubMed:21829689). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (PubMed:23160374). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Inhibits N(6)-methyladenosine (m6A) RNA methylation by mediating SUMO1 deconjugation from METTL3 and ALKBH5: METTL3 inhibits the m6A RNA methyltransferase activity, while ALKBH5 desumoylation promotes m6A demethylation (PubMed:29506078, PubMed:34048572, PubMed:37257451). Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032). Deconjugates SUMO1 from GPS2 (PubMed:24943844). {ECO:0000269\|PubMed:10652325, ECO:0000269\|PubMed:15199155, ECO:0000269\|PubMed:15487983, ECO:0000269\|PubMed:16253240, ECO:0000269\|PubMed:16553580, ECO:0000269\|PubMed:21829689, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:23160374, ECO:0000269\|PubMed:24943844, ECO:0000269\|PubMed:25406032, ECO:0000269\|PubMed:29506078, ECO:0000269\|PubMed:34048572, ECO:0000269\|PubMed:37257451}.
Q9P107	GMIP	S459	ochoa	GEM-interacting protein (GMIP)	Stimulates, in vitro and in vivo, the GTPase activity of RhoA. {ECO:0000269\|PubMed:12093360}.
Q9P107	GMIP	S460	ochoa	GEM-interacting protein (GMIP)	Stimulates, in vitro and in vivo, the GTPase activity of RhoA. {ECO:0000269\|PubMed:12093360}.
Q9P1T7	MDFIC	S143	ochoa	MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (hIC)	Required to control the activity of various transcription factors through their sequestration in the cytoplasm. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm and inhibits their transcriptional activation (By similarity). Modulates the expression from cellular promoters. Binds to the axin complex, resulting in an increase in the level of free beta-catenin (PubMed:12192039). Affects axin regulation of the WNT and JNK signaling pathways (PubMed:12192039). Involved in the development of lymphatic vessel valves (By similarity). Required to promote lymphatic endothelial cell migration, in a process that involves down-regulation of integrin beta 1 activation and control of cell adhesion to the extracellular matrix (PubMed:35235341). Regulates the activity of mechanosensitive Piezo channel (PubMed:37590348). {ECO:0000250\|UniProtKB:Q8BX65, ECO:0000269\|PubMed:12192039, ECO:0000269\|PubMed:35235341, ECO:0000269\|PubMed:37590348}.; FUNCTION: (Microbial infection) Modulates the expression from viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta (PubMed:12944466, PubMed:16260749, Ref.6). Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR (PubMed:10671520). {ECO:0000269\|PubMed:10671520, ECO:0000269\|PubMed:12944466, ECO:0000269\|PubMed:16260749, ECO:0000269\|Ref.6}.
Q9P1T7	MDFIC	S146	ochoa	MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (hIC)	Required to control the activity of various transcription factors through their sequestration in the cytoplasm. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm and inhibits their transcriptional activation (By similarity). Modulates the expression from cellular promoters. Binds to the axin complex, resulting in an increase in the level of free beta-catenin (PubMed:12192039). Affects axin regulation of the WNT and JNK signaling pathways (PubMed:12192039). Involved in the development of lymphatic vessel valves (By similarity). Required to promote lymphatic endothelial cell migration, in a process that involves down-regulation of integrin beta 1 activation and control of cell adhesion to the extracellular matrix (PubMed:35235341). Regulates the activity of mechanosensitive Piezo channel (PubMed:37590348). {ECO:0000250\|UniProtKB:Q8BX65, ECO:0000269\|PubMed:12192039, ECO:0000269\|PubMed:35235341, ECO:0000269\|PubMed:37590348}.; FUNCTION: (Microbial infection) Modulates the expression from viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta (PubMed:12944466, PubMed:16260749, Ref.6). Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR (PubMed:10671520). {ECO:0000269\|PubMed:10671520, ECO:0000269\|PubMed:12944466, ECO:0000269\|PubMed:16260749, ECO:0000269\|Ref.6}.
Q9P1Y5	CAMSAP3	S560	ochoa	Calmodulin-regulated spectrin-associated protein 3 (Protein Nezha)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742, PubMed:27802168). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). {ECO:0000250\|UniProtKB:Q80VC9, ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:26715742, ECO:0000269\|PubMed:27693509, ECO:0000269\|PubMed:27802168, ECO:0000269\|PubMed:28089391, ECO:0000269\|PubMed:28386021}.
Q9P1Y5	CAMSAP3	S1080	ochoa	Calmodulin-regulated spectrin-associated protein 3 (Protein Nezha)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742, PubMed:27802168). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). {ECO:0000250\|UniProtKB:Q80VC9, ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:26715742, ECO:0000269\|PubMed:27693509, ECO:0000269\|PubMed:27802168, ECO:0000269\|PubMed:28089391, ECO:0000269\|PubMed:28386021}.
Q9P1Y6	PHRF1	S107	ochoa	PHD and RING finger domain-containing protein 1	None
Q9P206	NHSL3	S325	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S333	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S526	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S568	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S579	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S868	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P242	NYAP2	S475	ochoa	Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 2	Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000250}.
Q9P246	STIM2	S609	ochoa	Stromal interaction molecule 2	Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx. {ECO:0000269\|PubMed:16005298, ECO:0000269\|PubMed:16860747, ECO:0000269\|PubMed:17905723, ECO:0000269\|PubMed:18160041, ECO:0000269\|PubMed:21217057, ECO:0000269\|PubMed:22464749, ECO:0000269\|PubMed:23359669}.
Q9P258	RCC2	S50	ochoa	Protein RCC2 (RCC1-like protein TD-60) (Telophase disk protein of 60 kDa)	Multifunctional protein that may affect its functions by regulating the activity of small GTPases, such as RAC1 and RALA (PubMed:12919680, PubMed:25074804, PubMed:26158537, PubMed:28869598). Required for normal progress through the cell cycle, both during interphase and during mitosis (PubMed:12919680, PubMed:23388455, PubMed:26158537). Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles (PubMed:12919680, PubMed:26158537). Required for normal organization of the microtubule cytoskeleton in interphase cells (PubMed:23388455). Functions as guanine nucleotide exchange factor (GEF) for RALA (PubMed:26158537). Interferes with the activation of RAC1 by guanine nucleotide exchange factors (PubMed:25074804). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions (PubMed:25074804, PubMed:28869598). Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (PubMed:25074804, PubMed:28869598). {ECO:0000269\|PubMed:12919680, ECO:0000269\|PubMed:23388455, ECO:0000269\|PubMed:25074804, ECO:0000269\|PubMed:26158537, ECO:0000269\|PubMed:28869598}.
Q9P258	RCC2	S51	ochoa	Protein RCC2 (RCC1-like protein TD-60) (Telophase disk protein of 60 kDa)	Multifunctional protein that may affect its functions by regulating the activity of small GTPases, such as RAC1 and RALA (PubMed:12919680, PubMed:25074804, PubMed:26158537, PubMed:28869598). Required for normal progress through the cell cycle, both during interphase and during mitosis (PubMed:12919680, PubMed:23388455, PubMed:26158537). Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles (PubMed:12919680, PubMed:26158537). Required for normal organization of the microtubule cytoskeleton in interphase cells (PubMed:23388455). Functions as guanine nucleotide exchange factor (GEF) for RALA (PubMed:26158537). Interferes with the activation of RAC1 by guanine nucleotide exchange factors (PubMed:25074804). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions (PubMed:25074804, PubMed:28869598). Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (PubMed:25074804, PubMed:28869598). {ECO:0000269\|PubMed:12919680, ECO:0000269\|PubMed:23388455, ECO:0000269\|PubMed:25074804, ECO:0000269\|PubMed:26158537, ECO:0000269\|PubMed:28869598}.
Q9P260	RELCH	S186	ochoa	RAB11-binding protein RELCH (LisH domain and HEAT repeat-containing protein KIAA1468) (RAB11 binding and LisH domain, coiled-coil and HEAT repeat-containing) (RAB11-binding protein containing LisH, coiled-coil, and HEAT repeats)	Regulates intracellular cholesterol distribution from recycling endosomes to the trans-Golgi network through interactions with RAB11 and OSBP (PubMed:29514919). Functions in membrane tethering and promotes OSBP-mediated cholesterol transfer between RAB11-bound recycling endosomes and OSBP-bound Golgi-like membranes (PubMed:29514919). {ECO:0000269\|PubMed:29514919}.
Q9P270	SLAIN2	S240	ochoa	SLAIN motif-containing protein 2	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269\|PubMed:21646404}.
Q9P270	SLAIN2	S257	ochoa	SLAIN motif-containing protein 2	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269\|PubMed:21646404}.
Q9P270	SLAIN2	S265	ochoa	SLAIN motif-containing protein 2	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269\|PubMed:21646404}.
Q9P275	USP36	S620	ochoa	Ubiquitin carboxyl-terminal hydrolase 36 (EC 2.3.2.-) (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)	Deubiquitinase essential for the regulation of nucleolar structure and function (PubMed:19208757, PubMed:22902402, PubMed:29273634). Required for cell and organism viability (PubMed:19208757, PubMed:22902402, PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:19208757, PubMed:22902402, PubMed:29273634, PubMed:36912080). Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (PubMed:29274341). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (PubMed:25775507). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (PubMed:25775507). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (PubMed:27445338). Deubiquitinates SOD2, regulates SOD2 protein stability (PubMed:21268071). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (PubMed:22622177). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (PubMed:35989368). Acts as a SUMO ligase to promote EXOSC10 sumoylation critical for the nucleolar RNA exosome function in rRNA processing (PubMed:36912080). Binds to pre-rRNAs (PubMed:36912080). {ECO:0000269\|PubMed:19208757, ECO:0000269\|PubMed:21268071, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:22902402, ECO:0000269\|PubMed:25775507, ECO:0000269\|PubMed:27445338, ECO:0000269\|PubMed:29273634, ECO:0000269\|PubMed:29274341, ECO:0000269\|PubMed:35989368, ECO:0000269\|PubMed:36912080}.
Q9P275	USP36	S646	ochoa	Ubiquitin carboxyl-terminal hydrolase 36 (EC 2.3.2.-) (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)	Deubiquitinase essential for the regulation of nucleolar structure and function (PubMed:19208757, PubMed:22902402, PubMed:29273634). Required for cell and organism viability (PubMed:19208757, PubMed:22902402, PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:19208757, PubMed:22902402, PubMed:29273634, PubMed:36912080). Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (PubMed:29274341). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (PubMed:25775507). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (PubMed:25775507). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (PubMed:27445338). Deubiquitinates SOD2, regulates SOD2 protein stability (PubMed:21268071). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (PubMed:22622177). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (PubMed:35989368). Acts as a SUMO ligase to promote EXOSC10 sumoylation critical for the nucleolar RNA exosome function in rRNA processing (PubMed:36912080). Binds to pre-rRNAs (PubMed:36912080). {ECO:0000269\|PubMed:19208757, ECO:0000269\|PubMed:21268071, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:22902402, ECO:0000269\|PubMed:25775507, ECO:0000269\|PubMed:27445338, ECO:0000269\|PubMed:29273634, ECO:0000269\|PubMed:29274341, ECO:0000269\|PubMed:35989368, ECO:0000269\|PubMed:36912080}.
Q9P2D0	IBTK	S1045	ochoa	Inhibitor of Bruton tyrosine kinase (IBtk)	Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription. {ECO:0000269\|PubMed:11577348}.
Q9P2Q2	FRMD4A	S371	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S372	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S374	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S377	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S657	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S673	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	S955	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2Q2	FRMD4A	Y959	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9P2R6	RERE	S600	ochoa	Arginine-glutamic acid dipeptide repeats protein (Atrophin-1-like protein) (Atrophin-1-related protein)	Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death. {ECO:0000269\|PubMed:11331249}.
Q9UBC2	EPS15L1	S235	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S244	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S247	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S253	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S377	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S713	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S718	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBW5	BIN2	S288	ochoa	Bridging integrator 2 (Breast cancer-associated protein 1)	Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis. {ECO:0000269\|PubMed:23285027}.
Q9UBW5	BIN2	S375	ochoa	Bridging integrator 2 (Breast cancer-associated protein 1)	Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis. {ECO:0000269\|PubMed:23285027}.
Q9UBY5	LPAR3	S331	ochoa	Lysophosphatidic acid receptor 3 (LPA receptor 3) (LPA-3) (Lysophosphatidic acid receptor Edg-7)	Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins.
Q9UD71	PPP1R1B	S52	ochoa	Protein phosphatase 1 regulatory subunit 1B (DARPP-32) (Dopamine- and cAMP-regulated neuronal phosphoprotein)	Inhibitor of protein-phosphatase 1.
Q9UDT6	CLIP2	S30	ochoa	CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2) (Williams-Beuren syndrome chromosomal region 3 protein) (Williams-Beuren syndrome chromosomal region 4 protein)	Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}.
Q9UDY2	TJP2	S430	ochoa	Tight junction protein 2 (Tight junction protein ZO-2) (Zona occludens protein 2) (Zonula occludens protein 2)	Plays a role in tight junctions and adherens junctions (By similarity). Acts as a positive regulator of RANKL-induced osteoclast differentiation, potentially via mediating downstream transcriptional activity (By similarity). {ECO:0000250\|UniProtKB:Q9Z0U1}.
Q9UER7	DAXX	S184	psp	Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269\|PubMed:12140263, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:15364927, ECO:0000269\|PubMed:16845383, ECO:0000269\|PubMed:17081986, ECO:0000269\|PubMed:17942542, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:23222847, ECO:0000269\|PubMed:24200965, ECO:0000269\|PubMed:24530302}.
Q9UER7	DAXX	S618	ochoa	Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269\|PubMed:12140263, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:15364927, ECO:0000269\|PubMed:16845383, ECO:0000269\|PubMed:17081986, ECO:0000269\|PubMed:17942542, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:23222847, ECO:0000269\|PubMed:24200965, ECO:0000269\|PubMed:24530302}.
Q9UER7	DAXX	S688	ochoa	Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269\|PubMed:12140263, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:15364927, ECO:0000269\|PubMed:16845383, ECO:0000269\|PubMed:17081986, ECO:0000269\|PubMed:17942542, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:23222847, ECO:0000269\|PubMed:24200965, ECO:0000269\|PubMed:24530302}.
Q9UER7	DAXX	S696	ochoa	Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269\|PubMed:12140263, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:15364927, ECO:0000269\|PubMed:16845383, ECO:0000269\|PubMed:17081986, ECO:0000269\|PubMed:17942542, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:23222847, ECO:0000269\|PubMed:24200965, ECO:0000269\|PubMed:24530302}.
Q9UFC0	LRWD1	S251	ochoa	Leucine-rich repeat and WD repeat-containing protein 1 (Centromere protein 33) (CENP-33) (Origin recognition complex-associated protein) (ORC-associated protein) (ORCA)	Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. {ECO:0000269\|PubMed:20850016, ECO:0000269\|PubMed:20932478, ECO:0000269\|PubMed:21029866, ECO:0000269\|PubMed:22427655, ECO:0000269\|PubMed:22645314}.
Q9UFC0	LRWD1	S259	ochoa	Leucine-rich repeat and WD repeat-containing protein 1 (Centromere protein 33) (CENP-33) (Origin recognition complex-associated protein) (ORC-associated protein) (ORCA)	Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. {ECO:0000269\|PubMed:20850016, ECO:0000269\|PubMed:20932478, ECO:0000269\|PubMed:21029866, ECO:0000269\|PubMed:22427655, ECO:0000269\|PubMed:22645314}.
Q9UGP4	LIMD1	S239	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UGP4	LIMD1	S304	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UGP4	LIMD1	S353	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UGU0	TCF20	S544	ochoa	Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Protein AR1) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein)	Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. {ECO:0000269\|PubMed:10995766}.
Q9UGU0	TCF20	S871	ochoa	Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Protein AR1) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein)	Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. {ECO:0000269\|PubMed:10995766}.
Q9UGU0	TCF20	S1675	ochoa	Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Protein AR1) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein)	Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. {ECO:0000269\|PubMed:10995766}.
Q9UGV2	NDRG3	S341	ochoa	Protein NDRG3 (N-myc downstream-regulated gene 3 protein)	None
Q9UGV2	NDRG3	S352	ochoa	Protein NDRG3 (N-myc downstream-regulated gene 3 protein)	None
Q9UH99	SUN2	S38	ochoa	SUN domain-containing protein 2 (Protein unc-84 homolog B) (Rab5-interacting protein) (Rab5IP) (Sad1/unc-84 protein-like 2)	As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000250\|UniProtKB:Q8BJS4, ECO:0000269\|PubMed:18396275, ECO:0000305}.
Q9UH99	SUN2	S116	ochoa\|psp	SUN domain-containing protein 2 (Protein unc-84 homolog B) (Rab5-interacting protein) (Rab5IP) (Sad1/unc-84 protein-like 2)	As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000250\|UniProtKB:Q8BJS4, ECO:0000269\|PubMed:18396275, ECO:0000305}.
Q9UHB6	LIMA1	S374	ochoa\|psp	LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)	Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250\|UniProtKB:Q9ERG0, ECO:0000269\|PubMed:12566430, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:33999101}.
Q9UHB6	LIMA1	S704	ochoa	LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)	Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250\|UniProtKB:Q9ERG0, ECO:0000269\|PubMed:12566430, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:33999101}.
Q9UHB7	AFF4	S161	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UHB7	AFF4	S555	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UHB7	AFF4	S686	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UHG3	PCYOX1	S177	ochoa	Prenylcysteine oxidase 1 (EC 1.8.3.5) (Prenylcysteine lyase)	Prenylcysteine oxidase that cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (PubMed:10585463, PubMed:11078725, PubMed:12186880). Only active against free prenylcysteines and not prenylcysteine residues within prenylated proteins or peptides (By similarity). Involved in the final step in the degradation of prenylated proteins, by degrading prenylcysteines after the protein has been degraded (PubMed:10585463). {ECO:0000250\|UniProtKB:F1N2K1, ECO:0000269\|PubMed:10585463, ECO:0000269\|PubMed:11078725, ECO:0000269\|PubMed:12186880}.
Q9UHR4	BAIAP2L1	S261	ochoa	BAR/IMD domain-containing adapter protein 2-like 1 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1) (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate)	May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269\|PubMed:17430976, ECO:0000269\|PubMed:19366662, ECO:0000269\|PubMed:22921828}.
Q9UHR4	BAIAP2L1	S420	ochoa	BAR/IMD domain-containing adapter protein 2-like 1 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1) (BAI1-associated protein 2-like protein 1) (Insulin receptor tyrosine kinase substrate)	May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269\|PubMed:17430976, ECO:0000269\|PubMed:19366662, ECO:0000269\|PubMed:22921828}.
Q9UHY1	NRBP1	S428	ochoa	Nuclear receptor-binding protein	Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication (PubMed:15084397). {ECO:0000250\|UniProtKB:Q99J45, ECO:0000269\|PubMed:11956649, ECO:0000269\|PubMed:15084397}.
Q9UI08	EVL	S337	ochoa	Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
Q9UIF9	BAZ2A	S1376	ochoa	Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5) (hWALp3)	Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (By similarity). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By similarity). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity). {ECO:0000250\|UniProtKB:Q91YE5, ECO:0000269\|PubMed:28801535}.
Q9UIG0	BAZ1B	S167	ochoa	Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor) (Williams-Beuren syndrome chromosomal region 10 protein) (Williams-Beuren syndrome chromosomal region 9 protein) (hWALp2)	Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator (PubMed:19092802). Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph) (PubMed:19092802, PubMed:19234442). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19092802, PubMed:19234442). Regulatory subunit of the ATP-dependent WICH-1 and WICH-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:11980720, PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The WICH-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the WICH-5 ISWI chromatin remodeling complex (PubMed:28801535). The WICH-5 ISWI chromatin-remodeling complex regulates the transcription of various genes, has a role in RNA polymerase I transcription (By similarity). Within the B-WICH complex has a role in RNA polymerase III transcription (PubMed:16603771). Mediates the recruitment of the WICH-5 ISWI chromatin remodeling complex to replication foci during DNA replication (PubMed:15543136). {ECO:0000250\|UniProtKB:Q9Z277, ECO:0000269\|PubMed:11980720, ECO:0000269\|PubMed:15543136, ECO:0000269\|PubMed:16603771, ECO:0000269\|PubMed:19092802, ECO:0000269\|PubMed:19234442, ECO:0000269\|PubMed:28801535}.
Q9UIQ6	LNPEP	S91	ochoa	Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (Insulin-regulated membrane aminopeptidase) (Insulin-responsive aminopeptidase) (IRAP) (Oxytocinase) (OTase) (Placental leucine aminopeptidase) (P-LAP) [Cleaved into: Leucyl-cystinyl aminopeptidase, pregnancy serum form]	Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. {ECO:0000269\|PubMed:11389728, ECO:0000269\|PubMed:11707427, ECO:0000269\|PubMed:1731608}.
Q9UIW2	PLXNA1	S1619	ochoa	Plexin-A1 (Semaphorin receptor NOV)	Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. Acts as coreceptor of TREM2 for SEMA6D in dendritic cells and is involved in the generation of immune responses and skeletal homeostasis. {ECO:0000250\|UniProtKB:P70206}.
Q9UJA3	MCM8	S636	ochoa	DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8)	Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (PubMed:26215093). Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:23401855). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:23401855). However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC) (PubMed:15684404). Probably by regulating HR, plays a key role during gametogenesis (By similarity). Stabilizes MCM9 protein (PubMed:23401855, PubMed:26215093). {ECO:0000250\|UniProtKB:Q9CWV1, ECO:0000269\|PubMed:15684404, ECO:0000269\|PubMed:23401855, ECO:0000269\|PubMed:26215093}.
Q9UJF2	RASAL2	S95	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9UJF2	RASAL2	S641	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9UJF2	RASAL2	S893	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9UJM3	ERRFI1	S340	ochoa	ERBB receptor feedback inhibitor 1 (Mitogen-inducible gene 6 protein) (MIG-6)	Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity). {ECO:0000250}.
Q9UJU6	DBNL	S275	ochoa	Drebrin-like protein (Cervical SH3P7) (Cervical mucin-associated protein) (Drebrin-F) (HPK1-interacting protein of 55 kDa) (HIP-55) (SH3 domain-containing protein 7)	Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. {ECO:0000250, ECO:0000269\|PubMed:14729663}.
Q9UJZ1	STOML2	S336	ochoa	Stomatin-like protein 2, mitochondrial (SLP-2) (EPB72-like protein 2) (Paraprotein target 7) (Paratarg-7)	Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. {ECO:0000269\|PubMed:17121834, ECO:0000269\|PubMed:18641330, ECO:0000269\|PubMed:19597348, ECO:0000269\|PubMed:19944461, ECO:0000269\|PubMed:21746876, ECO:0000269\|PubMed:22623988}.
Q9UK32	RPS6KA6	S378	ochoa	Ribosomal protein S6 kinase alpha-6 (S6K-alpha-6) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 6) (p90-RSK 6) (p90RSK6) (Ribosomal S6 kinase 4) (RSK-4) (pp90RSK4)	Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. {ECO:0000269\|PubMed:15042092, ECO:0000269\|PubMed:15632195}.
Q9UK61	TASOR	S1113	ochoa	Protein TASOR (CTCL tumor antigen se89-1) (Retinoblastoma-associated protein RAP140) (Transgene activation suppressor protein)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Plays a crucial role in early embryonic development (By similarity). Involved in the organization of spindle poles and spindle apparatus assembly during zygotic division (By similarity). Plays an important role in maintaining epiblast fitness or potency (By similarity). {ECO:0000250\|UniProtKB:Q69ZR9, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:28581500, ECO:0000269\|PubMed:29211708, ECO:0000269\|PubMed:30487602}.
Q9UK61	TASOR	S1206	ochoa	Protein TASOR (CTCL tumor antigen se89-1) (Retinoblastoma-associated protein RAP140) (Transgene activation suppressor protein)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Plays a crucial role in early embryonic development (By similarity). Involved in the organization of spindle poles and spindle apparatus assembly during zygotic division (By similarity). Plays an important role in maintaining epiblast fitness or potency (By similarity). {ECO:0000250\|UniProtKB:Q69ZR9, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:28581500, ECO:0000269\|PubMed:29211708, ECO:0000269\|PubMed:30487602}.
Q9UK61	TASOR	S1558	ochoa	Protein TASOR (CTCL tumor antigen se89-1) (Retinoblastoma-associated protein RAP140) (Transgene activation suppressor protein)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Plays a crucial role in early embryonic development (By similarity). Involved in the organization of spindle poles and spindle apparatus assembly during zygotic division (By similarity). Plays an important role in maintaining epiblast fitness or potency (By similarity). {ECO:0000250\|UniProtKB:Q69ZR9, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:28581500, ECO:0000269\|PubMed:29211708, ECO:0000269\|PubMed:30487602}.
Q9UKE5	TNIK	S707	ochoa	TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)	Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269\|PubMed:10521462, ECO:0000269\|PubMed:15342639, ECO:0000269\|PubMed:19061864, ECO:0000269\|PubMed:19816403, ECO:0000269\|PubMed:20159449, ECO:0000269\|PubMed:21690388, ECO:0000269\|PubMed:26437443}.
Q9UKE5	TNIK	S733	ochoa	TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)	Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269\|PubMed:10521462, ECO:0000269\|PubMed:15342639, ECO:0000269\|PubMed:19061864, ECO:0000269\|PubMed:19816403, ECO:0000269\|PubMed:20159449, ECO:0000269\|PubMed:21690388, ECO:0000269\|PubMed:26437443}.
Q9UKI8	TLK1	S80	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S88	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S100	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S103	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S176	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S182	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKV3	ACIN1	S667	ochoa	Apoptotic chromatin condensation inducer in the nucleus (Acinus)	Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269\|PubMed:10490026, ECO:0000269\|PubMed:12665594, ECO:0000269\|PubMed:18559500, ECO:0000269\|PubMed:22203037, ECO:0000269\|PubMed:22388736}.
Q9UKV3	ACIN1	S987	ochoa	Apoptotic chromatin condensation inducer in the nucleus (Acinus)	Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269\|PubMed:10490026, ECO:0000269\|PubMed:12665594, ECO:0000269\|PubMed:18559500, ECO:0000269\|PubMed:22203037, ECO:0000269\|PubMed:22388736}.
Q9UKV8	AGO2	S834	psp	Protein argonaute-2 (Argonaute2) (hAgo2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (PAZ Piwi domain protein) (PPD) (Protein slicer)	Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. {ECO:0000250\|UniProtKB:Q8CJG0, ECO:0000255\|HAMAP-Rule:MF_03031, ECO:0000269\|PubMed:15105377, ECO:0000269\|PubMed:15260970, ECO:0000269\|PubMed:15284456, ECO:0000269\|PubMed:15337849, ECO:0000269\|PubMed:15800637, ECO:0000269\|PubMed:16081698, ECO:0000269\|PubMed:16142218, ECO:0000269\|PubMed:16271387, ECO:0000269\|PubMed:16289642, ECO:0000269\|PubMed:16357216, ECO:0000269\|PubMed:16756390, ECO:0000269\|PubMed:16936728, ECO:0000269\|PubMed:17382880, ECO:0000269\|PubMed:17507929, ECO:0000269\|PubMed:17524464, ECO:0000269\|PubMed:17531811, ECO:0000269\|PubMed:17932509, ECO:0000269\|PubMed:18048652, ECO:0000269\|PubMed:18178619, ECO:0000269\|PubMed:18690212, ECO:0000269\|PubMed:18771919, ECO:0000269\|PubMed:19167051, ECO:0000269\|PubMed:23746446, ECO:0000269\|PubMed:37328606}.; FUNCTION: (Microbial infection) Upon Sars-CoV-2 infection, associates with viral miRNA-like small RNA, CoV2-miR-O7a, and may repress mRNAs, such as BATF2, to evade the IFN response. {ECO:0000269\|PubMed:34903581}.
Q9UKX7	NUP50	S227	ochoa	Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50)	Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:20016008). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (PubMed:20016008). Interacts with regulatory proteins of cell cycle progression including CDKN1B (By similarity). This interaction is required for correct intracellular transport and degradation of CDKN1B (By similarity). {ECO:0000250\|UniProtKB:Q9JIH2, ECO:0000269\|PubMed:20016008}.
Q9UKY7	CDV3	S197	ochoa	Protein CDV3 homolog	None
Q9ULC3	RAB23	S206	ochoa	Ras-related protein Rab-23 (EC 3.6.5.2)	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes. {ECO:0000269\|PubMed:22365972, ECO:0000269\|PubMed:22452336}.
Q9ULC8	ZDHHC8	S343	ochoa	Palmitoyltransferase ZDHHC8 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 8) (DHHC-8) (Zinc finger protein 378)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and therefore functions in several unrelated biological processes (Probable). Through the palmitoylation of ABCA1 regulates the localization of the transporter to the plasma membrane and thereby regulates its function in cholesterol and phospholipid efflux (Probable). Could also pamitoylate the D(2) dopamine receptor DRD2 and regulate its stability and localization to the plasma membrane (Probable). Could also play a role in glutamatergic transmission (By similarity). {ECO:0000250\|UniProtKB:Q5Y5T5, ECO:0000305\|PubMed:19556522, ECO:0000305\|PubMed:23034182, ECO:0000305\|PubMed:26535572}.; FUNCTION: (Microbial infection) Able to palmitoylate SARS coronavirus-2/SARS-CoV-2 spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell. {ECO:0000269\|PubMed:34599882}.
Q9ULG1	INO80	S1495	ochoa	Chromatin-remodeling ATPase INO80 (hINO80) (EC 3.6.4.-) (DNA helicase-related INO80 complex homolog 1) (DNA helicase-related protein INO80) (INO80 complex subunit A)	ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair (PubMed:16230350, PubMed:16298340, PubMed:17721549, PubMed:20237820, PubMed:20855601). Binds DNA (PubMed:16298340, PubMed:21303910). As part of the INO80 complex, remodels chromatin by shifting nucleosomes (PubMed:16230350, PubMed:21303910). Regulates transcription upon recruitment by YY1 to YY1-activated genes, where it acts as an essential coactivator (PubMed:17721549). Involved in UV-damage excision DNA repair (PubMed:20855601). The contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation (PubMed:20687897). Involved in DNA replication (PubMed:20237820). Required for microtubule assembly during mitosis thereby regulating chromosome segregation cycle (PubMed:20237820). {ECO:0000269\|PubMed:16230350, ECO:0000269\|PubMed:16298340, ECO:0000269\|PubMed:17721549, ECO:0000269\|PubMed:20237820, ECO:0000269\|PubMed:20687897, ECO:0000269\|PubMed:20855601, ECO:0000269\|PubMed:21303910}.
Q9ULH0	KIDINS220	S1365	ochoa	Kinase D-interacting substrate of 220 kDa (Ankyrin repeat-rich membrane-spanning protein)	Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269\|PubMed:18089783}.
Q9ULH1	ASAP1	S744	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879). {ECO:0000250, ECO:0000269\|PubMed:20393563, ECO:0000269\|PubMed:25673879}.
Q9ULH1	ASAP1	S823	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879). {ECO:0000250, ECO:0000269\|PubMed:20393563, ECO:0000269\|PubMed:25673879}.
Q9ULJ3	ZBTB21	S328	ochoa	Zinc finger and BTB domain-containing protein 21 (Zinc finger protein 295)	Acts as a transcription repressor. {ECO:0000269\|PubMed:15629158}.
Q9ULJ3	ZBTB21	S415	ochoa	Zinc finger and BTB domain-containing protein 21 (Zinc finger protein 295)	Acts as a transcription repressor. {ECO:0000269\|PubMed:15629158}.
Q9ULK2	ATXN7L1	S843	ochoa	Ataxin-7-like protein 1 (Ataxin-7-like protein 4)	None
Q9ULL1	PLEKHG1	S1192	ochoa	Pleckstrin homology domain-containing family G member 1	None
Q9ULM3	YEATS2	S124	ochoa	YEATS domain-containing protein 2	Chromatin reader component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (PubMed:18838386, PubMed:19103755, PubMed:27103431). YEATS2 specifically recognizes and binds histone H3 crotonylated at 'Lys-27' (H3K27cr) (PubMed:27103431). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:27103431). {ECO:0000269\|PubMed:18838386, ECO:0000269\|PubMed:19103755, ECO:0000269\|PubMed:27103431}.
Q9ULM3	YEATS2	S471	ochoa	YEATS domain-containing protein 2	Chromatin reader component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (PubMed:18838386, PubMed:19103755, PubMed:27103431). YEATS2 specifically recognizes and binds histone H3 crotonylated at 'Lys-27' (H3K27cr) (PubMed:27103431). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:27103431). {ECO:0000269\|PubMed:18838386, ECO:0000269\|PubMed:19103755, ECO:0000269\|PubMed:27103431}.
Q9ULT8	HECTD1	S1390	ochoa	E3 ubiquitin-protein ligase HECTD1 (EC 2.3.2.26) (E3 ligase for inhibin receptor) (EULIR) (HECT domain-containing protein 1)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:33711283). Mediates 'Lys-63'-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion (By similarity). Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells may impair their emigration and may be essential for the correct development of the cranial neural folds and neural tube closure (By similarity). Catalyzes ubiquitination and degradation of ZNF622, an assembly factor for the ribosomal 60S subunit, in hematopoietic cells, thereby promoting hematopoietic stem cell renewal (PubMed:33711283). {ECO:0000250\|UniProtKB:Q69ZR2, ECO:0000269\|PubMed:33711283}.
Q9ULT8	HECTD1	S1517	ochoa	E3 ubiquitin-protein ligase HECTD1 (EC 2.3.2.26) (E3 ligase for inhibin receptor) (EULIR) (HECT domain-containing protein 1)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:33711283). Mediates 'Lys-63'-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion (By similarity). Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells may impair their emigration and may be essential for the correct development of the cranial neural folds and neural tube closure (By similarity). Catalyzes ubiquitination and degradation of ZNF622, an assembly factor for the ribosomal 60S subunit, in hematopoietic cells, thereby promoting hematopoietic stem cell renewal (PubMed:33711283). {ECO:0000250\|UniProtKB:Q69ZR2, ECO:0000269\|PubMed:33711283}.
Q9ULU4	ZMYND8	S438	ochoa	MYND-type zinc finger-containing chromatin reader ZMYND8 (Cutaneous T-cell lymphoma-associated antigen se14-3) (CTCL-associated antigen se14-3) (Protein kinase C-binding protein 1) (Rack7) (Transcription coregulator ZMYND8) (Zinc finger MYND domain-containing protein 8)	Chromatin reader that recognizes dual histone modifications such as histone H3.1 dimethylated at 'Lys-36' and histone H4 acetylated at 'Lys-16' (H3.1K36me2-H4K16ac) and histone H3 methylated at 'Lys-4' and histone H4 acetylated at 'Lys-14' (H3K4me1-H3K14ac) (PubMed:26655721, PubMed:27477906, PubMed:31965980, PubMed:36064715). May act as a transcriptional corepressor for KDM5D by recognizing the dual histone signature H3K4me1-H3K14ac (PubMed:27477906). May also act as a transcriptional corepressor for KDM5C and EZH2 (PubMed:33323928). Recognizes acetylated histone H4 and recruits the NuRD chromatin remodeling complex to damaged chromatin for transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309, PubMed:27732854, PubMed:30134174). Also activates transcription elongation by RNA polymerase II through recruiting the P-TEFb complex to target promoters (PubMed:26655721, PubMed:30134174). Localizes to H3.1K36me2-H4K16ac marks at all-trans-retinoic acid (ATRA)-responsive genes and positively regulates their expression (PubMed:26655721). Promotes neuronal differentiation by associating with regulatory regions within the MAPT gene, to enhance transcription of a protein-coding MAPT isoform and suppress the non-coding MAPT213 isoform (PubMed:30134174, PubMed:35916866, PubMed:36064715). Suppresses breast cancer, and prostate cancer cell invasion and metastasis (PubMed:27477906, PubMed:31965980, PubMed:33323928). {ECO:0000269\|PubMed:25593309, ECO:0000269\|PubMed:26655721, ECO:0000269\|PubMed:27477906, ECO:0000269\|PubMed:27732854, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:31965980, ECO:0000269\|PubMed:33323928, ECO:0000269\|PubMed:35916866, ECO:0000269\|PubMed:36064715}.
Q9ULU4	ZMYND8	S478	ochoa	MYND-type zinc finger-containing chromatin reader ZMYND8 (Cutaneous T-cell lymphoma-associated antigen se14-3) (CTCL-associated antigen se14-3) (Protein kinase C-binding protein 1) (Rack7) (Transcription coregulator ZMYND8) (Zinc finger MYND domain-containing protein 8)	Chromatin reader that recognizes dual histone modifications such as histone H3.1 dimethylated at 'Lys-36' and histone H4 acetylated at 'Lys-16' (H3.1K36me2-H4K16ac) and histone H3 methylated at 'Lys-4' and histone H4 acetylated at 'Lys-14' (H3K4me1-H3K14ac) (PubMed:26655721, PubMed:27477906, PubMed:31965980, PubMed:36064715). May act as a transcriptional corepressor for KDM5D by recognizing the dual histone signature H3K4me1-H3K14ac (PubMed:27477906). May also act as a transcriptional corepressor for KDM5C and EZH2 (PubMed:33323928). Recognizes acetylated histone H4 and recruits the NuRD chromatin remodeling complex to damaged chromatin for transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309, PubMed:27732854, PubMed:30134174). Also activates transcription elongation by RNA polymerase II through recruiting the P-TEFb complex to target promoters (PubMed:26655721, PubMed:30134174). Localizes to H3.1K36me2-H4K16ac marks at all-trans-retinoic acid (ATRA)-responsive genes and positively regulates their expression (PubMed:26655721). Promotes neuronal differentiation by associating with regulatory regions within the MAPT gene, to enhance transcription of a protein-coding MAPT isoform and suppress the non-coding MAPT213 isoform (PubMed:30134174, PubMed:35916866, PubMed:36064715). Suppresses breast cancer, and prostate cancer cell invasion and metastasis (PubMed:27477906, PubMed:31965980, PubMed:33323928). {ECO:0000269\|PubMed:25593309, ECO:0000269\|PubMed:26655721, ECO:0000269\|PubMed:27477906, ECO:0000269\|PubMed:27732854, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:31965980, ECO:0000269\|PubMed:33323928, ECO:0000269\|PubMed:35916866, ECO:0000269\|PubMed:36064715}.
Q9ULV3	CIZ1	S584	ochoa	Cip1-interacting zinc finger protein (CDKN1A-interacting zinc finger protein 1) (Nuclear protein NP94) (Zinc finger protein 356)	May regulate the subcellular localization of CIP/WAF1.
Q9UMD9	COL17A1	S62	ochoa	Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen (120 kDa linear IgA dermatosis antigen) (Linear IgA disease antigen 1) (LAD-1); 97 kDa linear IgA disease antigen (97 kDa linear IgA bullous dermatosis antigen) (97 kDa LAD antigen) (97-LAD) (Linear IgA bullous disease antigen of 97 kDa) (LABD97)]	May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; FUNCTION: The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies.
Q9UMD9	COL17A1	S67	ochoa	Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen (120 kDa linear IgA dermatosis antigen) (Linear IgA disease antigen 1) (LAD-1); 97 kDa linear IgA disease antigen (97 kDa linear IgA bullous dermatosis antigen) (97 kDa LAD antigen) (97-LAD) (Linear IgA bullous disease antigen of 97 kDa) (LABD97)]	May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; FUNCTION: The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies.
Q9UMN6	KMT2B	S1893	ochoa	Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.364) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17707229, PubMed:25561738). Likely plays a redundant role with KMT2C in enriching H3K4me1 marks on primed and active enhancer elements (PubMed:24081332). Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2 (PubMed:17707229). Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development (By similarity). Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation (By similarity). {ECO:0000250\|UniProtKB:O08550, ECO:0000269\|PubMed:17707229, ECO:0000269\|PubMed:24081332, ECO:0000269\|PubMed:25561738}.
Q9UMX1	SUFU	S352	ochoa\|psp	Suppressor of fused homolog (SUFUH)	Negative regulator in the hedgehog/smoothened signaling pathway (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:12068298, PubMed:12975309, PubMed:15367681, PubMed:22365972, PubMed:24217340, PubMed:24311597, PubMed:27234298, PubMed:28965847). Down-regulates GLI1-mediated transactivation of target genes (PubMed:15367681, PubMed:24217340, PubMed:24311597). Down-regulates GLI2-mediated transactivation of target genes (PubMed:24217340, PubMed:24311597). Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:24217340). Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:24217340). Negative regulator of beta-catenin signaling (By similarity). Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full-length form of GLI3 (GLI3FL) (PubMed:24311597, PubMed:28965847). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state (PubMed:24311597, PubMed:28965847). Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R (PubMed:24311597, PubMed:28965847). When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A) (PubMed:24311597, PubMed:28965847). Required for normal embryonic development (By similarity). Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity). {ECO:0000250\|UniProtKB:Q9Z0P7, ECO:0000269\|PubMed:10559945, ECO:0000269\|PubMed:10564661, ECO:0000269\|PubMed:10806483, ECO:0000269\|PubMed:12068298, ECO:0000269\|PubMed:12975309, ECO:0000269\|PubMed:15367681, ECO:0000269\|PubMed:22365972, ECO:0000269\|PubMed:24217340, ECO:0000269\|PubMed:24311597, ECO:0000269\|PubMed:27234298, ECO:0000269\|PubMed:28965847}.
Q9UMZ2	SYNRG	S475	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UMZ2	SYNRG	S726	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UN36	NDRG2	S338	ochoa	Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Syld709613)	Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. {ECO:0000269\|PubMed:12845671, ECO:0000269\|PubMed:16103061, ECO:0000269\|PubMed:21247902}.
Q9UN81	L1RE1	S33	ochoa	LINE-1 retrotransposable element ORF1 protein (L1ORF1p) (LINE retrotransposable element 1) (LINE1 retrotransposable element 1)	Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded. {ECO:0000269\|PubMed:11158327, ECO:0000269\|PubMed:21937507, ECO:0000269\|PubMed:28806172, ECO:0000269\|PubMed:30122351, ECO:0000269\|PubMed:8945518}.
Q9UNF0	PACSIN2	S360	ochoa	Protein kinase C and casein kinase substrate in neurons protein 2 (Syndapin-2) (Syndapin-II) (SdpII)	Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus (PubMed:21693584, PubMed:23129763, PubMed:23236520, PubMed:23596323). Essential for endothelial organization in sprouting angiogenesis, modulates CDH5-based junctions. Facilitates endothelial front-rear polarity during migration by recruiting EHD4 and MICALL1 to asymmetric adherens junctions between leader and follower cells (By similarity). {ECO:0000250\|UniProtKB:Q9WVE8, ECO:0000269\|PubMed:21693584, ECO:0000269\|PubMed:23129763, ECO:0000269\|PubMed:23236520, ECO:0000269\|PubMed:23596323}.; FUNCTION: (Microbial infection) Specifically enhances the efficiency of HIV-1 virion spread by cell-to-cell transfer (PubMed:29891700). Also promotes the protrusion engulfment during cell-to-cell spread of bacterial pathogens like Listeria monocytogenes (PubMed:31242077). Involved in lipid droplet formation, which is important for HCV virion assembly (PubMed:31801866). {ECO:0000269\|PubMed:29891700, ECO:0000269\|PubMed:31242077, ECO:0000269\|PubMed:31801866}.
Q9UNF1	MAGED2	S197	ochoa	Melanoma-associated antigen D2 (11B6) (Breast cancer-associated gene 1 protein) (BCG-1) (Hepatocellular carcinoma-associated protein JCL-1) (MAGE-D2 antigen)	Regulates the expression, localization to the plasma membrane and function of the sodium chloride cotransporters SLC12A1 and SLC12A3, two key components of salt reabsorption in the distal renal tubule. {ECO:0000269\|PubMed:27120771}.
Q9UP95	SLC12A4	S973	ochoa	Solute carrier family 12 member 4 (Electroneutral potassium-chloride cotransporter 1) (Erythroid K-Cl cotransporter 1) (hKCC1)	Mediates electroneutral potassium-chloride cotransport when activated by cell swelling (PubMed:35759661). May contribute to cell volume homeostasis in single cells (PubMed:10913127, PubMed:34031912). May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). {ECO:0000250\|UniProtKB:Q9JIS8, ECO:0000269\|PubMed:10913127, ECO:0000269\|PubMed:34031912, ECO:0000269\|PubMed:35759661}.; FUNCTION: [Isoform 4]: No transporter activity. {ECO:0000269\|PubMed:11551954}.
Q9UPN3	MACF1	S820	ochoa	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPN3	MACF1	S1112	ochoa	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPN3	MACF1	S7236	ochoa	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPN4	CEP131	S120	ochoa	Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Pre-acrosome localization protein 1)	Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation (PubMed:17954613, PubMed:24185901). In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation (PubMed:24121310). In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310, PubMed:26616734). Also acts as a negative regulator of BBSome ciliary trafficking (PubMed:24550735). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells (PubMed:22797915, PubMed:26297806). Involved in centriole duplication (By similarity). Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). Essential for maintaining proper centriolar satellite integrity (PubMed:30804208). {ECO:0000250\|UniProtKB:Q62036, ECO:0000269\|PubMed:17954613, ECO:0000269\|PubMed:22797915, ECO:0000269\|PubMed:24121310, ECO:0000269\|PubMed:24185901, ECO:0000269\|PubMed:24550735, ECO:0000269\|PubMed:26297806, ECO:0000269\|PubMed:26616734, ECO:0000269\|PubMed:30804208}.
Q9UPN4	CEP131	S150	ochoa	Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Pre-acrosome localization protein 1)	Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation (PubMed:17954613, PubMed:24185901). In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation (PubMed:24121310). In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310, PubMed:26616734). Also acts as a negative regulator of BBSome ciliary trafficking (PubMed:24550735). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells (PubMed:22797915, PubMed:26297806). Involved in centriole duplication (By similarity). Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). Essential for maintaining proper centriolar satellite integrity (PubMed:30804208). {ECO:0000250\|UniProtKB:Q62036, ECO:0000269\|PubMed:17954613, ECO:0000269\|PubMed:22797915, ECO:0000269\|PubMed:24121310, ECO:0000269\|PubMed:24185901, ECO:0000269\|PubMed:24550735, ECO:0000269\|PubMed:26297806, ECO:0000269\|PubMed:26616734, ECO:0000269\|PubMed:30804208}.
Q9UPN9	TRIM33	S862	ochoa	E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RET-fused gene 7 protein) (Protein Rfg7) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33)	Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade). {ECO:0000250, ECO:0000269\|PubMed:10022127, ECO:0000269\|PubMed:15820681, ECO:0000269\|PubMed:16751102, ECO:0000269\|PubMed:19135894}.
Q9UPQ0	LIMCH1	S207	ochoa	LIM and calponin homology domains-containing protein 1	Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269\|PubMed:28228547}.
Q9UPQ0	LIMCH1	S210	ochoa	LIM and calponin homology domains-containing protein 1	Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269\|PubMed:28228547}.
Q9UPQ0	LIMCH1	S231	ochoa	LIM and calponin homology domains-containing protein 1	Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269\|PubMed:28228547}.
Q9UPQ0	LIMCH1	S756	ochoa	LIM and calponin homology domains-containing protein 1	Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269\|PubMed:28228547}.
Q9UPQ9	TNRC6B	S567	ochoa	Trinucleotide repeat-containing gene 6B protein	Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs) (PubMed:16289642, PubMed:19167051, PubMed:19304925, PubMed:32354837). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins (PubMed:16289642, PubMed:19167051, PubMed:19304925, PubMed:32354837). As scaffolding protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes (PubMed:21981923). {ECO:0000269\|PubMed:16289642, ECO:0000269\|PubMed:19167051, ECO:0000269\|PubMed:19304925, ECO:0000269\|PubMed:21981923, ECO:0000269\|PubMed:32354837}.
Q9UPS6	SETD1B	S1437	ochoa	Histone-lysine N-methyltransferase SETD1B (EC 2.1.1.364) (Lysine N-methyltransferase 2G) (SET domain-containing protein 1B) (hSET1B)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:17355966, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17355966, PubMed:25561738). Plays an essential role in regulating the transcriptional programming of multipotent hematopoietic progenitor cells and lymphoid lineage specification during hematopoiesis (By similarity). {ECO:0000250\|UniProtKB:Q8CFT2, ECO:0000269\|PubMed:17355966, ECO:0000269\|PubMed:25561738}.
Q9UPT8	ZC3H4	S165	ochoa	Zinc finger CCCH domain-containing protein 4	RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269\|PubMed:33767452, ECO:0000269\|PubMed:33913806}.
Q9UPT8	ZC3H4	S913	ochoa	Zinc finger CCCH domain-containing protein 4	RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269\|PubMed:33767452, ECO:0000269\|PubMed:33913806}.
Q9UPT8	ZC3H4	S1275	ochoa	Zinc finger CCCH domain-containing protein 4	RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269\|PubMed:33767452, ECO:0000269\|PubMed:33913806}.
Q9UPU5	USP24	S1138	ochoa	Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)	Ubiquitin-specific protease that regulates cell survival in various contexts through modulating the protein stability of some of its substrates including DDB2, MCL1 or TP53. Plays a positive role on ferritinophagy where ferritin is degraded in lysosomes and releases free iron. {ECO:0000269\|PubMed:23159851, ECO:0000269\|PubMed:29695420}.
Q9UPU5	USP24	S1141	ochoa	Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)	Ubiquitin-specific protease that regulates cell survival in various contexts through modulating the protein stability of some of its substrates including DDB2, MCL1 or TP53. Plays a positive role on ferritinophagy where ferritin is degraded in lysosomes and releases free iron. {ECO:0000269\|PubMed:23159851, ECO:0000269\|PubMed:29695420}.
Q9UPU5	USP24	S1378	ochoa	Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)	Ubiquitin-specific protease that regulates cell survival in various contexts through modulating the protein stability of some of its substrates including DDB2, MCL1 or TP53. Plays a positive role on ferritinophagy where ferritin is degraded in lysosomes and releases free iron. {ECO:0000269\|PubMed:23159851, ECO:0000269\|PubMed:29695420}.
Q9UPU5	USP24	S1379	ochoa	Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)	Ubiquitin-specific protease that regulates cell survival in various contexts through modulating the protein stability of some of its substrates including DDB2, MCL1 or TP53. Plays a positive role on ferritinophagy where ferritin is degraded in lysosomes and releases free iron. {ECO:0000269\|PubMed:23159851, ECO:0000269\|PubMed:29695420}.
Q9UPU7	TBC1D2B	S322	ochoa	TBC1 domain family member 2B	GTPase-activating protein that plays a role in the early steps of endocytosis (PubMed:32623794). {ECO:0000269\|PubMed:32623794}.
Q9UPV0	CEP164	S292	ochoa	Centrosomal protein of 164 kDa (Cep164)	Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1. {ECO:0000269\|PubMed:17954613, ECO:0000269\|PubMed:18283122, ECO:0000269\|PubMed:23348840}.
Q9UPV9	TRAK1	S543	ochoa	Trafficking kinesin-binding protein 1 (106 kDa O-GlcNAc transferase-interacting protein) (Protein Milton)	Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors (PubMed:18675823). Involved in mitochondrial motility. When O-glycosylated, abolishes mitochondrial motility. Crucial for recruiting OGT to the mitochondrial surface of neuronal processes (PubMed:24995978). TRAK1 and RHOT form an essential protein complex that links KIF5 to mitochondria for light chain-independent, anterograde transport of mitochondria (By similarity). {ECO:0000250\|UniProtKB:Q960V3, ECO:0000269\|PubMed:18675823, ECO:0000269\|PubMed:24995978}.
Q9UPZ3	HPS5	S467	ochoa	BLOC-2 complex member HPS5 (Alpha-integrin-binding protein 63) (Hermansky-Pudlak syndrome 5 protein) (Ruby-eye protein 2 homolog) (Ru2)	May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269\|PubMed:15296495, ECO:0000269\|PubMed:17301833}.
Q9UPZ3	HPS5	S666	ochoa	BLOC-2 complex member HPS5 (Alpha-integrin-binding protein 63) (Hermansky-Pudlak syndrome 5 protein) (Ruby-eye protein 2 homolog) (Ru2)	May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269\|PubMed:15296495, ECO:0000269\|PubMed:17301833}.
Q9UQ35	SRRM2	S150	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S317	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S421	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S424	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S901	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S908	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S974	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1014	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1034	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1048	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1079	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1142	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1150	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1264	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1326	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1404	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1658	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2147	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2388	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2459	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQC2	GAB2	S147	ochoa	GRB2-associated-binding protein 2 (GRB2-associated binder 2) (Growth factor receptor bound protein 2-associated protein 2) (pp100)	Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis. {ECO:0000269\|PubMed:15750601, ECO:0000269\|PubMed:19172738}.
Q9UQE7	SMC3	S1083	ochoa\|psp	Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP)	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269\|PubMed:11076961, ECO:0000269\|PubMed:19907496}.
Q9UQE7	SMC3	S1089	ochoa	Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP)	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269\|PubMed:11076961, ECO:0000269\|PubMed:19907496}.
Q9UQQ2	SH2B3	S343	ochoa	SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk)	Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}.
Q9UQR0	SCML2	S261	ochoa	Sex comb on midleg-like protein 2	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.
Q9UQR0	SCML2	S264	ochoa	Sex comb on midleg-like protein 2	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.
Q9UQR0	SCML2	S267	ochoa\|psp	Sex comb on midleg-like protein 2	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.
Q9Y250	LZTS1	S146	ochoa	Leucine zipper putative tumor suppressor 1 (F37/esophageal cancer-related gene-coding leucine-zipper motif) (Fez1)	Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor. {ECO:0000269\|PubMed:10097140, ECO:0000269\|PubMed:11464283, ECO:0000269\|PubMed:11504921}.
Q9Y250	LZTS1	S178	ochoa	Leucine zipper putative tumor suppressor 1 (F37/esophageal cancer-related gene-coding leucine-zipper motif) (Fez1)	Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor. {ECO:0000269\|PubMed:10097140, ECO:0000269\|PubMed:11464283, ECO:0000269\|PubMed:11504921}.
Q9Y261	FOXA2	S309	ochoa	Hepatocyte nuclear factor 3-beta (HNF-3-beta) (HNF-3B) (Forkhead box protein A2) (Transcription factor 3B) (TCF-3B)	Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation. {ECO:0000250}.
Q9Y294	ASF1A	S172	ochoa	Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (hAsf1) (hAsf1a) (CCG1-interacting factor A) (CIA) (hCIA)	Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). {ECO:0000269\|PubMed:10759893, ECO:0000269\|PubMed:11897662, ECO:0000269\|PubMed:12842904, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527, ECO:0000269\|PubMed:15664198, ECO:0000269\|PubMed:16151251, ECO:0000269\|PubMed:21454524, ECO:0000269\|PubMed:29408485, ECO:0000269\|PubMed:29478807}.
Q9Y294	ASF1A	S181	ochoa	Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (hAsf1) (hAsf1a) (CCG1-interacting factor A) (CIA) (hCIA)	Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). {ECO:0000269\|PubMed:10759893, ECO:0000269\|PubMed:11897662, ECO:0000269\|PubMed:12842904, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527, ECO:0000269\|PubMed:15664198, ECO:0000269\|PubMed:16151251, ECO:0000269\|PubMed:21454524, ECO:0000269\|PubMed:29408485, ECO:0000269\|PubMed:29478807}.
Q9Y2F5	ICE1	S931	ochoa	Little elongation complex subunit 1 (Interactor of little elongator complex ELL subunit 1)	Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically acts as a scaffold protein that promotes the LEC complex formation and recruitment and RNA polymerase II occupancy at snRNA genes in subnuclear bodies (PubMed:23932780). {ECO:0000269\|PubMed:22195968, ECO:0000269\|PubMed:23932780}.
Q9Y2H0	DLGAP4	S609	ochoa	Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)	May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Q9Y2H0	DLGAP4	S614	ochoa	Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)	May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Q9Y2H2	INPP5F	S913	ochoa	Phosphatidylinositide phosphatase SAC2 (EC 3.1.3.25) (Inositol polyphosphate 5-phosphatase F) (Sac domain-containing inositol phosphatase 2) (Sac domain-containing phosphoinositide 4-phosphatase 2) (hSAC2)	Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling (PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (PubMed:25869669). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus (PubMed:25476455). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (By similarity). May play a role as negative regulator of axon regeneration after central nervous system injuries (By similarity). {ECO:0000250\|UniProtKB:Q8CDA1, ECO:0000269\|PubMed:17322895, ECO:0000269\|PubMed:25476455, ECO:0000269\|PubMed:25869669}.
Q9Y2H5	PLEKHA6	S282	ochoa	Pleckstrin homology domain-containing family A member 6 (PH domain-containing family A member 6) (Phosphoinositol 3-phosphate-binding protein 3) (PEPP-3)	None
Q9Y2H6	FNDC3A	S213	ochoa	Fibronectin type-III domain-containing protein 3A (Human gene expressed in odontoblasts)	Mediates spermatid-Sertoli adhesion during spermatogenesis. {ECO:0000250}.
Q9Y2I7	PIKFYVE	S318	ochoa\|psp	1-phosphatidylinositol 3-phosphate 5-kinase (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (FYVE finger-containing phosphoinositide kinase) (PIKfyve) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (Serine-protein kinase PIKFYVE) (EC 2.7.11.1)	Dual specificity kinase implicated in myriad essential cellular processes such as maintenance of endomembrane homeostasis, and endocytic-vacuolar pathway, lysosomal trafficking, nuclear transport, stress- or hormone-induced signaling and cell cycle progression (PubMed:23086417). The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Sole enzyme to catalyze the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form (PtdIns(3,5)P2) (PubMed:17556371). Also catalyzes the phosphorylation of phosphatidylinositol on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 5-phosphate (PtdIns(5)P) (PubMed:22621786). Has serine-protein kinase activity and is able to autophosphorylate and transphosphorylate. Autophosphorylation inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (PubMed:33098764). Involved in key endosome operations such as fission and fusion in the course of endosomal cargo transport (PubMed:22621786). Required for the maturation of early into late endosomes, phagosomes and lysosomes (PubMed:30612035). Regulates vacuole maturation and nutrient recovery following engulfment of macromolecules, initiates the redistribution of accumulated lysosomal contents back into the endosome network (PubMed:27623384). Critical regulator of the morphology, degradative activity, and protein turnover of the endolysosomal system in macrophages and platelets (By similarity). In neutrophils, critical to perform chemotaxis, generate ROS, and undertake phagosome fusion with lysosomes (PubMed:28779020). Plays a key role in the processing and presentation of antigens by major histocompatibility complex class II (MHC class II) mediated by CTSS (PubMed:30612035). Regulates melanosome biogenesis by controlling the delivery of proteins from the endosomal compartment to the melanosome (PubMed:29584722). Essential for systemic glucose homeostasis, mediates insulin-induced signals for endosome/actin remodeling in the course of GLUT4 translocation/glucose uptake activation (By similarity). Supports microtubule-based endosome-to-trans-Golgi network cargo transport, through association with SPAG9 and RABEPK (By similarity). Mediates EGFR trafficking to the nucleus (PubMed:17909029). {ECO:0000250\|UniProtKB:Q9Z1T6, ECO:0000269\|PubMed:17556371, ECO:0000269\|PubMed:17909029, ECO:0000269\|PubMed:22621786, ECO:0000269\|PubMed:27623384, ECO:0000269\|PubMed:28779020, ECO:0000269\|PubMed:29584722, ECO:0000269\|PubMed:30612035, ECO:0000269\|PubMed:33098764, ECO:0000303\|PubMed:23086417}.; FUNCTION: (Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC) by endocytosis. {ECO:0000269\|PubMed:32221306}.
Q9Y2J4	AMOTL2	S540	ochoa	Angiomotin-like protein 2 (Leman coiled-coil protein) (LCCP)	Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Plays a role in coupling actin fibers to cell junctions in endothelial cells and is therefore required for correct endothelial cell morphology via facilitating transcellular transmission of mechanical force resulting in endothelial cell elongation (By similarity). Required for the anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane which facilitates organization of radial actin fiber structure and cellular response to contractile forces (PubMed:28842668). This contributes to maintenance of cell area, size, shape, epithelial sheet organization and trophectoderm cell properties that facilitate blastocyst zona hatching (PubMed:28842668). Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. Activates the Hippo signaling pathway in response to cell contact inhibition via interaction with and ubiquitination by Crumbs complex-bound WWP1 (PubMed:34404733). Ubiquitinated AMOTL2 then interacts with LATS2 which in turn phosphorylates YAP1, excluding it from the nucleus and localizing it to the cytoplasm and tight junctions, therefore ultimately repressing YAP1-driven transcription of target genes (PubMed:17293535, PubMed:21205866, PubMed:26598551). Acts to inhibit WWTR1/TAZ transcriptional coactivator activity via sequestering WWTR1/TAZ in the cytoplasm and at tight junctions (PubMed:23911299). Regulates the size and protein composition of the podosome cortex and core at myofibril neuromuscular junctions (PubMed:23525008). Selectively promotes FGF-induced MAPK activation through SRC (PubMed:17293535). May play a role in the polarity, proliferation and migration of endothelial cells. {ECO:0000250\|UniProtKB:Q8K371, ECO:0000269\|PubMed:17293535, ECO:0000269\|PubMed:21205866, ECO:0000269\|PubMed:21937427, ECO:0000269\|PubMed:22362771, ECO:0000269\|PubMed:23525008, ECO:0000269\|PubMed:23911299, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:28842668, ECO:0000269\|PubMed:34404733}.
Q9Y2K5	R3HDM2	S354	ochoa	R3H domain-containing protein 2	None
Q9Y2K7	KDM2A	S832	ochoa	Lysine-specific demethylase 2A (EC 1.14.11.27) (CXXC-type zinc finger protein 8) (F-box and leucine-rich repeat protein 11) (F-box protein FBL7) (F-box protein Lilina) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)	Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. Regulates circadian gene expression by repressing the transcriptional activator activity of CLOCK-BMAL1 heterodimer and RORA in a catalytically-independent manner (PubMed:26037310). {ECO:0000269\|PubMed:16362057, ECO:0000269\|PubMed:19001877, ECO:0000269\|PubMed:26037310, ECO:0000269\|PubMed:28262558}.
Q9Y2L5	TRAPPC8	S279	ochoa	Trafficking protein particle complex subunit 8 (Protein TRS85 homolog)	Plays a role in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage (PubMed:21525244). Maintains together with TBC1D14 the cycling pool of ATG9 required for initiation of autophagy (PubMed:26711178). Involved in collagen secretion (PubMed:32095531). {ECO:0000269\|PubMed:21525244, ECO:0000269\|PubMed:26711178, ECO:0000269\|PubMed:32095531}.
Q9Y2L6	FRMD4B	S778	ochoa	FERM domain-containing protein 4B (GRP1-binding protein GRSP1)	Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex. Plays a redundant role with FRMD4A in epithelial polarization. {ECO:0000250\|UniProtKB:Q920B0}.
Q9Y2U5	MAP3K2	S300	ochoa	Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2)	Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. {ECO:0000250, ECO:0000269\|PubMed:10713157, ECO:0000269\|PubMed:16001074}.
Q9Y2U5	MAP3K2	S315	ochoa	Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2)	Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. {ECO:0000250, ECO:0000269\|PubMed:10713157, ECO:0000269\|PubMed:16001074}.
Q9Y2U8	LEMD3	S117	ochoa	Inner nuclear membrane protein Man1 (LEM domain-containing protein 3)	Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. {ECO:0000269\|PubMed:15601644, ECO:0000269\|PubMed:15647271}.
Q9Y2W1	THRAP3	S190	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2W1	THRAP3	S217	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2W1	THRAP3	S240	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2W1	THRAP3	S295	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2W1	THRAP3	S326	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2W1	THRAP3	S336	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2X7	GIT1	S514	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y2X7	GIT1	S577	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y2X7	GIT1	S581	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y3C5	RNF11	S25	ochoa	RING finger protein 11	Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. {ECO:0000269\|PubMed:14755250}.
Q9Y3M2	CBY1	S26	ochoa	Protein chibby homolog 1 (ARPP-binding protein) (Cytosolic leucine-rich protein) (PIGEA-14) (PKD2 interactor, Golgi and endoplasmic reticulum-associated 1)	Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors (PubMed:12712206, PubMed:19435523). Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins (PubMed:15194699). Promotes adipocyte and cardiomyocyte differentiation (By similarity). {ECO:0000250\|UniProtKB:Q9D1C2, ECO:0000269\|PubMed:12712206, ECO:0000269\|PubMed:15194699, ECO:0000269\|PubMed:19435523}.
Q9Y3R5	DOP1B	S586	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y3Z3	SAMHD1	S33	ochoa\|psp	Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Dendritic cell-derived IFNG-induced protein) (DCIP) (Monocyte protein 5) (MOP-5) (SAM domain and HD domain-containing protein 1) (hSAMHD1)	Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:26294762, PubMed:26431200, PubMed:28229507, PubMed:28834754, PubMed:29670289). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses, such as HIV-1: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23364794, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:25038827, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:24217394, PubMed:29610582). Not able to restrict infection by HIV-2 virus; because restriction activity is counteracted by HIV-2 viral protein Vpx (PubMed:21613998, PubMed:21720370). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (PubMed:23858451). Phosphorylation at Thr-592 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (PubMed:23601106, PubMed:23602554, PubMed:29610582, PubMed:29670289). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (PubMed:29670289). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (PubMed:27477283, PubMed:29670289). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (PubMed:29670289). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (By similarity). {ECO:0000250\|UniProtKB:Q60710, ECO:0000269\|PubMed:19525956, ECO:0000269\|PubMed:21613998, ECO:0000269\|PubMed:21720370, ECO:0000269\|PubMed:22056990, ECO:0000269\|PubMed:23364794, ECO:0000269\|PubMed:23601106, ECO:0000269\|PubMed:23602554, ECO:0000269\|PubMed:23858451, ECO:0000269\|PubMed:24035396, ECO:0000269\|PubMed:24217394, ECO:0000269\|PubMed:24336198, ECO:0000269\|PubMed:25038827, ECO:0000269\|PubMed:26101257, ECO:0000269\|PubMed:26294762, ECO:0000269\|PubMed:26431200, ECO:0000269\|PubMed:27477283, ECO:0000269\|PubMed:28229507, ECO:0000269\|PubMed:28834754, ECO:0000269\|PubMed:29610582, ECO:0000269\|PubMed:29670289}.
Q9Y426	C2CD2	S441	ochoa	C2 domain-containing protein 2 (Transmembrane protein 24-like)	None
Q9Y426	C2CD2	S522	ochoa	C2 domain-containing protein 2 (Transmembrane protein 24-like)	None
Q9Y446	PKP3	S121	ochoa	Plakophilin-3	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:24124604). Required for the localization of DSG2, DSP and PKP2 to mature desmosome junctions (PubMed:20859650). May also play a role in the maintenance of DSG3 protein abundance in keratinocytes (By similarity). Required for the formation of DSP-containing desmosome precursors in the cytoplasm during desmosome assembly (PubMed:25208567). Also regulates the accumulation of CDH1 to mature desmosome junctions, via cAMP-dependent signaling and its interaction with activated RAP1A (PubMed:25208567). Positively regulates the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with FXR1, may also regulate the protein abundance of DSP via the same mechanism (PubMed:25225333). May also regulate the protein abundance of the desmosome component PKP1 (By similarity). Required for the organization of desmosome junctions at intercellular borders between basal keratinocytes of the epidermis, as a result plays a role in maintenance of the dermal barrier and regulation of the dermal inflammatory response (By similarity). Required during epidermal keratinocyte differentiation for cell adherence at tricellular cell-cell contacts, via regulation of the timely formation of adherens junctions and desmosomes in a calcium-dependent manner, and may also play a role in the organization of the intracellular actin fiber belt (By similarity). Acts as a negative regulator of the inflammatory response in hematopoietic cells of the skin and intestine, via modulation of proinflammatory cytokine production (By similarity). Important for epithelial barrier maintenance in the intestine to reduce intestinal permeability, thereby plays a role in protection from intestinal-derived endotoxemia (By similarity). Required for the development of hair follicles, via a role in the regulation of inner root sheaf length, correct alignment and anterior-posterior polarity of hair follicles (By similarity). Promotes proliferation and cell-cycle G1/S phase transition of keratinocytes (By similarity). Promotes E2F1-driven transcription of G1/S phase promoting genes by acting to release E2F1 from its inhibitory interaction with RB1, via sequestering RB1 and CDKN1A to the cytoplasm and thereby increasing CDK4- and CDK6-driven phosphorylation of RB1 (By similarity). May act as a scaffold protein to facilitate MAPK phosphorylation of RPS6KA protein family members and subsequently promote downstream EGFR signaling (By similarity). May play a role in the positive regulation of transcription of Wnt-mediated TCF-responsive target genes (PubMed:34058472). {ECO:0000250\|UniProtKB:Q9QY23, ECO:0000269\|PubMed:20859650, ECO:0000269\|PubMed:24124604, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:34058472}.
Q9Y446	PKP3	S141	ochoa	Plakophilin-3	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:24124604). Required for the localization of DSG2, DSP and PKP2 to mature desmosome junctions (PubMed:20859650). May also play a role in the maintenance of DSG3 protein abundance in keratinocytes (By similarity). Required for the formation of DSP-containing desmosome precursors in the cytoplasm during desmosome assembly (PubMed:25208567). Also regulates the accumulation of CDH1 to mature desmosome junctions, via cAMP-dependent signaling and its interaction with activated RAP1A (PubMed:25208567). Positively regulates the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with FXR1, may also regulate the protein abundance of DSP via the same mechanism (PubMed:25225333). May also regulate the protein abundance of the desmosome component PKP1 (By similarity). Required for the organization of desmosome junctions at intercellular borders between basal keratinocytes of the epidermis, as a result plays a role in maintenance of the dermal barrier and regulation of the dermal inflammatory response (By similarity). Required during epidermal keratinocyte differentiation for cell adherence at tricellular cell-cell contacts, via regulation of the timely formation of adherens junctions and desmosomes in a calcium-dependent manner, and may also play a role in the organization of the intracellular actin fiber belt (By similarity). Acts as a negative regulator of the inflammatory response in hematopoietic cells of the skin and intestine, via modulation of proinflammatory cytokine production (By similarity). Important for epithelial barrier maintenance in the intestine to reduce intestinal permeability, thereby plays a role in protection from intestinal-derived endotoxemia (By similarity). Required for the development of hair follicles, via a role in the regulation of inner root sheaf length, correct alignment and anterior-posterior polarity of hair follicles (By similarity). Promotes proliferation and cell-cycle G1/S phase transition of keratinocytes (By similarity). Promotes E2F1-driven transcription of G1/S phase promoting genes by acting to release E2F1 from its inhibitory interaction with RB1, via sequestering RB1 and CDKN1A to the cytoplasm and thereby increasing CDK4- and CDK6-driven phosphorylation of RB1 (By similarity). May act as a scaffold protein to facilitate MAPK phosphorylation of RPS6KA protein family members and subsequently promote downstream EGFR signaling (By similarity). May play a role in the positive regulation of transcription of Wnt-mediated TCF-responsive target genes (PubMed:34058472). {ECO:0000250\|UniProtKB:Q9QY23, ECO:0000269\|PubMed:20859650, ECO:0000269\|PubMed:24124604, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:34058472}.
Q9Y446	PKP3	S291	ochoa	Plakophilin-3	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:24124604). Required for the localization of DSG2, DSP and PKP2 to mature desmosome junctions (PubMed:20859650). May also play a role in the maintenance of DSG3 protein abundance in keratinocytes (By similarity). Required for the formation of DSP-containing desmosome precursors in the cytoplasm during desmosome assembly (PubMed:25208567). Also regulates the accumulation of CDH1 to mature desmosome junctions, via cAMP-dependent signaling and its interaction with activated RAP1A (PubMed:25208567). Positively regulates the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with FXR1, may also regulate the protein abundance of DSP via the same mechanism (PubMed:25225333). May also regulate the protein abundance of the desmosome component PKP1 (By similarity). Required for the organization of desmosome junctions at intercellular borders between basal keratinocytes of the epidermis, as a result plays a role in maintenance of the dermal barrier and regulation of the dermal inflammatory response (By similarity). Required during epidermal keratinocyte differentiation for cell adherence at tricellular cell-cell contacts, via regulation of the timely formation of adherens junctions and desmosomes in a calcium-dependent manner, and may also play a role in the organization of the intracellular actin fiber belt (By similarity). Acts as a negative regulator of the inflammatory response in hematopoietic cells of the skin and intestine, via modulation of proinflammatory cytokine production (By similarity). Important for epithelial barrier maintenance in the intestine to reduce intestinal permeability, thereby plays a role in protection from intestinal-derived endotoxemia (By similarity). Required for the development of hair follicles, via a role in the regulation of inner root sheaf length, correct alignment and anterior-posterior polarity of hair follicles (By similarity). Promotes proliferation and cell-cycle G1/S phase transition of keratinocytes (By similarity). Promotes E2F1-driven transcription of G1/S phase promoting genes by acting to release E2F1 from its inhibitory interaction with RB1, via sequestering RB1 and CDKN1A to the cytoplasm and thereby increasing CDK4- and CDK6-driven phosphorylation of RB1 (By similarity). May act as a scaffold protein to facilitate MAPK phosphorylation of RPS6KA protein family members and subsequently promote downstream EGFR signaling (By similarity). May play a role in the positive regulation of transcription of Wnt-mediated TCF-responsive target genes (PubMed:34058472). {ECO:0000250\|UniProtKB:Q9QY23, ECO:0000269\|PubMed:20859650, ECO:0000269\|PubMed:24124604, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:34058472}.
Q9Y485	DMXL1	S924	ochoa	DmX-like protein 1 (X-like 1 protein)	None
Q9Y4A5	TRRAP	S2083	ochoa	Transformation/transcription domain-associated protein (350/400 kDa PCAF-associated factor) (PAF350/400) (STAF40) (Tra1 homolog)	Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. May play a role in the formation and maintenance of the auditory system (By similarity). {ECO:0000250\|UniProtKB:A0A0R4ITC5, ECO:0000269\|PubMed:11418595, ECO:0000269\|PubMed:12138177, ECO:0000269\|PubMed:12660246, ECO:0000269\|PubMed:12743606, ECO:0000269\|PubMed:14966270, ECO:0000269\|PubMed:17967892, ECO:0000269\|PubMed:24463511, ECO:0000269\|PubMed:9708738}.
Q9Y4B5	MTCL1	S1820	ochoa	Microtubule cross-linking factor 1 (Coiled-coil domain-containing protein 165) (PAR-1-interacting protein) (SOGA family member 2)	Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation (PubMed:23902687). Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells (PubMed:23902687). Required for faithful chromosome segregation during mitosis (PubMed:33587225). {ECO:0000269\|PubMed:23902687, ECO:0000269\|PubMed:33587225}.
Q9Y4B6	DCAF1	S1006	ochoa	DDB1- and CUL4-associated factor 1 (HIV-1 Vpr-binding protein) (VprBP) (Serine/threonine-protein kinase VPRBP) (EC 2.7.11.1) (Vpr-interacting protein)	Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2 (PubMed:23063525). Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination (By similarity). Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:19287380, PubMed:23362280). The EDVP complex also mediates ubiquitination and degradation of CCP110 (PubMed:28242748, PubMed:34259627). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription (PubMed:24140421). H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). {ECO:0000250\|UniProtKB:Q80TR8, ECO:0000269\|PubMed:16964240, ECO:0000269\|PubMed:17609381, ECO:0000269\|PubMed:17630831, ECO:0000269\|PubMed:18332868, ECO:0000269\|PubMed:18524771, ECO:0000269\|PubMed:18606781, ECO:0000269\|PubMed:19287380, ECO:0000269\|PubMed:20644714, ECO:0000269\|PubMed:22184063, ECO:0000269\|PubMed:23063525, ECO:0000269\|PubMed:23362280, ECO:0000269\|PubMed:24140421, ECO:0000269\|PubMed:28242748, ECO:0000269\|PubMed:34259627}.; FUNCTION: (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. {ECO:0000269\|PubMed:17314515, ECO:0000269\|PubMed:17559673, ECO:0000269\|PubMed:17609381, ECO:0000269\|PubMed:17620334, ECO:0000269\|PubMed:17626091, ECO:0000269\|PubMed:17630831, ECO:0000269\|PubMed:18524771, ECO:0000269\|PubMed:24116224}.; FUNCTION: (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. {ECO:0000269\|PubMed:17314515, ECO:0000269\|PubMed:18464893, ECO:0000269\|PubMed:19264781, ECO:0000269\|PubMed:19923175, ECO:0000269\|PubMed:24336198}.
Q9Y4E8	USP15	S242	ochoa	Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4)	Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways (PubMed:16005295, PubMed:17318178, PubMed:19576224, PubMed:19826004, PubMed:21947082, PubMed:22344298, PubMed:24852371). Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:33093067). May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B (PubMed:24526689). Acts as an inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on target proteins such as MFN2, thereby reducing parkin's ability to drive mitophagy (PubMed:24852371). Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP (PubMed:16005295, PubMed:17318178, PubMed:19576224, PubMed:19826004). Involved in endosome organization by mediating deubiquitination of SQSTM1: ubiquitinated SQSTM1 forms a molecular bridge that restrains cognate vesicles in the perinuclear region and its deubiquitination releases target vesicles for fast transport into the cell periphery (PubMed:27368102). Acts as a negative regulator of antifungal immunity by mediating 'Lys-27'-linked deubiquitination of CARD9, thereby inactivating CARD9 (PubMed:33093067). {ECO:0000269\|PubMed:16005295, ECO:0000269\|PubMed:17318178, ECO:0000269\|PubMed:19576224, ECO:0000269\|PubMed:19826004, ECO:0000269\|PubMed:21947082, ECO:0000269\|PubMed:22344298, ECO:0000269\|PubMed:24526689, ECO:0000269\|PubMed:24852371, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:33093067}.; FUNCTION: (Microbial infection) Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway. {ECO:0000269\|PubMed:19553310}.
Q9Y4F1	FARP1	S878	ochoa	FERM, ARHGEF and pleckstrin domain-containing protein 1 (Chondrocyte-derived ezrin-like protein) (FERM, RhoGEF and pleckstrin domain-containing protein 1) (Pleckstrin homology domain-containing family C member 2) (PH domain-containing family C member 2)	Functions as a guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}.
Q9Y4F5	CEP170B	S425	ochoa	Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B)	Plays a role in microtubule organization. {ECO:0000250\|UniProtKB:Q5SW79}.
Q9Y4F5	CEP170B	S1362	ochoa	Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B)	Plays a role in microtubule organization. {ECO:0000250\|UniProtKB:Q5SW79}.
Q9Y4F5	CEP170B	S1551	ochoa	Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B)	Plays a role in microtubule organization. {ECO:0000250\|UniProtKB:Q5SW79}.
Q9Y4G8	RAPGEF2	S1162	ochoa	Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)	Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Also acts as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10548487, PubMed:10608844, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Also provides inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269\|PubMed:10548487, ECO:0000269\|PubMed:10608844, ECO:0000269\|PubMed:10608883, ECO:0000269\|PubMed:10801446, ECO:0000269\|PubMed:10934204, ECO:0000269\|PubMed:11359771, ECO:0000269\|PubMed:12391161, ECO:0000269\|PubMed:16272156, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:23800469}.
Q9Y4G8	RAPGEF2	S1254	ochoa\|psp	Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)	Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Also acts as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10548487, PubMed:10608844, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Also provides inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269\|PubMed:10548487, ECO:0000269\|PubMed:10608844, ECO:0000269\|PubMed:10608883, ECO:0000269\|PubMed:10801446, ECO:0000269\|PubMed:10934204, ECO:0000269\|PubMed:11359771, ECO:0000269\|PubMed:12391161, ECO:0000269\|PubMed:16272156, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:23800469}.
Q9Y4H2	IRS2	S312	ochoa	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
Q9Y4H2	IRS2	S1154	ochoa	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
Q9Y4W2	LAS1L	S520	ochoa	Ribosomal biogenesis protein LAS1L (Endoribonuclease LAS1L) (EC 3.1.-.-) (Protein LAS1 homolog)	Required for the synthesis of the 60S ribosomal subunit and maturation of the 28S rRNA (PubMed:20647540). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Required for the efficient pre-rRNA processing at both ends of internal transcribed spacer 2 (ITS2) (PubMed:22083961). {ECO:0000269\|PubMed:20647540, ECO:0000269\|PubMed:22083961, ECO:0000269\|PubMed:22872859}.
Q9Y520	PRRC2C	S785	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y520	PRRC2C	S1280	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y520	PRRC2C	S2019	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y520	PRRC2C	S2035	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y520	PRRC2C	S2686	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y520	PRRC2C	S2692	ochoa	Protein PRRC2C (BAT2 domain-containing protein 1) (HBV X-transactivated gene 2 protein) (HBV XAg-transactivated protein 2) (HLA-B-associated transcript 2-like 2) (Proline-rich and coiled-coil-containing protein 2C)	Required for efficient formation of stress granules. {ECO:0000269\|PubMed:29395067}.
Q9Y5A6	ZSCAN21	S157	ochoa	Zinc finger and SCAN domain-containing protein 21 (Renal carcinoma antigen NY-REN-21) (Zinc finger protein 38 homolog) (Zfp-38)	Strong transcriptional activator (By similarity). Plays an important role in spermatogenesis; essential for the progression of meiotic prophase I in spermatocytes (By similarity). {ECO:0000250\|UniProtKB:Q07231}.
Q9Y5B6	PAXBP1	S564	ochoa	PAX3- and PAX7-binding protein 1 (GC-rich sequence DNA-binding factor 1)	Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with a histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20. {ECO:0000250\|UniProtKB:P58501}.
Q9Y5K6	CD2AP	S556	ochoa	CD2-associated protein (Adapter protein CMS) (Cas ligand with multiple SH3 domains)	Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (PubMed:10339567). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis (PubMed:15800069). Plays a role in epithelial cell junctions formation (PubMed:22891260). {ECO:0000250\|UniProtKB:F1LRS8, ECO:0000250\|UniProtKB:Q9JLQ0, ECO:0000269\|PubMed:10339567, ECO:0000269\|PubMed:15800069, ECO:0000269\|PubMed:22891260}.
Q9Y5M8	SRPRB	S219	ochoa	Signal recognition particle receptor subunit beta (SR-beta) (Protein APMCF1)	Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity). {ECO:0000250\|UniProtKB:P47758}.
Q9Y5P4	CERT1	S132	ochoa\|psp	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y5P4	CERT1	S141	ochoa	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y5P4	CERT1	S147	ochoa	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y5P4	CERT1	S150	ochoa	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y5S2	CDC42BPB	S1677	ochoa	Serine/threonine-protein kinase MRCK beta (EC 2.7.11.1) (CDC42-binding protein kinase beta) (CDC42BP-beta) (DMPK-like beta) (Myotonic dystrophy kinase-related CDC42-binding kinase beta) (MRCK beta) (Myotonic dystrophy protein kinase-like beta)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250\|UniProtKB:Q7TT50, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:21949762}.
Q9Y5S2	CDC42BPB	S1683	ochoa\|psp	Serine/threonine-protein kinase MRCK beta (EC 2.7.11.1) (CDC42-binding protein kinase beta) (CDC42BP-beta) (DMPK-like beta) (Myotonic dystrophy kinase-related CDC42-binding kinase beta) (MRCK beta) (Myotonic dystrophy protein kinase-like beta)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250\|UniProtKB:Q7TT50, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:21949762}.
Q9Y5U2	TSSC4	S93	ochoa	U5 small nuclear ribonucleoprotein TSSC4 (Tumor-suppressing STF cDNA 4 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein)	Protein associated with the U5 snRNP, during its maturation and its post-splicing recycling and which is required for spliceosomal tri-snRNP complex assembly in the nucleus (PubMed:34131137, PubMed:35188580). Has a molecular sequestering activity and transiently hinders SNRNP200 binding sites for constitutive splicing factors that intervene later during the assembly of the spliceosome and splicing (PubMed:35188580). Together with its molecular sequestering activity, may also function as a molecular adapter and placeholder, coordinating the assembly of the U5 snRNP and its association with the U4/U6 di-snRNP (PubMed:34131137). {ECO:0000269\|PubMed:34131137, ECO:0000269\|PubMed:35188580}.
Q9Y5U5	TNFRSF18	S217	ochoa	Tumor necrosis factor receptor superfamily member 18 (Activation-inducible TNFR family receptor) (Glucocorticoid-induced TNFR-related protein) (CD antigen CD357)	Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway.
Q9Y608	LRRFIP2	S314	ochoa	Leucine-rich repeat flightless-interacting protein 2 (LRR FLII-interacting protein 2)	May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269\|PubMed:15677333, ECO:0000269\|PubMed:19265123}.
Q9Y653	ADGRG1	S676	ochoa	Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) [Cleaved into: Adhesion G-protein coupled receptor G1, N-terminal fragment (ADGRG1 N-terminal fragment) (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); Adhesion G-protein coupled receptor G1, C-terminal fragment (ADGRG1 C-terminal fragment) (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]	Adhesion G-protein coupled receptor (aGPCR) for steroid hormone 17alpha-hydroxypregnenolone (17-OH), which is involved in cell adhesion and cell-cell interactions (PubMed:39389061). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as RhoA pathway (PubMed:28874577, PubMed:35418682, PubMed:39389061). ADGRG1 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:22238662, PubMed:28424266, PubMed:35418682, PubMed:39389061). Acts as a potent suppressor of ferroptosis: binding to 17-OH-binding initiates signaling that down-regulates CD36 and alleviates ferroptosis-induced liver injury (By similarity). Ligand-binding also induces cell adhesion activity via association with proteins such as collagen III/COL3A1 and TGM2 (By similarity). Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells (By similarity). Involved in cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination: association with COL3A1 in the developing brain inhibits neuronal migration via activation of the RhoA pathway (PubMed:24531968). Together with TGM2, acts as a regulator of myelination and myelin repair in oligodendrocyte precursor cells (By similarity). Acts as a hemostatic sensor of shear force: G protein-coupled receptor signaling is activated in response to shear force in platelets, promoting G(13) G protein signaling, and platelet shape change and aggregation in a COL3A1-dependent manner (PubMed:33097663). Acts as an inhibitor of VEGFA production thereby inhibiting angiogenesis through a signaling pathway mediated by PRKCA (PubMed:16757564, PubMed:19572147, PubMed:21724588). Plays a role in the maintenance of hematopoietic stem cells in bone marrow niche (By similarity). Plays an essential role in testis development (By similarity). {ECO:0000250\|UniProtKB:Q8K209, ECO:0000269\|PubMed:16757564, ECO:0000269\|PubMed:19572147, ECO:0000269\|PubMed:21724588, ECO:0000269\|PubMed:22238662, ECO:0000269\|PubMed:24531968, ECO:0000269\|PubMed:28424266, ECO:0000269\|PubMed:28874577, ECO:0000269\|PubMed:33097663, ECO:0000269\|PubMed:35418682, ECO:0000269\|PubMed:39389061}.
Q9Y6D5	ARFGEF2	S620	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2)	Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269\|PubMed:12051703, ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15385626, ECO:0000269\|PubMed:16477018, ECO:0000269\|PubMed:17276987, ECO:0000269\|PubMed:18625701, ECO:0000269\|PubMed:20360857}.
Q9Y6D5	ARFGEF2	S623	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2)	Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269\|PubMed:12051703, ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15385626, ECO:0000269\|PubMed:16477018, ECO:0000269\|PubMed:17276987, ECO:0000269\|PubMed:18625701, ECO:0000269\|PubMed:20360857}.
Q9Y6D5	ARFGEF2	S1520	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2)	Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269\|PubMed:12051703, ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15385626, ECO:0000269\|PubMed:16477018, ECO:0000269\|PubMed:17276987, ECO:0000269\|PubMed:18625701, ECO:0000269\|PubMed:20360857}.
Q9Y6D6	ARFGEF1	S403	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S670	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S673	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S678	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S680	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D9	MAD1L1	S22	ochoa\|psp	Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181)	Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). {ECO:0000269\|PubMed:10049595, ECO:0000269\|PubMed:20133940, ECO:0000269\|PubMed:29162720, ECO:0000269\|PubMed:36322655}.; FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. {ECO:0000269\|PubMed:19010891}.
Q9Y6G9	DYNC1LI1	S421	ochoa	Cytoplasmic dynein 1 light intermediate chain 1 (LIC1) (Dynein light chain A) (DLC-A) (Dynein light intermediate chain 1, cytosolic) (DLIC-1)	Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. Forms a functional Rab11/RAB11FIP3/dynein complex onto endosomal membrane that regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endosomal recycling compartment (ERC) (PubMed:20026645). {ECO:0000269\|PubMed:19229290, ECO:0000269\|PubMed:20026645}.
Q9Y6J0	CABIN1	S2100	ochoa	Calcineurin-binding protein cabin-1 (Calcineurin inhibitor) (CAIN)	May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes. {ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:9655484}.
Q9Y6J9	TAF6L	S501	ochoa	TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) (PCAF-associated factor 65-alpha) (PAF65-alpha)	Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF5L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state. Functions with MYC to activate target gene expression through RNA polymerase II pause release (By similarity). {ECO:0000250\|UniProtKB:Q8R2K4, ECO:0000305\|PubMed:9674419}.
Q9Y6M5	SLC30A1	S173	ochoa	Proton-coupled zinc antiporter SLC30A1 (Solute carrier family 30 member 1) (Zinc transporter 1)	Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (PubMed:31471319). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells (By similarity). In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (PubMed:32441444). Forms a complex with TMC6/EVER1 and TMC8/EVER2 at the ER membrane of keratynocytes which facilitates zinc uptake into the ER (PubMed:18158319). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). {ECO:0000250\|UniProtKB:Q62720, ECO:0000269\|PubMed:18158319, ECO:0000269\|PubMed:31471319, ECO:0000269\|PubMed:32441444}.
Q9Y6N7	ROBO1	S1608	ochoa	Roundabout homolog 1 (Deleted in U twenty twenty) (H-Robo-1)	Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity). {ECO:0000250\|UniProtKB:O89026, ECO:0000269\|PubMed:10102268, ECO:0000269\|PubMed:24560577, ECO:0000269\|PubMed:26529257, ECO:0000305}.
Q9Y6N7	ROBO1	S1609	ochoa	Roundabout homolog 1 (Deleted in U twenty twenty) (H-Robo-1)	Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity). {ECO:0000250\|UniProtKB:O89026, ECO:0000269\|PubMed:10102268, ECO:0000269\|PubMed:24560577, ECO:0000269\|PubMed:26529257, ECO:0000305}.
Q9Y6N7	ROBO1	S1612	ochoa	Roundabout homolog 1 (Deleted in U twenty twenty) (H-Robo-1)	Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity). {ECO:0000250\|UniProtKB:O89026, ECO:0000269\|PubMed:10102268, ECO:0000269\|PubMed:24560577, ECO:0000269\|PubMed:26529257, ECO:0000305}.
Q9Y6Q9	NCOA3	S569	ochoa	Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.
Q9Y6Q9	NCOA3	S589	ochoa	Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.
Q9Y6R4	MAP3K4	S1274	ochoa	Mitogen-activated protein kinase kinase kinase 4 (EC 2.7.11.25) (MAP three kinase 1) (MAPK/ERK kinase kinase 4) (MEK kinase 4) (MEKK 4)	Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269\|PubMed:12052864, ECO:0000269\|PubMed:9305639}.
Q9Y6Y0	IVNS1ABP	S276	ochoa	Influenza virus NS1A-binding protein (NS1-BP) (NS1-binding protein) (Aryl hydrocarbon receptor-associated protein 3) (Kelch-like protein 39)	Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834). Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811). May play a role in mRNA nuclear export (PubMed:30538201). {ECO:0000250\|UniProtKB:Q920Q8, ECO:0000269\|PubMed:16582008, ECO:0000269\|PubMed:25619834, ECO:0000269\|PubMed:30538201, ECO:0000269\|PubMed:9696811}.; FUNCTION: (Microbial infection) Involved in the alternative splicing of influenza A virus M1 mRNA through interaction with HNRNPK, thereby facilitating the generation of viral M2 protein (PubMed:23825951, PubMed:9696811). The BTB and Kelch domains are required for splicing activity (PubMed:30538201). Promotes export of viral M mRNA and RNP via its interaction with mRNA export factor ALYREF (PubMed:30538201). {ECO:0000269\|PubMed:23825951, ECO:0000269\|PubMed:30538201, ECO:0000269\|PubMed:9696811}.
Q9Y6Y0	IVNS1ABP	S277	ochoa	Influenza virus NS1A-binding protein (NS1-BP) (NS1-binding protein) (Aryl hydrocarbon receptor-associated protein 3) (Kelch-like protein 39)	Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834). Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811). May play a role in mRNA nuclear export (PubMed:30538201). {ECO:0000250\|UniProtKB:Q920Q8, ECO:0000269\|PubMed:16582008, ECO:0000269\|PubMed:25619834, ECO:0000269\|PubMed:30538201, ECO:0000269\|PubMed:9696811}.; FUNCTION: (Microbial infection) Involved in the alternative splicing of influenza A virus M1 mRNA through interaction with HNRNPK, thereby facilitating the generation of viral M2 protein (PubMed:23825951, PubMed:9696811). The BTB and Kelch domains are required for splicing activity (PubMed:30538201). Promotes export of viral M mRNA and RNP via its interaction with mRNA export factor ALYREF (PubMed:30538201). {ECO:0000269\|PubMed:23825951, ECO:0000269\|PubMed:30538201, ECO:0000269\|PubMed:9696811}.
R4GMW8	BIVM-ERCC5	S772	ochoa	DNA excision repair protein ERCC-5	None
R4GMW8	BIVM-ERCC5	S986	ochoa	DNA excision repair protein ERCC-5	None
P14314	PRKCSH	S451	Sugiyama	Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH)	Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (By similarity). {ECO:0000250\|UniProtKB:O08795, ECO:0000269\|PubMed:10929008}.
P20618	PSMB1	S157	Sugiyama	Proteasome subunit beta type-1 (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain) (Proteasome subunit beta-6) (beta-6)	Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269\|PubMed:15244466, ECO:0000269\|PubMed:27176742, ECO:0000269\|PubMed:8610016}.
P36871	PGM1	S483	Sugiyama	Phosphoglucomutase-1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1)	Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:15378030, PubMed:25288802). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable) (PubMed:25288802). This enzyme participates in both the breakdown and synthesis of glucose (PubMed:17924679, PubMed:25288802). {ECO:0000269\|PubMed:15378030, ECO:0000269\|PubMed:17924679, ECO:0000269\|PubMed:25288802, ECO:0000305\|PubMed:15378030}.
P60174	TPI1	S204	Sugiyama	Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase)	Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000269\|PubMed:18562316}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250\|UniProtKB:P00939}.
Q9Y285	FARSA	S199	Sugiyama	Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (CML33) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS)	None
O14733	MAP2K7	S277	Sugiyama	Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (Stress-activated protein kinase kinase 4) (SAPK kinase 4) (SAPKK-4) (SAPKK4) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). {ECO:0000269\|PubMed:28111074, ECO:0000269\|PubMed:9312068, ECO:0000269\|PubMed:9372971, ECO:0000269\|PubMed:9535930, ECO:0000269\|Ref.5}.
Q14966	ZNF638	S375	EPSD\|PSP	Zinc finger protein 638 (Cutaneous T-cell lymphoma-associated antigen se33-1) (CTCL-associated antigen se33-1) (Nuclear protein 220) (Zinc finger matrin-like protein)	Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity). {ECO:0000250\|UniProtKB:Q61464, ECO:0000269\|PubMed:30487602, ECO:0000269\|PubMed:8647861}.
O75369	FLNB	S2492	Sugiyama	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
P05556	ITGB1	S509	Sugiyama	Integrin beta-1 (Fibronectin receptor subunit beta) (Glycoprotein IIa) (GPIIA) (VLA-4 subunit beta) (CD antigen CD29)	Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072). {ECO:0000250\|UniProtKB:P07228, ECO:0000250\|UniProtKB:P09055, ECO:0000269\|PubMed:10455171, ECO:0000269\|PubMed:12473654, ECO:0000269\|PubMed:12807887, ECO:0000269\|PubMed:16256741, ECO:0000269\|PubMed:17158881, ECO:0000269\|PubMed:18635536, ECO:0000269\|PubMed:18804435, ECO:0000269\|PubMed:19064666, ECO:0000269\|PubMed:21768292, ECO:0000269\|PubMed:23125415, ECO:0000269\|PubMed:24789099, ECO:0000269\|PubMed:25398877, ECO:0000269\|PubMed:29030430, ECO:0000269\|PubMed:31331973, ECO:0000269\|PubMed:33962943, ECO:0000269\|PubMed:35802072, ECO:0000269\|PubMed:7523423}.; FUNCTION: [Isoform 2]: Interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). {ECO:0000305\|PubMed:2249781}.; FUNCTION: [Isoform 5]: Isoform 5 displaces isoform 1 in striated muscles. {ECO:0000250\|UniProtKB:P09055}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. {ECO:0000269\|PubMed:8411387}.; FUNCTION: (Microbial infection) Acts as a receptor for Cytomegalovirus/HHV-5. {ECO:0000269\|PubMed:20660204}.; FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus/HHV-4. {ECO:0000269\|PubMed:17945327}.; FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human parvovirus B19. {ECO:0000269\|PubMed:12907437}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus. {ECO:0000269\|PubMed:12941907}.; FUNCTION: (Microbial infection) Acts as a receptor for Mammalian reovirus. {ECO:0000269\|PubMed:16501085}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000269\|PubMed:10397733}.; FUNCTION: (Microbial infection) Interacts with CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi (PubMed:32487760). Integrin ITGA3:ITGB1 may act as a receptor for R.delemar CotH7 in alveolar epithelial cells, which may be an early step in pulmonary mucormycosis disease progression (PubMed:32487760). {ECO:0000269\|PubMed:32487760}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A (nadA) of N.meningitidis. {ECO:0000305\|PubMed:21471204}.; FUNCTION: (Microbial infection) Facilitates rabies infection in a fibronectin-dependent manner and participates in rabies virus traffic after internalization. {ECO:0000269\|PubMed:31666383}.
P08195	SLC3A2	S292	Sugiyama	Amino acid transporter heavy chain SLC3A2 (4F2 cell-surface antigen heavy chain) (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98)	Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:11557028, PubMed:30867591, PubMed:33298890, PubMed:33758168, PubMed:34880232, PubMed:9751058, PubMed:9829974, PubMed:9878049). Heterodimers function as amino acids exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids (PubMed:10903140, PubMed:9829974). Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:34880232). SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, thyroid hormones and L-DOPA (PubMed:10574970, PubMed:11389679, PubMed:11557028, PubMed:11564694, PubMed:11742812, PubMed:12117417, PubMed:12225859, PubMed:12716892, PubMed:15980244, PubMed:30867591, PubMed:33298890, PubMed:33758168). SLC3A2 is essential for plasma membrane localization, stability, and the transport activity of SLC7A5 and SLC7A8 (PubMed:10391915, PubMed:10574970, PubMed:11311135, PubMed:15769744, PubMed:33066406). When associated with LAPTM4B, the heterodimer SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression (PubMed:11121428, PubMed:15625115). {ECO:0000250\|UniProtKB:P63115, ECO:0000269\|PubMed:10391915, ECO:0000269\|PubMed:10574970, ECO:0000269\|PubMed:10903140, ECO:0000269\|PubMed:11121428, ECO:0000269\|PubMed:11311135, ECO:0000269\|PubMed:11389679, ECO:0000269\|PubMed:11557028, ECO:0000269\|PubMed:11564694, ECO:0000269\|PubMed:11742812, ECO:0000269\|PubMed:12117417, ECO:0000269\|PubMed:12225859, ECO:0000269\|PubMed:12716892, ECO:0000269\|PubMed:15625115, ECO:0000269\|PubMed:15769744, ECO:0000269\|PubMed:15980244, ECO:0000269\|PubMed:25998567, ECO:0000269\|PubMed:30867591, ECO:0000269\|PubMed:33066406, ECO:0000269\|PubMed:33298890, ECO:0000269\|PubMed:33758168, ECO:0000269\|PubMed:34880232, ECO:0000269\|PubMed:9751058, ECO:0000269\|PubMed:9829974, ECO:0000269\|PubMed:9878049}.; FUNCTION: (Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis. {ECO:0000269\|PubMed:30341327}.; FUNCTION: (Microbial infection) Acts as a receptor for malaria parasite Plasmodium vivax (Thai isolate) in immature red blood cells. {ECO:0000269\|PubMed:34294905}.
P27695	APEX1	S135	Sugiyama	DNA repair nuclease/redox regulator APEX1 (EC 3.1.11.2) (EC 3.1.21.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (DNA-(apurinic or apyrimidinic site) endonuclease) (Redox factor-1) (REF-1) [Cleaved into: DNA repair nuclease/redox regulator APEX1, mitochondrial]	Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors (PubMed:11118054, PubMed:11452037, PubMed:15831793, PubMed:18439621, PubMed:18579163, PubMed:21762700, PubMed:24079850, PubMed:8355688, PubMed:9108029, PubMed:9560228). Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules (PubMed:15380100, PubMed:16617147, PubMed:18439621, PubMed:19123919, PubMed:19188445, PubMed:19934257, PubMed:20699270, PubMed:21762700, PubMed:24079850, PubMed:8932375, PubMed:8995436, PubMed:9804799). Operates at switch sites of immunoglobulin (Ig) constant regions where it mediates Ig isotype class switch recombination. Processes AP sites induced by successive action of AICDA and UNG. Generates staggered nicks in opposite DNA strands resulting in the formation of double-strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity). Has 3'-5' exodeoxyribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER (PubMed:11832948, PubMed:1719477). Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate and 8-oxoguanine) blocking the 3' side of DNA strand breaks (PubMed:15831793, PubMed:7516064). Also acts as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression (PubMed:19188445, PubMed:19401441, PubMed:21762700). Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB (PubMed:9207062). Exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR (PubMed:10023679, PubMed:11118054, PubMed:11452037, PubMed:18579163, PubMed:8355688, PubMed:9108029). Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression (PubMed:11809897, PubMed:14633989, PubMed:8621488). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance (PubMed:18809583). Plays a role in protection from granzyme-mediated cellular repair leading to cell death (PubMed:18179823). Binds DNA and RNA. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA (PubMed:19188445, PubMed:19401441, PubMed:20699270). {ECO:0000250\|UniProtKB:P28352, ECO:0000269\|PubMed:10023679, ECO:0000269\|PubMed:11118054, ECO:0000269\|PubMed:11452037, ECO:0000269\|PubMed:11809897, ECO:0000269\|PubMed:11832948, ECO:0000269\|PubMed:12524539, ECO:0000269\|PubMed:14633989, ECO:0000269\|PubMed:15380100, ECO:0000269\|PubMed:15831793, ECO:0000269\|PubMed:16617147, ECO:0000269\|PubMed:1719477, ECO:0000269\|PubMed:18179823, ECO:0000269\|PubMed:18439621, ECO:0000269\|PubMed:18579163, ECO:0000269\|PubMed:18809583, ECO:0000269\|PubMed:19123919, ECO:0000269\|PubMed:19188445, ECO:0000269\|PubMed:19401441, ECO:0000269\|PubMed:19934257, ECO:0000269\|PubMed:20699270, ECO:0000269\|PubMed:21496894, ECO:0000269\|PubMed:21762700, ECO:0000269\|PubMed:24079850, ECO:0000269\|PubMed:7516064, ECO:0000269\|PubMed:8355688, ECO:0000269\|PubMed:8621488, ECO:0000269\|PubMed:8932375, ECO:0000269\|PubMed:8995436, ECO:0000269\|PubMed:9108029, ECO:0000269\|PubMed:9207062, ECO:0000269\|PubMed:9560228, ECO:0000269\|PubMed:9804799}.
Q08209	PPP3CA	S498	Sugiyama	Protein phosphatase 3 catalytic subunit alpha (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calcineurin A alpha) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha) (Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform)	Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (PubMed:15671020, PubMed:18838687, PubMed:19154138, PubMed:23468591, PubMed:30254215). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (PubMed:17498738, PubMed:17502104, PubMed:22343722, PubMed:23468591, PubMed:27974827). In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (PubMed:15671020). In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (PubMed:18838687). Positively regulates the CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138). In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation (PubMed:26248042). Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32 (PubMed:19154138). May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (PubMed:30611118). Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation (PubMed:33691586). Required for postnatal development of the nephrogenic zone and superficial glomeruli in the kidneys, cell cycle homeostasis in the nephrogenic zone, and ultimately normal kidney function (By similarity). Plays a role in intracellular AQP2 processing and localization to the apical membrane in the kidney, may thereby be required for efficient kidney filtration (By similarity). Required for secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic acid via formation of secretory vesicles in the submandibular glands (By similarity). Required for calcineurin activity and homosynaptic depotentiation in the hippocampus (By similarity). Required for normal differentiation and survival of keratinocytes and therefore required for epidermis superstructure formation (By similarity). Positively regulates osteoblastic bone formation, via promotion of osteoblast differentiation (By similarity). Positively regulates osteoclast differentiation, potentially via NFATC1 signaling (By similarity). May play a role in skeletal muscle fiber type specification, potentially via NFATC1 signaling (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). Required for antigen-specific T-cell proliferation response (By similarity). Dephosphorylates KLHL3, promoting the interaction between KLHL3 and WNK4 and subsequent degradation of WNK4 (PubMed:30718414). Negatively regulates SLC9A1 activity (PubMed:31375679). {ECO:0000250\|UniProtKB:P48452, ECO:0000250\|UniProtKB:P63328, ECO:0000250\|UniProtKB:P63329, ECO:0000269\|PubMed:15671020, ECO:0000269\|PubMed:17498738, ECO:0000269\|PubMed:17502104, ECO:0000269\|PubMed:18838687, ECO:0000269\|PubMed:19154138, ECO:0000269\|PubMed:22343722, ECO:0000269\|PubMed:23468591, ECO:0000269\|PubMed:26248042, ECO:0000269\|PubMed:27974827, ECO:0000269\|PubMed:30254215, ECO:0000269\|PubMed:30611118, ECO:0000269\|PubMed:30718414, ECO:0000269\|PubMed:31375679, ECO:0000269\|PubMed:33691586}.
Q16881	TXNRD1	S335	Sugiyama	Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Peroxidase TXNRD1) (EC 1.11.1.2) (Thioredoxin reductase TR1)	Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437). {ECO:0000269\|PubMed:10849437, ECO:0000269\|PubMed:8577704, ECO:0000305\|PubMed:17512005}.; FUNCTION: [Isoform 1]: Induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. {ECO:0000269\|PubMed:18042542, ECO:0000269\|PubMed:8577704}.; FUNCTION: [Isoform 4]: Enhances the transcriptional activity of estrogen receptors ESR1 and ESR2. {ECO:0000269\|PubMed:15199063}.; FUNCTION: [Isoform 5]: Enhances the transcriptional activity of the estrogen receptor ESR2 only (PubMed:15199063). Mediates cell death induced by a combination of interferon-beta and retinoic acid (PubMed:9774665). {ECO:0000269\|PubMed:15199063, ECO:0000269\|PubMed:9774665}.
Q6PKG0	LARP1	S830	Sugiyama	La-related protein 1 (La ribonucleoprotein domain family member 1)	RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543). {ECO:0000269\|PubMed:20430826, ECO:0000269\|PubMed:23711370, ECO:0000269\|PubMed:24532714, ECO:0000269\|PubMed:25940091, ECO:0000269\|PubMed:26206669, ECO:0000269\|PubMed:28379136, ECO:0000269\|PubMed:28650797, ECO:0000269\|PubMed:28673543, ECO:0000269\|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269\|PubMed:26735137}.
Q7LBC6	KDM3B	S1259	Sugiyama	Lysine-specific demethylase 3B (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3B)	Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269\|PubMed:16603237}.
Q7Z417	NUFIP2	S592	Sugiyama	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
O43353	RIPK2	S180	EPSD\|PSP	Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)	Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269\|PubMed:14638696, ECO:0000269\|PubMed:17054981, ECO:0000269\|PubMed:17562858, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:21123652, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:22607974, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:28545134, ECO:0000269\|PubMed:28656966, ECO:0000269\|PubMed:29452636, ECO:0000269\|PubMed:30026309, ECO:0000269\|PubMed:30279485, ECO:0000269\|PubMed:30478312, ECO:0000269\|PubMed:9575181, ECO:0000269\|PubMed:9642260}.
O60566	BUB1B	S697	Sugiyama	Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)	Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269\|PubMed:10477750, ECO:0000269\|PubMed:11702782, ECO:0000269\|PubMed:14706340, ECO:0000269\|PubMed:15020684, ECO:0000269\|PubMed:19411850, ECO:0000269\|PubMed:19503101}.
O14974	PPP1R12A	S894	Sugiyama	Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269\|PubMed:18477460, ECO:0000269\|PubMed:19245366, ECO:0000269\|PubMed:20354225}.
O75676	RPS6KA4	S700	Sugiyama	Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (Ribosomal protein kinase B) (RSKB)	Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. {ECO:0000269\|PubMed:11035004, ECO:0000269\|PubMed:12773393, ECO:0000269\|PubMed:9792677}.
O94804	STK10	S444	Sugiyama	Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269\|PubMed:11903060, ECO:0000269\|PubMed:12639966, ECO:0000269\|PubMed:19255442}.
P14625	HSP90B1	S680	Sugiyama	Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog)	ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269\|PubMed:11584270, ECO:0000269\|PubMed:23572575, ECO:0000269\|PubMed:32272059, ECO:0000269\|PubMed:39509507}.
P00519	ABL1	S559	Sugiyama	Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)	Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 also acts as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250\|UniProtKB:P00520, ECO:0000269\|PubMed:10391250, ECO:0000269\|PubMed:11971963, ECO:0000269\|PubMed:12379650, ECO:0000269\|PubMed:12531427, ECO:0000269\|PubMed:12672821, ECO:0000269\|PubMed:15031292, ECO:0000269\|PubMed:15556646, ECO:0000269\|PubMed:15657060, ECO:0000269\|PubMed:15886098, ECO:0000269\|PubMed:16424036, ECO:0000269\|PubMed:16678104, ECO:0000269\|PubMed:16943190, ECO:0000269\|PubMed:17306540, ECO:0000269\|PubMed:17623672, ECO:0000269\|PubMed:18328268, ECO:0000269\|PubMed:18945674, ECO:0000269\|PubMed:19891780, ECO:0000269\|PubMed:20357770, ECO:0000269\|PubMed:20417104, ECO:0000269\|PubMed:22810897, ECO:0000269\|PubMed:28428613, ECO:0000269\|PubMed:9037071, ECO:0000269\|PubMed:9144171, ECO:0000269\|PubMed:9461559}.
Q9H9S0	NANOG	S71	PSP	Homeobox protein NANOG (Homeobox transcription factor Nanog) (hNanog)	Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Binds to the POU5F1/OCT4 promoter (PubMed:25825768). Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation. {ECO:0000269\|PubMed:15983365, ECO:0000269\|PubMed:16000880, ECO:0000269\|PubMed:16391521, ECO:0000269\|PubMed:25825768}.
Q9UPT8	ZC3H4	S146	Sugiyama	Zinc finger CCCH domain-containing protein 4	RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269\|PubMed:33767452, ECO:0000269\|PubMed:33913806}.
Q13242	SRSF9	S178	Sugiyama	Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:10196175, ECO:0000269\|PubMed:11875052, ECO:0000269\|PubMed:12024014, ECO:0000269\|PubMed:12604611, ECO:0000269\|PubMed:15009090, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:15695522, ECO:0000269\|PubMed:7556075}.
P12268	IMPDH2	S432	Sugiyama	Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (Inosine-5'-monophosphate dehydrogenase type II) (IMP dehydrogenase II) (IMPDH-II)	Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (PubMed:7763314, PubMed:7903306). Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism (PubMed:14766016). It may also have a role in the development of malignancy and the growth progression of some tumors. {ECO:0000269\|PubMed:14766016, ECO:0000269\|PubMed:7763314, ECO:0000269\|PubMed:7903306}.
Q8TDD1	DDX54	S587	Sugiyama	ATP-dependent RNA helicase DDX54 (EC 3.6.4.13) (ATP-dependent RNA helicase DP97) (DEAD box RNA helicase 97 kDa) (DEAD box protein 54)	Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors. {ECO:0000269\|PubMed:12466272}.
Q9HC52	CBX8	S196	PSP	Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (hPc3) (Rectachrome 1)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269\|PubMed:21282530}.
P30086	PEBP1	S104	Sugiyama	Phosphatidylethanolamine-binding protein 1 (PEBP-1) (HCNPpp) (Neuropolypeptide h3) (Prostatic-binding protein) (Raf kinase inhibitor protein) (RKIP) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)]	Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. {ECO:0000250, ECO:0000269\|PubMed:18294816}.; FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). {ECO:0000250}.
P24046	GABRR1	S440	SIGNOR\|iPTMNet\|EPSD	Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABAAR subunit rho-1) (GABA(C) receptor)	Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain (PubMed:37659407). Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (PubMed:37659407). When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:37659407). Rho-1 subunits are primarily expressed in retina where rho-1-containing GABAARs may play a role in retinal neurotransmission (PubMed:1849271). Rho-1 GABAARs are also involved in neuronal tonic (extrasynaptic) and phasic (synaptic) transmission in the Purkinje neurons of the cerebellum (By similarity). Rho-1 GABAARs may also contribute to the regulation of glial development in the cerebellum by controlling extrasynaptic transmission (By similarity). {ECO:0000250\|UniProtKB:P56475, ECO:0000269\|PubMed:1849271, ECO:0000269\|PubMed:37659407}.
P35368	ADRA1B	S412	SIGNOR\|iPTMNet\|EPSD	Alpha-1B adrenergic receptor (Alpha-1B adrenoreceptor) (Alpha-1B adrenoceptor)	This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269\|PubMed:18802028, ECO:0000269\|PubMed:22120526}.
P19525	EIF2AK2	S462	Sugiyama	Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)	IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250\|UniProtKB:Q03963, ECO:0000269\|PubMed:10848580, ECO:0000269\|PubMed:11836380, ECO:0000269\|PubMed:15121867, ECO:0000269\|PubMed:15229216, ECO:0000269\|PubMed:18835251, ECO:0000269\|PubMed:19189853, ECO:0000269\|PubMed:19229320, ECO:0000269\|PubMed:19507191, ECO:0000269\|PubMed:19840259, ECO:0000269\|PubMed:20171114, ECO:0000269\|PubMed:20395957, ECO:0000269\|PubMed:20685959, ECO:0000269\|PubMed:21072047, ECO:0000269\|PubMed:21123651, ECO:0000269\|PubMed:21710204, ECO:0000269\|PubMed:22214662, ECO:0000269\|PubMed:22381929, ECO:0000269\|PubMed:22801494, ECO:0000269\|PubMed:22948139, ECO:0000269\|PubMed:23084476, ECO:0000269\|PubMed:23115276, ECO:0000269\|PubMed:23229543, ECO:0000269\|PubMed:23372823, ECO:0000269\|PubMed:23399035, ECO:0000269\|PubMed:32197074}.
P29401	TKT	S449	Sugiyama	Transketolase (TK) (EC 2.2.1.1)	Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000269\|PubMed:27259054}.
Q9UHX1	PUF60	S238	Sugiyama	Poly(U)-binding-splicing factor PUF60 (60 kDa poly(U)-binding-splicing factor) (FUSE-binding protein-interacting repressor) (FBP-interacting repressor) (Ro-binding protein 1) (RoBP1) (Siah-binding protein 1) (Siah-BP1)	DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA. {ECO:0000269\|PubMed:10606266, ECO:0000269\|PubMed:10882074, ECO:0000269\|PubMed:11239393, ECO:0000269\|PubMed:16452196, ECO:0000269\|PubMed:16628215, ECO:0000269\|PubMed:17579712}.
Q9UPT8	ZC3H4	S143	Sugiyama	Zinc finger CCCH domain-containing protein 4	RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269\|PubMed:33767452, ECO:0000269\|PubMed:33913806}.
Q13011	ECH1	S43	Sugiyama	Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC 5.3.3.-)	Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA. {ECO:0000250\|UniProtKB:Q62651}.
Q96S66	CLCC1	S65	Sugiyama	Chloride channel CLIC-like protein 1 (ER anion channel 1) (ERAC1) (Mid-1-related chloride channel protein)	Anion-selective channel with Ca(2+)-dependent and voltage-independent gating. Permeable to small monovalent anions with selectivity for bromide > chloride > nitrate > fluoride (By similarity). Operates in the endoplasmic reticulum (ER) membrane where it mediates chloride efflux to compensate for the loss of positive charges from the ER lumen upon Ca(2+) release. Contributes to the maintenance of ER Ca(2+) pools and activation of unfolded protein response to prevent accumulation of misfolded proteins in the ER lumen. Particularly involved in ER homeostasis mechanisms underlying motor neurons and retinal photoreceptors survival (By similarity) (PubMed:25698737, PubMed:30157172, PubMed:37142673). {ECO:0000250\|UniProtKB:Q99LI2, ECO:0000269\|PubMed:25698737, ECO:0000269\|PubMed:30157172, ECO:0000269\|PubMed:37142673}.
P41219	PRPH	S59	SIGNOR	Peripherin (Neurofilament 4)	Class-III neuronal intermediate filament protein (By similarity). May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form a filamentous network (PubMed:15322088, PubMed:15446584). Assembly of the neuronal intermediate filaments may be regulated by RAB7A (By similarity). Plays a role in the development of unmyelinated sensory neurons (By similarity). May be involved in axon elongation and axon regeneration after injury (By similarity). Inhibits neurite extension in type II spiral ganglion neurons in the cochlea (By similarity). {ECO:0000250\|UniProtKB:P15331, ECO:0000250\|UniProtKB:P21807, ECO:0000269\|PubMed:15322088, ECO:0000269\|PubMed:15446584}.
P36896	ACVR1B	S174	Sugiyama	Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2)	Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269\|PubMed:12364468, ECO:0000269\|PubMed:12639945, ECO:0000269\|PubMed:18039968, ECO:0000269\|PubMed:20226172, ECO:0000269\|PubMed:8196624, ECO:0000269\|PubMed:9032295, ECO:0000269\|PubMed:9892009}.
Q9H1A4	ANAPC1	S323	Sugiyama	Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
P11308	ERG	S45	EPSD	Transcriptional regulator ERG (Transforming protein ERG)	Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
O75821	EIF3G	S223	Sugiyama	Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44)	RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255\|HAMAP-Rule:MF_03006, ECO:0000269\|PubMed:17581632, ECO:0000269\|PubMed:25849773, ECO:0000269\|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269\|PubMed:18056426}.
P30101	PDIA3	S169	Sugiyama	Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60)	Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323). {ECO:0000269\|PubMed:11825568, ECO:0000269\|PubMed:16193070, ECO:0000269\|PubMed:27897272, ECO:0000269\|PubMed:35948544, ECO:0000269\|PubMed:36104323, ECO:0000269\|PubMed:7487104}.
Q04760	GLO1	S120	Sugiyama	Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase)	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:20454679, PubMed:23122816, PubMed:9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed:19199007). Required for normal osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:Q9CPU0, ECO:0000269\|PubMed:19199007, ECO:0000269\|PubMed:20454679, ECO:0000269\|PubMed:23122816, ECO:0000269\|PubMed:9705294}.
Q8WYR1	PIK3R5	S446	Sugiyama	Phosphoinositide 3-kinase regulatory subunit 5 (PI3-kinase regulatory subunit 5) (PI3-kinase p101 subunit) (Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit) (PtdIns-3-kinase regulatory subunit) (Protein FOAP-2) (PtdIns-3-kinase p101) (p101-PI3K)	Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity). {ECO:0000250}.
O15055	PER2	S671	iPTMNet	Period circadian protein homolog 2 (hPER2) (Circadian clock protein PERIOD 2)	Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250\|UniProtKB:O54943}.
O15055	PER2	S674	iPTMNet	Period circadian protein homolog 2 (hPER2) (Circadian clock protein PERIOD 2)	Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250\|UniProtKB:O54943}.
P56645	PER3	S628	SIGNOR\|iPTMNet	Period circadian protein homolog 3 (hPER3) (Cell growth-inhibiting gene 13 protein) (Circadian clock protein PERIOD 3)	Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. {ECO:0000269\|PubMed:17346965, ECO:0000269\|PubMed:19716732, ECO:0000269\|PubMed:24439663, ECO:0000269\|PubMed:24577121, ECO:0000269\|PubMed:26903630}.
P56645	PER3	S634	SIGNOR\|iPTMNet	Period circadian protein homolog 3 (hPER3) (Cell growth-inhibiting gene 13 protein) (Circadian clock protein PERIOD 3)	Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. {ECO:0000269\|PubMed:17346965, ECO:0000269\|PubMed:19716732, ECO:0000269\|PubMed:24439663, ECO:0000269\|PubMed:24577121, ECO:0000269\|PubMed:26903630}.
P10636	MAPT	S525	EPSD	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
O60563	CCNT1	S433	Sugiyama	Cyclin-T1 (CycT1) (Cyclin-T)	Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539). {ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:29849146, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:35393539}.; FUNCTION: (Microbial infection) In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269\|PubMed:10329125, ECO:0000269\|PubMed:10329126}.
P51617	IRAK1	S607	Sugiyama	Interleukin-1 receptor-associated kinase 1 (IRAK-1) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. {ECO:0000269\|PubMed:11397809, ECO:0000269\|PubMed:12860405, ECO:0000269\|PubMed:14684752, ECO:0000269\|PubMed:15084582, ECO:0000269\|PubMed:15465816, ECO:0000269\|PubMed:15767370, ECO:0000269\|PubMed:17997719, ECO:0000269\|PubMed:20400509}.
P51957	NEK4	S467	Sugiyama	Serine/threonine-protein kinase Nek4 (EC 2.7.11.1) (Never in mitosis A-related kinase 4) (NimA-related protein kinase 4) (Serine/threonine-protein kinase 2) (Serine/threonine-protein kinase NRK2)	Protein kinase that seems to act exclusively upon threonine residues (By similarity). Required for normal entry into proliferative arrest after a limited number of cell divisions, also called replicative senescence. Required for normal cell cycle arrest in response to double-stranded DNA damage. {ECO:0000250\|UniProtKB:Q9Z1J2, ECO:0000269\|PubMed:22851694}.
Q15785	TOMM34	S51	Sugiyama	Mitochondrial import receptor subunit TOM34 (hTom34) (Translocase of outer membrane 34 kDa subunit)	Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state. {ECO:0000269\|PubMed:10101285, ECO:0000269\|PubMed:11913975, ECO:0000269\|PubMed:9324309}.
P53667	LIMK1	S313	Sugiyama	LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11832213, PubMed:12807904, PubMed:15660133, PubMed:16230460, PubMed:18028908, PubMed:22328514, PubMed:23633677). Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop (PubMed:10436159). LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly (PubMed:18028908). Stimulates axonal outgrowth and may be involved in brain development (PubMed:18028908). {ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:11832213, ECO:0000269\|PubMed:12807904, ECO:0000269\|PubMed:15660133, ECO:0000269\|PubMed:16230460, ECO:0000269\|PubMed:18028908, ECO:0000269\|PubMed:22328514, ECO:0000269\|PubMed:23633677}.; FUNCTION: [Isoform 3]: Has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1). {ECO:0000269\|PubMed:10196227}.
Q15751	HERC1	S3244	Sugiyama	Probable E3 ubiquitin-protein ligase HERC1 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 1) (HECT-type E3 ubiquitin transferase HERC1) (p532) (p619)	Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269\|PubMed:15642342, ECO:0000269\|PubMed:8861955, ECO:0000269\|PubMed:9233772}.
P18846	ATF1	S44	SIGNOR	Cyclic AMP-dependent transcription factor ATF-1 (cAMP-dependent transcription factor ATF-1) (Activating transcription factor 1) (Protein TREB36)	This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269\|PubMed:18794154, ECO:0000269\|PubMed:20980392}.
Q32M45	ANO4	S849	Sugiyama	Anoctamin-4 (Transmembrane protein 16D)	Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity (By similarity). {ECO:0000250\|UniProtKB:Q8C5H1}.
Q9UQ80	PA2G4	S47	Sugiyama	Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1)	May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250\|UniProtKB:P50580, ECO:0000250\|UniProtKB:Q6AYD3, ECO:0000269\|PubMed:11268000, ECO:0000269\|PubMed:12682367, ECO:0000269\|PubMed:15064750, ECO:0000269\|PubMed:15583694, ECO:0000269\|PubMed:16832058}.
Q9Y262	EIF3L	S255	Sugiyama	Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein)	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255\|HAMAP-Rule:MF_03011, ECO:0000269\|PubMed:17581632, ECO:0000269\|PubMed:25849773, ECO:0000269\|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269\|PubMed:18056426}.
P49792	RANBP2	S2810	Sugiyama	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P39019	RPS19	S96	Sugiyama	Small ribosomal subunit protein eS19 (40S ribosomal protein S19)	Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Required for pre-rRNA processing and maturation of 40S ribosomal subunits (PubMed:16990592). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:16990592, ECO:0000269\|PubMed:23636399, ECO:0000269\|PubMed:34516797}.
Q12778	FOXO1	S218	PSP	Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)	Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). {ECO:0000250\|UniProtKB:A4L7N3, ECO:0000250\|UniProtKB:G3V7R4, ECO:0000250\|UniProtKB:Q9R1E0, ECO:0000269\|PubMed:10358076, ECO:0000269\|PubMed:12228231, ECO:0000269\|PubMed:15220471, ECO:0000269\|PubMed:15890677, ECO:0000269\|PubMed:17024043, ECO:0000269\|PubMed:18356527, ECO:0000269\|PubMed:19221179, ECO:0000269\|PubMed:19483080, ECO:0000269\|PubMed:20543840, ECO:0000269\|PubMed:21245099, ECO:0000269\|PubMed:31063815}.
Q13163	MAP2K5	S139	Sugiyama	Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)	Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250\|UniProtKB:Q62862, ECO:0000269\|PubMed:7759517, ECO:0000269\|PubMed:9384584}.
P08151	GLI1	S550	GPS6	Zinc finger protein GLI1 (Glioma-associated oncogene) (Oncogene GLI)	Acts as a transcriptional activator (PubMed:10806483, PubMed:19706761, PubMed:19878745, PubMed:24076122, PubMed:24217340, PubMed:24311597). Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456, PubMed:24217340, PubMed:8378770). Regulates the transcription of specific genes during normal development (PubMed:19706761). Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling (PubMed:19706761, PubMed:28973407). Plays a role in cell proliferation and differentiation via its role in SHH signaling (PubMed:11238441, PubMed:28973407). {ECO:0000269\|PubMed:10806483, ECO:0000269\|PubMed:11238441, ECO:0000269\|PubMed:19706761, ECO:0000269\|PubMed:19878745, ECO:0000269\|PubMed:2105456, ECO:0000269\|PubMed:24076122, ECO:0000269\|PubMed:24217340, ECO:0000269\|PubMed:24311597, ECO:0000269\|PubMed:28973407, ECO:0000269\|PubMed:8378770}.; FUNCTION: [Isoform 2]: Acts as a transcriptional activator, but activates a different set of genes than isoform 1. Activates expression of CD24, unlike isoform 1. Mediates SHH signaling. Promotes cancer cell migration. {ECO:0000269\|PubMed:19706761}.
P08151	GLI1	S608	GPS6	Zinc finger protein GLI1 (Glioma-associated oncogene) (Oncogene GLI)	Acts as a transcriptional activator (PubMed:10806483, PubMed:19706761, PubMed:19878745, PubMed:24076122, PubMed:24217340, PubMed:24311597). Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456, PubMed:24217340, PubMed:8378770). Regulates the transcription of specific genes during normal development (PubMed:19706761). Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling (PubMed:19706761, PubMed:28973407). Plays a role in cell proliferation and differentiation via its role in SHH signaling (PubMed:11238441, PubMed:28973407). {ECO:0000269\|PubMed:10806483, ECO:0000269\|PubMed:11238441, ECO:0000269\|PubMed:19706761, ECO:0000269\|PubMed:19878745, ECO:0000269\|PubMed:2105456, ECO:0000269\|PubMed:24076122, ECO:0000269\|PubMed:24217340, ECO:0000269\|PubMed:24311597, ECO:0000269\|PubMed:28973407, ECO:0000269\|PubMed:8378770}.; FUNCTION: [Isoform 2]: Acts as a transcriptional activator, but activates a different set of genes than isoform 1. Activates expression of CD24, unlike isoform 1. Mediates SHH signaling. Promotes cancer cell migration. {ECO:0000269\|PubMed:19706761}.
Q9Y4W2	LAS1L	S642	Sugiyama	Ribosomal biogenesis protein LAS1L (Endoribonuclease LAS1L) (EC 3.1.-.-) (Protein LAS1 homolog)	Required for the synthesis of the 60S ribosomal subunit and maturation of the 28S rRNA (PubMed:20647540). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Required for the efficient pre-rRNA processing at both ends of internal transcribed spacer 2 (ITS2) (PubMed:22083961). {ECO:0000269\|PubMed:20647540, ECO:0000269\|PubMed:22083961, ECO:0000269\|PubMed:22872859}.
Q7LBC6	KDM3B	S816	Sugiyama	Lysine-specific demethylase 3B (EC 1.14.11.65) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA) ([histone H3]-dimethyl-L-lysine(9) demethylase 3B)	Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269\|PubMed:16603237}.
O43290	SART1	S117	Sugiyama	U4/U6.U5 tri-snRNP-associated protein 1 (SNU66 homolog) (hSnu66) (Squamous cell carcinoma antigen recognized by T-cells 1) (SART-1) (hSART-1) (U4/U6.U5 tri-snRNP-associated 110 kDa protein) (allergen Hom s 1)	Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269\|PubMed:11350945, ECO:0000269\|PubMed:25092792}.
Q15139	PRKD1	S225	Sugiyama	Serine/threonine-protein kinase D1 (EC 2.7.11.13) (Protein kinase C mu type) (Protein kinase D) (nPKC-D1) (nPKC-mu)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response (PubMed:10764790, PubMed:12505989, PubMed:12637538, PubMed:17442957, PubMed:18509061, PubMed:19135240, PubMed:19211839). Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation (PubMed:10523301). Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1 (PubMed:12505989). Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2 (PubMed:18509061). In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling (PubMed:18332134). Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation (PubMed:19211839). In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents (PubMed:10764790). In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines (PubMed:17442957). Acts as an activator of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (By similarity). May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor (PubMed:15471852). Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells (PubMed:24623306). Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (By similarity). {ECO:0000250\|UniProtKB:Q62101, ECO:0000269\|PubMed:10523301, ECO:0000269\|PubMed:10764790, ECO:0000269\|PubMed:12505989, ECO:0000269\|PubMed:12637538, ECO:0000269\|PubMed:15471852, ECO:0000269\|PubMed:17442957, ECO:0000269\|PubMed:18332134, ECO:0000269\|PubMed:18509061, ECO:0000269\|PubMed:19135240, ECO:0000269\|PubMed:19211839, ECO:0000269\|PubMed:24623306}.
O00267	SUPT5H	S818	Sugiyama	Transcription elongation factor SPT5 (hSPT5) (DRB sensitivity-inducing factor 160 kDa subunit) (DSIF p160) (DRB sensitivity-inducing factor large subunit) (DSIF large subunit) (Tat-cotransactivator 1 protein) (Tat-CT1 protein)	Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A (PubMed:10075709, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter (PubMed:10075709, PubMed:10199401, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II (PubMed:16214896). TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme (PubMed:16214896). Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (PubMed:16214896). Following phosphorylation by CDK9, DSIF can also positively regulate transcriptional elongation (PubMed:16427012). Required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat (PubMed:10393184, PubMed:10454543, PubMed:11809800, PubMed:9514752). DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences (PubMed:11112772, PubMed:14701750). {ECO:0000269\|PubMed:10075709, ECO:0000269\|PubMed:10199401, ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:10421630, ECO:0000269\|PubMed:10454543, ECO:0000269\|PubMed:10757782, ECO:0000269\|PubMed:10912001, ECO:0000269\|PubMed:11112772, ECO:0000269\|PubMed:11553615, ECO:0000269\|PubMed:11809800, ECO:0000269\|PubMed:12653964, ECO:0000269\|PubMed:12718890, ECO:0000269\|PubMed:14701750, ECO:0000269\|PubMed:15136722, ECO:0000269\|PubMed:15380072, ECO:0000269\|PubMed:16214896, ECO:0000269\|PubMed:16427012, ECO:0000269\|PubMed:9450929, ECO:0000269\|PubMed:9514752, ECO:0000269\|PubMed:9857195}.
Q15349	RPS6KA2	S366	Sugiyama	Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells. {ECO:0000269\|PubMed:16878154, ECO:0000269\|PubMed:7623830}.
Q7RTN6	STRADA	S52	Sugiyama	STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) (Serologically defined breast cancer antigen NY-BR-96)	Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation. {ECO:0000269\|PubMed:12805220, ECO:0000269\|PubMed:14517248, ECO:0000269\|PubMed:19892943}.
O14734	ACOT8	S111	Sugiyama	Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (HIV-Nef-associated acyl-CoA thioesterase) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Thioesterase II) (hACTE-III) (hACTEIII) (hTE)	Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:15194431, PubMed:9153233, PubMed:9299485). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:9153233, PubMed:9299485). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431). {ECO:0000250\|UniProtKB:P58137, ECO:0000269\|PubMed:15194431, ECO:0000269\|PubMed:9153233, ECO:0000269\|PubMed:9299485}.; FUNCTION: (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233). {ECO:0000269\|PubMed:9153233}.
Q07157	TJP1	S1071	Sugiyama	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q6P0Q8	MAST2	S817	Sugiyama	Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1)	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.
P43243	MATR3	S240	Sugiyama	Matrin-3	May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:11525732, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32245947}.
Q9Y6D6	ARFGEF1	S1575	Sugiyama	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
P05362	ICAM1	S49	Sugiyama	Intercellular adhesion molecule 1 (ICAM-1) (Major group rhinovirus receptor) (CD antigen CD54)	ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. {ECO:0000269\|PubMed:11173916, ECO:0000269\|PubMed:17875742}.; FUNCTION: (Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins. {ECO:0000269\|PubMed:1968231, ECO:0000269\|PubMed:2538243}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus A21 capsid proteins. {ECO:0000269\|PubMed:11160747, ECO:0000269\|PubMed:16004874, ECO:0000269\|PubMed:9539703}.; FUNCTION: (Microbial infection) Upon Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, is degraded by viral E3 ubiquitin ligase MIR2, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes and NK cell. {ECO:0000269\|PubMed:11413168}.
Q8NE71	ABCF1	S293	Sugiyama	ATP-binding cassette sub-family F member 1 (ATP-binding cassette 50) (TNF-alpha-stimulated ABC protein)	Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. {ECO:0000269\|PubMed:19570978}.
Q9UGV2	NDRG3	S344	Sugiyama	Protein NDRG3 (N-myc downstream-regulated gene 3 protein)	None
Q99558	MAP3K14	S826	Sugiyama	Mitogen-activated protein kinase kinase kinase 14 (EC 2.7.11.25) (NF-kappa-beta-inducing kinase) (HsNIK) (Serine/threonine-protein kinase NIK)	Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Phosphorylates CHUK/IKKA, thereby promoting proteolytic processing of NFKB2/P100, which leads to NF-kappa-B activation via the non-canonical pathway (PubMed:25406581, PubMed:29230214). Has an essential role in the non-canonical NF-kappa-B signaling that regulates genes encoding molecules involved in B-cell survival, lymphoid organogenesis, and immune response (PubMed:25406581). Could act in a receptor-selective manner. {ECO:0000269\|PubMed:15084608, ECO:0000269\|PubMed:25406581}.
Q9BYT3	STK33	S474	Sugiyama	Serine/threonine-protein kinase 33 (EC 2.7.11.1)	Serine/threonine protein kinase required for spermatid differentiation and male fertility (PubMed:37146716, PubMed:38781365). Promotes sperm flagella assembly during spermatogenesis by mediating phosphorylation of fibrous sheath proteins AKAP3 and AKAP4 (By similarity). Also phosphorylates vimentin/VIM, thereby regulating the dynamic behavior of the intermediate filament cytoskeleton (By similarity). {ECO:0000250\|UniProtKB:Q924X7, ECO:0000269\|PubMed:37146716, ECO:0000269\|PubMed:38781365}.
Q9BZL6	PRKD2	S189	Sugiyama	Serine/threonine-protein kinase D2 (EC 2.7.11.13) (nPKC-D2)	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:14743217, PubMed:15604256, PubMed:16928771, PubMed:17077180, PubMed:17951978, PubMed:17962809, PubMed:18262756, PubMed:19001381, PubMed:19192391, PubMed:23503467, PubMed:28428613). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (By similarity). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-717 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (PubMed:15604256, PubMed:28428613). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (PubMed:17962809). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation (PubMed:17077180). During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (By similarity). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (PubMed:16928771). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (PubMed:19192391). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (PubMed:14743217). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (PubMed:19001381). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (PubMed:18262756). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (PubMed:17951978). Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion (PubMed:23503467). {ECO:0000250\|UniProtKB:Q8BZ03, ECO:0000269\|PubMed:14743217, ECO:0000269\|PubMed:15604256, ECO:0000269\|PubMed:16928771, ECO:0000269\|PubMed:17077180, ECO:0000269\|PubMed:17951978, ECO:0000269\|PubMed:17962809, ECO:0000269\|PubMed:18262756, ECO:0000269\|PubMed:19001381, ECO:0000269\|PubMed:19192391, ECO:0000269\|PubMed:23503467, ECO:0000269\|PubMed:28428613}.
Q9NRA0	SPHK2	S393	Sugiyama	Sphingosine kinase 2 (SK 2) (SPK 2) (EC 2.7.1.91)	Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides (PubMed:12954646, PubMed:19168031). In contrast to prosurvival SPHK1, has a positive effect on intracellular ceramide levels, inhibits cells growth and enhances apoptosis (PubMed:16118219). In mitochondria, is important for cytochrome-c oxidase assembly and mitochondrial respiration. The SPP produced in mitochondria binds PHB2 and modulates the regulation via PHB2 of complex IV assembly and respiration (PubMed:20959514). In nucleus, plays a role in epigenetic regulation of gene expression. Interacts with HDAC1 and HDAC2 and, through SPP production, inhibits their enzymatic activity, preventing the removal of acetyl groups from lysine residues with histones. Up-regulates acetylation of histone H3-K9, histone H4-K5 and histone H2B-K12 (PubMed:19729656). In nucleus, may have an inhibitory effect on DNA synthesis and cell cycle (PubMed:12954646, PubMed:16103110). In mast cells, is the main regulator of SPP production which mediates calcium influx, NF-kappa-B activation, cytokine production, such as TNF and IL6, and degranulation of mast cells (By similarity). In dopaminergic neurons, is involved in promoting mitochondrial functions regulating ATP and ROS levels (By similarity). Also involved in the regulation of glucose and lipid metabolism (By similarity). {ECO:0000250\|UniProtKB:Q9JIA7, ECO:0000269\|PubMed:12954646, ECO:0000269\|PubMed:16103110, ECO:0000269\|PubMed:16118219, ECO:0000269\|PubMed:19168031, ECO:0000269\|PubMed:19729656, ECO:0000269\|PubMed:20959514}.
A6NCI8	C2orf78	S822	ochoa	Uncharacterized protein C2orf78	None
A8CG34	POM121C	S278	ochoa	Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
A8CG34	POM121C	S373	ochoa	Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
H0YJW9	None	S68	ochoa	Uncharacterized protein	None
O00291	HIP1	S323	ochoa	Huntingtin-interacting protein 1 (HIP-1) (Huntingtin-interacting protein I) (HIP-I)	Plays a role in clathrin-mediated endocytosis and trafficking (PubMed:11532990, PubMed:11577110, PubMed:11889126). Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner (By similarity). Regulates presynaptic nerve terminal activity (By similarity). Enhances androgen receptor (AR)-mediated transcription (PubMed:16027218). May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway (PubMed:11007801). Binds 3-phosphoinositides (via ENTH domain) (PubMed:14732715). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis (PubMed:14732715). May play a functional role in the cell filament networks (PubMed:18790740). May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors (PubMed:11007801, PubMed:12163454). {ECO:0000250\|UniProtKB:Q8VD75, ECO:0000269\|PubMed:11007801, ECO:0000269\|PubMed:11532990, ECO:0000269\|PubMed:11577110, ECO:0000269\|PubMed:11889126, ECO:0000269\|PubMed:12163454, ECO:0000269\|PubMed:14732715, ECO:0000269\|PubMed:16027218, ECO:0000269\|PubMed:18790740, ECO:0000269\|PubMed:9147654}.
O00512	BCL9	S157	ochoa	B-cell CLL/lymphoma 9 protein (B-cell lymphoma 9 protein) (Bcl-9) (Protein legless homolog)	Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11955446}.
O14607	UTY	S768	ochoa	Histone demethylase UTY (EC 1.14.11.68) (Ubiquitously-transcribed TPR protein on the Y chromosome) (Ubiquitously-transcribed Y chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase UTY)	Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity. {ECO:0000269\|PubMed:24798337}.
O15040	TECPR2	S415	ochoa	Tectonin beta-propeller repeat-containing protein 2 (WD repeat-containing protein KIAA0329/KIAA0297)	Probably plays a role as positive regulator of autophagy. {ECO:0000269\|PubMed:23176824}.
O15042	U2SURP	S27	ochoa	U2 snRNP-associated SURP motif-containing protein (140 kDa Ser/Arg-rich domain protein) (U2-associated protein SR140)	None
O15066	KIF3B	S729	ochoa	Kinesin-like protein KIF3B (HH0048) (Microtubule plus end-directed kinesin motor 3B) [Cleaved into: Kinesin-like protein KIF3B, N-terminally processed]	Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation (PubMed:32386558). Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors (PubMed:32386558). Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). {ECO:0000250\|UniProtKB:Q61771, ECO:0000269\|PubMed:32386558}.
O15066	KIF3B	S730	ochoa	Kinesin-like protein KIF3B (HH0048) (Microtubule plus end-directed kinesin motor 3B) [Cleaved into: Kinesin-like protein KIF3B, N-terminally processed]	Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation (PubMed:32386558). Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors (PubMed:32386558). Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). {ECO:0000250\|UniProtKB:Q61771, ECO:0000269\|PubMed:32386558}.
O15085	ARHGEF11	S658	ochoa	Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269\|PubMed:21670212}.
O15164	TRIM24	S771	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15550	KDM6A	S821	ochoa	Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously-transcribed TPR protein on the X chromosome) (Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A)	Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17713478, PubMed:17761849, PubMed:17851529). Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27' (PubMed:17713478, PubMed:17761849, PubMed:17851529). Plays a central role in regulation of posterior development, by regulating HOX gene expression (PubMed:17851529). Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (PubMed:17761849). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (By similarity). {ECO:0000250\|UniProtKB:O70546, ECO:0000269\|PubMed:17713478, ECO:0000269\|PubMed:17761849, ECO:0000269\|PubMed:17851529, ECO:0000269\|PubMed:18003914}.
O43166	SIPA1L1	S97	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43295	SRGAP3	S1072	ochoa	SLIT-ROBO Rho GTPase-activating protein 3 (srGAP3) (Mental disorder-associated GAP) (Rho GTPase-activating protein 14) (WAVE-associated Rac GTPase-activating protein) (WRP)	GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons. {ECO:0000269\|PubMed:12195014, ECO:0000269\|PubMed:12447388}.
O43314	PPIP5K2	S1016	ochoa	Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (hsVIP2)	Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Required for normal hearing (PubMed:29590114). {ECO:0000269\|PubMed:17690096, ECO:0000269\|PubMed:17702752, ECO:0000269\|PubMed:21222653, ECO:0000269\|PubMed:29590114}.
O43318	MAP3K7	S458	ochoa	Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Plays an important role in the cascades of cellular responses evoked by changes in the environment (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) (PubMed:16893890, PubMed:9079627). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7 (PubMed:11460167, PubMed:8663074). These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1) (PubMed:11460167, PubMed:12589052, PubMed:8663074). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex (PubMed:12589052, PubMed:8663074). Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation (PubMed:10094049, PubMed:11460167). In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B (PubMed:16893890). Promotes TRIM5 capsid-specific restriction activity (PubMed:21512573). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity). Phosphorylates STING1 in response to cGAMP-activation, promoting association between STEEP1 and STING1 and STING1 translocation to COPII vesicles (PubMed:37832545). {ECO:0000250\|UniProtKB:Q62073, ECO:0000269\|PubMed:10094049, ECO:0000269\|PubMed:11460167, ECO:0000269\|PubMed:12589052, ECO:0000269\|PubMed:16845370, ECO:0000269\|PubMed:16893890, ECO:0000269\|PubMed:21512573, ECO:0000269\|PubMed:37832545, ECO:0000269\|PubMed:8663074, ECO:0000269\|PubMed:9079627}.
O43318	MAP3K7	S461	ochoa	Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Plays an important role in the cascades of cellular responses evoked by changes in the environment (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) (PubMed:16893890, PubMed:9079627). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7 (PubMed:11460167, PubMed:8663074). These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1) (PubMed:11460167, PubMed:12589052, PubMed:8663074). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex (PubMed:12589052, PubMed:8663074). Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation (PubMed:10094049, PubMed:11460167). In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B (PubMed:16893890). Promotes TRIM5 capsid-specific restriction activity (PubMed:21512573). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity). Phosphorylates STING1 in response to cGAMP-activation, promoting association between STEEP1 and STING1 and STING1 translocation to COPII vesicles (PubMed:37832545). {ECO:0000250\|UniProtKB:Q62073, ECO:0000269\|PubMed:10094049, ECO:0000269\|PubMed:11460167, ECO:0000269\|PubMed:12589052, ECO:0000269\|PubMed:16845370, ECO:0000269\|PubMed:16893890, ECO:0000269\|PubMed:21512573, ECO:0000269\|PubMed:37832545, ECO:0000269\|PubMed:8663074, ECO:0000269\|PubMed:9079627}.
O43524	FOXO3	S432	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43524	FOXO3	S442	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43822	CFAP410	S166	ochoa	Cilia- and flagella-associated protein 410 (C21orf-HUMF09G8.5) (Leucine-rich repeat-containing protein 76) (YF5/A2)	Plays a role in cilia formation and/or maintenance (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987). Involved in DNA damage repair (PubMed:26290490). {ECO:0000250\|UniProtKB:Q8C6G1, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:26290490}.
O60271	SPAG9	S597	ochoa	C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (Cancer/testis antigen 89) (CT89) (Human lung cancer oncogene 6 protein) (HLC-6) (JNK-associated leucine-zipper protein) (JLP) (Mitogen-activated protein kinase 8-interacting protein 4) (Proliferation-inducing protein 6) (Protein highly expressed in testis) (PHET) (Sperm surface protein) (Sperm-associated antigen 9) (Sperm-specific protein) (Sunday driver 1)	The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250\|UniProtKB:Q58A65, ECO:0000269\|PubMed:14743216, ECO:0000269\|PubMed:29146937}.
O60292	SIPA1L3	S1386	ochoa	Signal-induced proliferation-associated 1-like protein 3 (SIPA1-like protein 3) (SPA-1-like protein 3)	Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269\|PubMed:26231217}.
O60307	MAST3	S108	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S109	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60503	ADCY9	S60	ochoa	Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (ACIX) (Adenylyl cyclase 9) (AC9)	Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors (PubMed:10987815, PubMed:12972952, PubMed:15879435, PubMed:9628827). Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and beta-adrenergic receptors (PubMed:9628827). {ECO:0000269\|PubMed:10987815, ECO:0000269\|PubMed:12972952, ECO:0000269\|PubMed:15879435, ECO:0000269\|PubMed:9628827}.
O75113	N4BP1	S331	ochoa	NEDD4-binding protein 1 (N4BP1) (EC 3.1.-.-)	Potent suppressor of cytokine production that acts as a regulator of innate immune signaling and inflammation. Acts as a key negative regulator of select cytokine and chemokine responses elicited by TRIF-independent Toll-like receptors (TLRs), thereby limiting inflammatory cytokine responses to minor insults. In response to more threatening pathogens, cleaved by CASP8 downstream of TLR3 or TLR4, leading to its inactivation, thereby allowing production of inflammatory cytokines (By similarity). Acts as a restriction factor against some viruses, such as HIV-1: restricts HIV-1 replication by binding to HIV-1 mRNAs and mediating their degradation via its ribonuclease activity (PubMed:31133753). Also acts as an inhibitor of the E3 ubiquitin-protein ligase ITCH: acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates (By similarity). {ECO:0000250\|UniProtKB:Q6A037, ECO:0000269\|PubMed:31133753}.
O75122	CLASP2	S327	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75140	DEPDC5	S505	ochoa	GATOR1 complex protein DEPDC5 (DEP domain-containing protein 5)	As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:31548394, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide-binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (PubMed:29590090, PubMed:35338845). However, it does not execute the GAP activity, which is mediated by NPRL2 (PubMed:29590090). {ECO:0000269\|PubMed:23723238, ECO:0000269\|PubMed:25457612, ECO:0000269\|PubMed:29590090, ECO:0000269\|PubMed:29769719, ECO:0000269\|PubMed:31548394, ECO:0000269\|PubMed:35338845}.
O75152	ZC3H11A	S738	ochoa	Zinc finger CCCH domain-containing protein 11A	Through its association with TREX complex components, may participate in the export and post-transcriptional coordination of selected mRNA transcripts, including those required to maintain the metabolic processes in embryonic cells (PubMed:22928037, PubMed:37356722). Binds RNA (PubMed:29610341, PubMed:37356722). {ECO:0000269\|PubMed:22928037, ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.; FUNCTION: (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA export (PubMed:29610341). May be required for proper polyadenylation of adenovirus type 5/HAdV-5 capsid mRNA (PubMed:37356722). {ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.
O75970	MPDZ	S1824	ochoa	Multiple PDZ domain protein (Multi-PDZ domain protein 1)	Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250\|UniProtKB:O55164, ECO:0000269\|PubMed:11150294, ECO:0000269\|PubMed:15312654}.
O94875	SORBS2	S301	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94875	SORBS2	S302	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94880	PHF14	S29	ochoa	PHD finger protein 14	Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity). {ECO:0000250\|UniProtKB:A0A286Y9D1, ECO:0000250\|UniProtKB:Q9D4H9, ECO:0000269\|PubMed:23688586}.
O95049	TJP3	S568	ochoa	Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250\|UniProtKB:O62683, ECO:0000250\|UniProtKB:Q9QXY1, ECO:0000269\|PubMed:16129888, ECO:0000269\|PubMed:21411630}.
O95155	UBE4B	S90	ochoa	Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250\|UniProtKB:P54860, ECO:0000250\|UniProtKB:Q9ES00, ECO:0000269\|PubMed:17369820}.
O95163	ELP1	S1174	ochoa\|psp	Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) (p150)	Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (PubMed:9751059). {ECO:0000250\|UniProtKB:Q06706, ECO:0000250\|UniProtKB:Q7TT37, ECO:0000269\|PubMed:9751059, ECO:0000303\|PubMed:29332244}.
O95251	KAT7	S56	ochoa	Histone acetyltransferase KAT7 (EC 2.3.1.48) (Histone acetyltransferase binding to ORC1) (Lysine acetyltransferase 7) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2) (MYST-2)	Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:31767635, PubMed:31827282). Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:10438470, PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:26620551). H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II (PubMed:31827282). Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation (PubMed:21753189). H3K14ac is also required for T-cell development (By similarity). KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, PubMed:24065767, PubMed:26620551). Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange (PubMed:27270040). Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity (PubMed:16997280). {ECO:0000250\|UniProtKB:Q5SVQ0, ECO:0000269\|PubMed:10438470, ECO:0000269\|PubMed:11278932, ECO:0000269\|PubMed:16387653, ECO:0000269\|PubMed:16997280, ECO:0000269\|PubMed:18832067, ECO:0000269\|PubMed:19187766, ECO:0000269\|PubMed:20129055, ECO:0000269\|PubMed:21753189, ECO:0000269\|PubMed:21856198, ECO:0000269\|PubMed:24065767, ECO:0000269\|PubMed:26620551, ECO:0000269\|PubMed:27270040, ECO:0000269\|PubMed:28719581, ECO:0000269\|PubMed:31767635, ECO:0000269\|PubMed:31827282}.; FUNCTION: Plays a central role in the maintenance of leukemia stem cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby facilitating the processivity of RNA polymerase II to maintain the high expression of key genes, such as HOXA9 and HOXA10 that help to sustain the functional properties of leukemia stem cells (PubMed:31827282). {ECO:0000269\|PubMed:31827282}.
O95817	BAG3	S194	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
P02671	FGA	S294	ochoa	Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]	Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250\|UniProtKB:E9PV24}.
P04004	VTN	S410	ochoa	Vitronectin (VN) (S-protein) (Serum-spreading factor) (V75) [Cleaved into: Vitronectin V65 subunit; Vitronectin V10 subunit; Somatomedin-B]	Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
P04049	RAF1	S29	ochoa\|psp	RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269\|PubMed:11427728, ECO:0000269\|PubMed:11719507, ECO:0000269\|PubMed:15385642, ECO:0000269\|PubMed:15618521, ECO:0000269\|PubMed:15849194, ECO:0000269\|PubMed:16892053, ECO:0000269\|PubMed:16924233, ECO:0000269\|PubMed:9360956}.
P04792	HSPB1	S86	ochoa\|psp	Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Heat shock protein family B member 1) (Stress-responsive protein 27) (SRP27)	Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742). {ECO:0000269\|PubMed:10383393, ECO:0000269\|PubMed:19166925, ECO:0000269\|PubMed:20178975, ECO:0000269\|PubMed:23728742}.
P07814	EPRS1	S817	ochoa	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P08183	ABCB1	S658	ochoa	ATP-dependent translocase ABCB1 (ATP-binding cassette sub-family B member 1) (Multidrug resistance protein 1) (EC 7.6.2.2) (P-glycoprotein 1) (Phospholipid transporter ABCB1) (EC 7.6.2.1) (CD antigen CD243)	Translocates drugs and phospholipids across the membrane (PubMed:2897240, PubMed:35970996, PubMed:8898203, PubMed:9038218, PubMed:35507548). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:35970996, PubMed:9038218). {ECO:0000269\|PubMed:2897240, ECO:0000269\|PubMed:35507548, ECO:0000269\|PubMed:35970996, ECO:0000269\|PubMed:8898203, ECO:0000269\|PubMed:9038218}.
P08195	SLC3A2	S406	psp	Amino acid transporter heavy chain SLC3A2 (4F2 cell-surface antigen heavy chain) (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98)	Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:11557028, PubMed:30867591, PubMed:33298890, PubMed:33758168, PubMed:34880232, PubMed:9751058, PubMed:9829974, PubMed:9878049). Heterodimers function as amino acids exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids (PubMed:10903140, PubMed:9829974). Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:34880232). SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, thyroid hormones and L-DOPA (PubMed:10574970, PubMed:11389679, PubMed:11557028, PubMed:11564694, PubMed:11742812, PubMed:12117417, PubMed:12225859, PubMed:12716892, PubMed:15980244, PubMed:30867591, PubMed:33298890, PubMed:33758168). SLC3A2 is essential for plasma membrane localization, stability, and the transport activity of SLC7A5 and SLC7A8 (PubMed:10391915, PubMed:10574970, PubMed:11311135, PubMed:15769744, PubMed:33066406). When associated with LAPTM4B, the heterodimer SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression (PubMed:11121428, PubMed:15625115). {ECO:0000250\|UniProtKB:P63115, ECO:0000269\|PubMed:10391915, ECO:0000269\|PubMed:10574970, ECO:0000269\|PubMed:10903140, ECO:0000269\|PubMed:11121428, ECO:0000269\|PubMed:11311135, ECO:0000269\|PubMed:11389679, ECO:0000269\|PubMed:11557028, ECO:0000269\|PubMed:11564694, ECO:0000269\|PubMed:11742812, ECO:0000269\|PubMed:12117417, ECO:0000269\|PubMed:12225859, ECO:0000269\|PubMed:12716892, ECO:0000269\|PubMed:15625115, ECO:0000269\|PubMed:15769744, ECO:0000269\|PubMed:15980244, ECO:0000269\|PubMed:25998567, ECO:0000269\|PubMed:30867591, ECO:0000269\|PubMed:33066406, ECO:0000269\|PubMed:33298890, ECO:0000269\|PubMed:33758168, ECO:0000269\|PubMed:34880232, ECO:0000269\|PubMed:9751058, ECO:0000269\|PubMed:9829974, ECO:0000269\|PubMed:9878049}.; FUNCTION: (Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis. {ECO:0000269\|PubMed:30341327}.; FUNCTION: (Microbial infection) Acts as a receptor for malaria parasite Plasmodium vivax (Thai isolate) in immature red blood cells. {ECO:0000269\|PubMed:34294905}.
P08727	KRT19	Y61	ochoa	Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19)	Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269\|PubMed:16000376}.
P10636	MAPT	S447	ochoa	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P10636	MAPT	S733	ochoa	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. {ECO:0000269\|PubMed:21985311, ECO:0000269\|PubMed:32961270}.
P10809	HSPD1	S256	ochoa	60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Heat shock protein family D member 1) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)	Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). {ECO:0000269\|PubMed:11422376, ECO:0000269\|PubMed:1346131, ECO:0000305\|PubMed:25918392}.
P11137	MAP2	S1802	ochoa	Microtubule-associated protein 2 (MAP-2)	The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
P11274	BCR	S239	ochoa	Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)	Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119). {ECO:0000250\|UniProtKB:Q6PAJ1, ECO:0000269\|PubMed:1657398, ECO:0000269\|PubMed:17116687, ECO:0000269\|PubMed:1903516, ECO:0000269\|PubMed:23940119, ECO:0000269\|PubMed:7479768}.
P15884	TCF4	S346	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15923	TCF3	S354	ochoa	Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)	Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (By similarity). Together with TCF15, required for the mesenchymal to epithelial transition (By similarity). Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (By similarity). Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (PubMed:2493990). Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (By similarity). {ECO:0000250\|UniProtKB:P15806, ECO:0000269\|PubMed:2493990}.; FUNCTION: [Isoform E47]: Facilitates ATOH7 binding to DNA at the consensus sequence 5'-CAGGTG-3', and positively regulates transcriptional activity. {ECO:0000269\|PubMed:31696227}.
P16070	CD44	S183	ochoa	CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)	Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment (PubMed:16541107, PubMed:19703720, PubMed:22726066). Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection (PubMed:7528188). Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:18757307, PubMed:23589287). Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion (PubMed:15123640). {ECO:0000269\|PubMed:15123640, ECO:0000269\|PubMed:16541107, ECO:0000269\|PubMed:18757307, ECO:0000269\|PubMed:19703720, ECO:0000269\|PubMed:22726066, ECO:0000269\|PubMed:23589287, ECO:0000269\|PubMed:7528188}.
P16144	ITGB4	S1212	ochoa	Integrin beta-4 (GP150) (CD antigen CD104)	Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:19403692, ECO:0000269\|PubMed:20682778, ECO:0000269\|PubMed:22351760, ECO:0000269\|PubMed:28873464}.
P18850	ATF6	S101	ochoa	Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha]	[Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464). {ECO:0000269\|PubMed:10564271, ECO:0000269\|PubMed:11158310, ECO:0000269\|PubMed:11779464}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR (PubMed:10564271, PubMed:11158310, PubMed:11163209, PubMed:11779464). Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3') (PubMed:10564271, PubMed:11158310, PubMed:11779464). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor (PubMed:10564271, PubMed:11158310, PubMed:11779464). May play a role in foveal development and cone function in the retina (PubMed:26029869). {ECO:0000269\|PubMed:10564271, ECO:0000269\|PubMed:11158310, ECO:0000269\|PubMed:11163209, ECO:0000269\|PubMed:11779464, ECO:0000269\|PubMed:26029869}.
P21359	NF1	S883	ochoa	Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]	Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269\|PubMed:2121371, ECO:0000269\|PubMed:8417346}.
P22059	OSBP	S389	ochoa	Oxysterol-binding protein 1	Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269\|PubMed:15746430, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18450749, ECO:0000269\|PubMed:24209621}.
P22681	CBL	S798	ochoa	E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)	E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250\|UniProtKB:P22682, ECO:0000269\|PubMed:10514377, ECO:0000269\|PubMed:11896602, ECO:0000269\|PubMed:14661060, ECO:0000269\|PubMed:14739300, ECO:0000269\|PubMed:15190072, ECO:0000269\|PubMed:17094949, ECO:0000269\|PubMed:17509076, ECO:0000269\|PubMed:17974561, ECO:0000269\|PubMed:18374639, ECO:0000269\|PubMed:19689429, ECO:0000269\|PubMed:21596750, ECO:0000269\|PubMed:28381567}.
P25054	APC	S1238	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S1344	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S1507	psp	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25054	APC	S2771	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P25116	F2R	S399	ochoa\|psp	Proteinase-activated receptor 1 (PAR-1) (Coagulation factor II receptor) (Thrombin receptor)	High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores (PubMed:1672265, PubMed:8136362). The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores (By similarity). In astrocytes, the calcium released into the cytosol allows the Ca(2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). May play a role in platelets activation and in vascular development (PubMed:10079109). Mediates up-regulation of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, triggered by coagulation factor Xa (F10) in cardiac fibroblasts and umbilical vein endothelial cells (PubMed:30568593, PubMed:34831181). {ECO:0000250\|UniProtKB:P26824, ECO:0000250\|UniProtKB:P30558, ECO:0000269\|PubMed:10079109, ECO:0000269\|PubMed:1672265, ECO:0000269\|PubMed:30568593, ECO:0000269\|PubMed:34831181, ECO:0000269\|PubMed:8136362}.
P27448	MARK3	S380	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P28827	PTPRM	S824	ochoa	Receptor-type tyrosine-protein phosphatase mu (Protein-tyrosine phosphatase mu) (R-PTP-mu) (EC 3.1.3.48)	Receptor protein-tyrosine phosphatase that mediates homotypic cell-cell interactions and plays a role in adipogenic differentiation via modulation of p120 catenin/CTNND1 phosphorylation (PubMed:10753936, PubMed:17761881). Promotes CTNND1 dephosphorylation and prevents its cytoplasmic localization where it inhibits SLC2A4 membrane trafficking. In turn, SLC2A4 is directed to the plasma membrane and performs its glucose transporter function (PubMed:21998202). {ECO:0000269\|PubMed:10753936, ECO:0000269\|PubMed:16456543, ECO:0000269\|PubMed:17761881, ECO:0000269\|PubMed:21998202}.
P29375	KDM5A	S1330	ochoa	Lysine-specific demethylase 5A (EC 1.14.11.67) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2) ([histone H3]-trimethyl-L-lysine(4) demethylase 5A)	Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511). May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228). {ECO:0000250\|UniProtKB:Q3UXZ9, ECO:0000269\|PubMed:11358960, ECO:0000269\|PubMed:15949438, ECO:0000269\|PubMed:17320160, ECO:0000269\|PubMed:17320161, ECO:0000269\|PubMed:17320163, ECO:0000269\|PubMed:18270511, ECO:0000269\|PubMed:19430464, ECO:0000269\|PubMed:27427228}.
P29558	RBMS1	S52	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29590	PML	S583	ochoa	Protein PML (E3 SUMO-protein ligase PML) (EC 2.3.2.-) (Promyelocytic leukemia protein) (RING finger protein 71) (RING-type E3 SUMO transferase PML) (Tripartite motif-containing protein 19) (TRIM19)	Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Inhibits EIF4E-mediated mRNA nuclear export by reducing EIF4E affinity for the 5' 7-methylguanosine (m7G) cap of target mRNAs (PubMed:11500381, PubMed:11575918, PubMed:18391071). Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration. {ECO:0000269\|PubMed:11500381, ECO:0000269\|PubMed:11575918, ECO:0000269\|PubMed:18391071}.; FUNCTION: Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response (PubMed:20972456, PubMed:28250117). Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity (PubMed:20972456, PubMed:28250117). {ECO:0000269\|PubMed:20972456, ECO:0000269\|PubMed:28250117}.
P30260	CDC27	S438	ochoa	Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (APC3) (CDC27 homolog) (CDC27Hs) (H-NUC)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
P30414	NKTR	S518	ochoa	NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase)	PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). {ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:8421688}.
P30622	CLIP1	S47	ochoa	CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)	Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269\|PubMed:12433698, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:17889670}.
P30622	CLIP1	S162	ochoa	CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)	Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269\|PubMed:12433698, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:17889670}.
P32004	L1CAM	S1194	ochoa	Neural cell adhesion molecule L1 (N-CAM-L1) (NCAM-L1) (CD antigen CD171)	Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity. {ECO:0000269\|PubMed:20621658, ECO:0000305}.
P35611	ADD1	S468	ochoa	Alpha-adducin (Erythrocyte adducin subunit alpha)	Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.
P41214	EIF2D	S187	ochoa	Eukaryotic translation initiation factor 2D (eIF2d) (Hepatocellular carcinoma-associated antigen 56) (Ligatin)	Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. {ECO:0000269\|PubMed:20566627, ECO:0000269\|PubMed:20713520}.
P41235	HNF4A	S151	psp	Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)	Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes (PubMed:30597922). Activates the transcription of CYP2C38 (By similarity). Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells (PubMed:30530698). {ECO:0000250\|UniProtKB:P49698, ECO:0000269\|PubMed:30530698, ECO:0000269\|PubMed:30597922}.
P42356	PI4KA	S260	ochoa	Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67) (Phosphatidylinositol 4-Kinase III alpha)	Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000269\|PubMed:10101268, ECO:0000269\|PubMed:23229899}.
P46019	PHKA2	S979	ochoa	Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit)	Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
P49790	NUP153	S192	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49792	RANBP2	S1651	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P49792	RANBP2	S1768	ochoa	E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269\|PubMed:11792325, ECO:0000269\|PubMed:12032081, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:20386726, ECO:0000269\|PubMed:20676357, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22194619, ECO:0000269\|PubMed:22902403, ECO:0000269\|PubMed:23353830, ECO:0000269\|PubMed:7775481, ECO:0000303\|PubMed:10078529}.
P50548	ERF	S170	ochoa	ETS domain-containing transcription factor ERF (Ets2 repressor factor) (PE-2)	Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity). {ECO:0000250}.
P50616	TOB1	S154	ochoa\|psp	Protein Tob1 (Transducer of erbB-2 1)	Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex (PubMed:23236473, PubMed:8632892). Mediates CPEB3-accelerated mRNA deadenylation by binding to CPEB3 and recruiting CNOT7 which leads to target mRNA deadenylation and decay (PubMed:21336257). {ECO:0000269\|PubMed:21336257, ECO:0000269\|PubMed:23236473, ECO:0000269\|PubMed:8632892}.
P51805	PLXNA3	S1610	ochoa	Plexin-A3 (Plexin-4) (Semaphorin receptor SEX)	Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.
P54725	RAD23A	S147	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P55196	AFDN	S565	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55196	AFDN	S1318	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55197	MLLT10	S367	ochoa	Protein AF-10 (ALL1-fused gene from chromosome 10 protein)	Probably involved in transcriptional regulation. In vitro or as fusion protein with KMT2A/MLL1 has transactivation activity. Binds to cruciform DNA. In cells, binding to unmodified histone H3 regulates DOT1L functions including histone H3 'Lys-79' dimethylation (H3K79me2) and gene activation (PubMed:26439302). {ECO:0000269\|PubMed:17868029, ECO:0000269\|PubMed:26439302}.
P55198	MLLT6	S280	ochoa	Protein AF-17 (ALL1-fused gene from chromosome 17 protein)	None
P56524	HDAC4	S636	ochoa	Histone deacetylase 4 (HD4) (EC 3.5.1.98)	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256). {ECO:0000269\|PubMed:10523670, ECO:0000269\|PubMed:24413532, ECO:0000269\|PubMed:27708256}.
P61244	MAX	S121	ochoa	Protein max (Class D basic helix-loop-helix protein 4) (bHLHd4) (Myc-associated factor X)	Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements. {ECO:0000269\|PubMed:26070438}.
P78310	CXADR	S304	ochoa	Coxsackievirus and adenovirus receptor (CAR) (hCAR) (CVB3-binding protein) (Coxsackievirus B-adenovirus receptor) (HCVADR)	Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. {ECO:0000269\|PubMed:11734628, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:15800062, ECO:0000269\|PubMed:19064666, ECO:0000269\|PubMed:9096397}.; FUNCTION: (Microbial infection) Acts as a receptor for adenovirus type C. {ECO:0000269\|PubMed:10567268, ECO:0000269\|PubMed:10666333, ECO:0000269\|PubMed:12297051, ECO:0000269\|PubMed:9733828}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus B1 to B6. {ECO:0000269\|PubMed:10814575, ECO:0000269\|PubMed:14978041}.
P78559	MAP1A	S121	ochoa	Microtubule-associated protein 1A (MAP-1A) (Proliferation-related protein p80) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]	Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
P82094	TMF1	S254	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P98082	DAB2	S328	ochoa	Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)	Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269\|PubMed:11387212, ECO:0000269\|PubMed:12805222, ECO:0000269\|PubMed:16267015, ECO:0000269\|PubMed:16984970, ECO:0000269\|PubMed:19306879, ECO:0000269\|PubMed:21995445, ECO:0000269\|PubMed:22323290, ECO:0000269\|PubMed:22491013}.
Q01974	ROR2	S864	ochoa	Tyrosine-protein kinase transmembrane receptor ROR2 (EC 2.7.10.1) (Neurotrophic tyrosine kinase, receptor-related 2)	Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation (PubMed:17717073). In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443). {ECO:0000250\|UniProtKB:Q9Z138, ECO:0000269\|PubMed:17717073, ECO:0000269\|PubMed:25029443}.
Q03188	CENPC	S713	ochoa	Centromere protein C (CENP-C) (Centromere autoantigen C) (Centromere protein C 1) (CENP-C 1) (Interphase centromere complex protein 7)	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269\|PubMed:19482874, ECO:0000269\|PubMed:21529714}.
Q08170	SRSF4	S116	ochoa	Serine/arginine-rich splicing factor 4 (Pre-mRNA-splicing factor SRP75) (SRP001LB) (Splicing factor, arginine/serine-rich 4)	Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:15009664}.
Q08378	GOLGA3	S282	ochoa	Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160)	Golgi auto-antigen; probably involved in maintaining Golgi structure.
Q08AD1	CAMSAP2	S1343	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q09666	AHNAK	S110	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5867	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q12888	TP53BP1	S834	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12959	DLG1	S571	ochoa	Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97) (hDlg)	Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). May also play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. During long-term depression in hippocampal neurons, it recruits ADAM10 to the plasma membrane (PubMed:23676497). {ECO:0000250\|UniProtKB:A0A8C0TYJ0, ECO:0000250\|UniProtKB:Q811D0, ECO:0000269\|PubMed:10656683, ECO:0000269\|PubMed:12445884, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15263016, ECO:0000269\|PubMed:19213956, ECO:0000269\|PubMed:20605917, ECO:0000269\|PubMed:23676497}.
Q12965	MYO1E	S1009	ochoa	Unconventional myosin-Ie (Myosin-Ic) (Unconventional myosin 1E)	Actin-based motor molecule with ATPase activity (PubMed:11940582, PubMed:36316095). Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated vesicles (PubMed:36316095). Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. {ECO:0000269\|PubMed:11940582, ECO:0000269\|PubMed:17257598, ECO:0000269\|PubMed:20860408, ECO:0000269\|PubMed:36316095}.
Q13029	PRDM2	S450	ochoa	PR domain zinc finger protein 2 (EC 2.1.1.355) (GATA-3-binding protein G3B) (Lysine N-methyltransferase 8) (MTB-ZF) (MTE-binding protein) (PR domain-containing protein 2) (Retinoblastoma protein-interacting zinc finger protein) (Zinc finger protein RIZ)	S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene. {ECO:0000269\|PubMed:14633678}.
Q13107	USP4	S596	ochoa	Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Ubiquitous nuclear protein homolog)	Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins (PubMed:16316627, PubMed:16339847, PubMed:16472766, PubMed:20595234, PubMed:22347420, PubMed:25404403, PubMed:28604766, PubMed:30514904). Deubiquitinates PDPK1 (PubMed:22347420). Deubiquitinates TRIM21 (PubMed:16316627). Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface (PubMed:16339847). Deubiquitinates HAS2 (PubMed:28604766). Deubiquitinates RHEB in response to EGF signaling, promoting mTORC1 signaling (PubMed:30514904). May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3 (PubMed:20595234). This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP (PubMed:20595234). May also play a role in the regulation of quality control in the ER (PubMed:16339847). {ECO:0000269\|PubMed:16316627, ECO:0000269\|PubMed:16339847, ECO:0000269\|PubMed:16472766, ECO:0000269\|PubMed:20595234, ECO:0000269\|PubMed:22347420, ECO:0000269\|PubMed:25404403, ECO:0000269\|PubMed:28604766, ECO:0000269\|PubMed:30514904}.
Q13131	PRKAA1	S520	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13131	PRKAA1	S527	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13136	PPFIA1	S790	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13136	PPFIA1	S1172	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13247	SRSF6	S122	ochoa	Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6)	Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269\|PubMed:12549914, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:22767602, ECO:0000269\|PubMed:24440982}.
Q13428	TCOF1	S482	ochoa	Treacle protein (Treacher Collins syndrome protein)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269\|PubMed:12777385, ECO:0000269\|PubMed:26399832}.
Q13435	SF3B2	S347	ochoa	Splicing factor 3B subunit 2 (Pre-mRNA-splicing factor SF3b 145 kDa subunit) (SF3b145) (Spliceosome-associated protein 145) (SAP 145)	Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B2 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). {ECO:0000269\|PubMed:10882114, ECO:0000269\|PubMed:12234937, ECO:0000269\|PubMed:15146077, ECO:0000269\|PubMed:27720643, ECO:0000269\|PubMed:32494006, ECO:0000269\|PubMed:33509932, ECO:0000269\|PubMed:34822310}.
Q13501	SQSTM1	S291	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13796	SHROOM2	S177	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13813	SPTAN1	S2142	ochoa	Spectrin alpha chain, non-erythrocytic 1 (Alpha-II spectrin) (Fodrin alpha chain) (Spectrin, non-erythroid alpha subunit)	Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
Q14004	CDK13	S1346	ochoa	Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)	Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269\|PubMed:16721827, ECO:0000269\|PubMed:1731328, ECO:0000269\|PubMed:18480452, ECO:0000269\|PubMed:20952539}.
Q14126	DSG2	S887	ochoa	Desmoglein-2 (Cadherin family member 5) (HDGC)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:38395410). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Required for proliferation and viability of embryonic stem cells in the blastocyst, thereby crucial for progression of post-implantation embryonic development (By similarity). Maintains pluripotency by regulating epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via interacting with and sequestering CTNNB1 to sites of cell-cell contact, thereby reducing translocation of CTNNB1 to the nucleus and subsequent transcription of CTNNB1/TCF-target genes (PubMed:29910125). Promotes pluripotency and the multi-lineage differentiation potential of hematopoietic stem cells (PubMed:27338829). Plays a role in endothelial cell sprouting and elongation via mediating the junctional-association of cortical actin fibers and CDH5 (PubMed:27338829). Plays a role in limiting inflammatory infiltration and the apoptotic response to injury in kidney tubular epithelial cells, potentially via its role in maintaining cell-cell adhesion and the epithelial barrier (PubMed:38395410). {ECO:0000250\|UniProtKB:O55111, ECO:0000269\|PubMed:27338829, ECO:0000269\|PubMed:29910125, ECO:0000269\|PubMed:38395410}.
Q14315	FLNC	S2627	ochoa	Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)	Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250\|UniProtKB:Q8VHX6, ECO:0000269\|PubMed:34405687}.
Q14498	RBM39	S337	ochoa	RNA-binding protein 39 (CAPER alpha) (CAPERalpha) (Hepatocellular carcinoma protein 1) (RNA-binding motif protein 39) (RNA-binding region-containing protein 2) (Splicing factor HCC1)	RNA-binding protein that acts as a pre-mRNA splicing factor (PubMed:15694343, PubMed:24795046, PubMed:28302793, PubMed:28437394, PubMed:31271494). Acts by promoting exon inclusion via regulation of exon cassette splicing (PubMed:31271494). Also acts as a transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1, independently of the pre-mRNA splicing factor activity (By similarity). {ECO:0000250\|UniProtKB:Q8VH51, ECO:0000269\|PubMed:15694343, ECO:0000269\|PubMed:24795046, ECO:0000269\|PubMed:28302793, ECO:0000269\|PubMed:28437394, ECO:0000269\|PubMed:31271494}.
Q14671	PUM1	S803	ochoa	Pumilio homolog 1 (HsPUM) (Pumilio-1)	Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:18328718, PubMed:21397187, PubMed:21572425, PubMed:21653694). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517, PubMed:29474920). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000250\|UniProtKB:Q80U78, ECO:0000269\|PubMed:18328718, ECO:0000269\|PubMed:18776931, ECO:0000269\|PubMed:20818387, ECO:0000269\|PubMed:20860814, ECO:0000269\|PubMed:21397187, ECO:0000269\|PubMed:21572425, ECO:0000269\|PubMed:21653694, ECO:0000269\|PubMed:22345517, ECO:0000269\|PubMed:22955276, ECO:0000269\|PubMed:25340845, ECO:0000269\|PubMed:25768905, ECO:0000269\|PubMed:26724866, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:29474920}.
Q14739	LBR	S73	ochoa	Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (LMN2R) (Lamin-B receptor) (Sterol C14-reductase)	Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963). {ECO:0000250\|UniProtKB:Q3U9G9, ECO:0000269\|PubMed:10828963, ECO:0000269\|PubMed:12618959, ECO:0000269\|PubMed:16784888, ECO:0000269\|PubMed:21327084, ECO:0000269\|PubMed:27336722, ECO:0000269\|PubMed:9630650}.
Q14980	NUMA1	S1792	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1837	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1856	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q15032	R3HDM1	S365	ochoa	R3H domain-containing protein 1	None
Q15047	SETDB1	S508	ochoa	Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.366) (ERG-associated protein with SET domain) (ESET) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Lysine N-methyltransferase 1E) (SET domain bifurcated 1)	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation (PubMed:12869583, PubMed:27237050, PubMed:39096901). Required for HUSH-mediated heterochromatin formation and gene silencing. Forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation (PubMed:14536086, PubMed:27732843). Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1 (PubMed:14536086). SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with TRIM28, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250\|UniProtKB:O88974, ECO:0000269\|PubMed:12869583, ECO:0000269\|PubMed:14536086, ECO:0000269\|PubMed:24623306, ECO:0000269\|PubMed:27029610, ECO:0000269\|PubMed:27237050, ECO:0000269\|PubMed:27732843, ECO:0000269\|PubMed:39096901}.
Q15052	ARHGEF6	S144	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15052	ARHGEF6	S565	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15149	PLEC	Y4393	ochoa	Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1)	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:21109228}.
Q15648	MED1	S1141	ochoa\|psp	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15910	EZH2	S366	ochoa\|psp	Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6)	Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2 (PubMed:22323599, PubMed:30923826). Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. {ECO:0000269\|PubMed:14532106, ECO:0000269\|PubMed:15225548, ECO:0000269\|PubMed:15231737, ECO:0000269\|PubMed:15385962, ECO:0000269\|PubMed:16179254, ECO:0000269\|PubMed:16357870, ECO:0000269\|PubMed:16618801, ECO:0000269\|PubMed:16717091, ECO:0000269\|PubMed:16936726, ECO:0000269\|PubMed:17210787, ECO:0000269\|PubMed:17344414, ECO:0000269\|PubMed:18285464, ECO:0000269\|PubMed:19026781, ECO:0000269\|PubMed:20935635, ECO:0000269\|PubMed:22323599, ECO:0000269\|PubMed:23063525, ECO:0000269\|PubMed:24474760, ECO:0000269\|PubMed:30026490, ECO:0000269\|PubMed:30923826}.
Q16566	CAMK4	S348	ochoa	Calcium/calmodulin-dependent protein kinase type IV (CaMK IV) (EC 2.7.11.17) (CaM kinase-GR)	Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4(+)/CD8(+) double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18. {ECO:0000269\|PubMed:10617605, ECO:0000269\|PubMed:17909078, ECO:0000269\|PubMed:18829949, ECO:0000269\|PubMed:7961813, ECO:0000269\|PubMed:8065343, ECO:0000269\|PubMed:8855261, ECO:0000269\|PubMed:8980227, ECO:0000269\|PubMed:9154845}.
Q2KHR3	QSER1	S1231	ochoa	Glutamine and serine-rich protein 1	Plays an essential role in the protection and maintenance of transcriptional and developmental programs. Protects many bivalent promoters and poised enhancers from hypermethylation, showing a marked preference for these regulatory elements over other types of promoters or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in a common complex to inhibit the binding of DNMT3A/3B and therefore de novo methylation. {ECO:0000269\|PubMed:33833093}.
Q2NKX8	ERCC6L	Y949	ochoa	DNA excision repair protein ERCC-6-like (EC 3.6.4.12) (ATP-dependent helicase ERCC6-like) (PLK1-interacting checkpoint helicase) (Tumor antigen BJ-HCC-15)	DNA helicase that acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase (PubMed:17218258, PubMed:23973328). Functions as ATP-dependent DNA translocase (PubMed:23973328, PubMed:28977671). Can promote Holliday junction branch migration (in vitro) (PubMed:23973328). {ECO:0000269\|PubMed:17218258, ECO:0000269\|PubMed:23973328, ECO:0000269\|PubMed:28977671}.
Q2TB10	ZNF800	S422	ochoa	Zinc finger protein 800	May be involved in transcriptional regulation.
Q4ADV7	RIC1	S1132	ochoa	Guanine nucleotide exchange factor subunit RIC1 (Connexin-43-interacting protein of 150 kDa) (Protein RIC1 homolog) (RAB6A-GEF complex partner protein 1)	The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP, and may thereby be required for efficient fusion of endosome-derived vesicles with the Golgi compartment (PubMed:23091056). The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors (PubMed:23091056). Required for phosphorylation and localization of GJA1 (PubMed:16112082). Is a regulator of procollagen transport and secretion, and is required for correct cartilage morphogenesis and development of the craniofacial skeleton (PubMed:31932796). {ECO:0000269\|PubMed:16112082, ECO:0000269\|PubMed:23091056, ECO:0000269\|PubMed:31932796}.
Q4V328	GRIPAP1	S669	ochoa	GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]	Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity). {ECO:0000250\|UniProtKB:Q9JHZ4}.; FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity. {ECO:0000269\|PubMed:17761173}.
Q53GG5	PDLIM3	S136	ochoa	PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein)	May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
Q53GG5	PDLIM3	S152	ochoa	PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein)	May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
Q5FWE3	PRRT3	S928	ochoa	Proline-rich transmembrane protein 3	None
Q5JQS6	GCSAML	S84	ochoa	Germinal center-associated signaling and motility-like protein	None
Q5JSZ5	PRRC2B	S1690	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5M775	SPECC1	S38	ochoa	Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1)	None
Q5M775	SPECC1	S364	ochoa	Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1)	None
Q5QJE6	DNTTIP2	S41	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5T1M5	FKBP15	S307	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T4S7	UBR4	S1737	ochoa	E3 ubiquitin-protein ligase UBR4 (EC 2.3.2.27) (600 kDa retinoblastoma protein-associated factor) (p600) (N-recognin-4) (Retinoblastoma-associated factor of 600 kDa) (RBAF600)	E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm (PubMed:25582440, PubMed:29033132, PubMed:34893540, PubMed:37891180, PubMed:38030679, PubMed:38182926, PubMed:38297121). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (PubMed:34893540, PubMed:37891180, PubMed:38030679). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:38030679). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:37891180). Together with UBR5, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR4 probably synthesizes mixed chains containing multiple linkages, while UBR5 is likely branching multiple 'Lys-48'-linked chains of substrates initially modified (PubMed:29033132). Together with KCMF1, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy (PubMed:34893540). Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). Mediates ubiquitination of ACLY, leading to its subsequent degradation (PubMed:23932781). Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization (PubMed:16214886). {ECO:0000269\|PubMed:16214886, ECO:0000269\|PubMed:23932781, ECO:0000269\|PubMed:25582440, ECO:0000269\|PubMed:29033132, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:37891180, ECO:0000269\|PubMed:38030679, ECO:0000269\|PubMed:38182926, ECO:0000269\|PubMed:38297121}.
Q5T5P2	KIAA1217	S1899	ochoa	Sickle tail protein homolog	Required for normal development of intervertebral disks. {ECO:0000250\|UniProtKB:A2AQ25}.
Q5T9C2	EEIG1	S189	ochoa	Early estrogen-induced gene 1 protein (EEIG1)	Key component of TNFSF11/RANKL- and TNF-induced osteoclastogenesis pathways, thereby mediates bone resorption in pathological bone loss conditions (By similarity). Required for TNFSF11/RANKL-induced osteoclastogenesis via its interaction with TNFRSF11A/RANK, thereby facilitates the downsteam transcription of NFATC1 and activation of PLCG2 (By similarity). Facilitates recruitment of the transcriptional repressor PRDM1/BLIMP1 to the promoter of the anti-osteoclastogenesis gene IRF8, thereby resulting in transcription of osteoclast differentiation factors (By similarity). May play a role in estrogen action (PubMed:14605097). {ECO:0000250\|UniProtKB:Q78T81, ECO:0000269\|PubMed:14605097}.
Q5VT06	CEP350	S261	ochoa	Centrosome-associated protein 350 (Cep350) (Centrosome-associated protein of 350 kDa)	Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CPAP (PubMed:19052644). Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity (PubMed:15615782). Required for ciliation (PubMed:28659385). {ECO:0000269\|PubMed:15615782, ECO:0000269\|PubMed:16314388, ECO:0000269\|PubMed:17878239, ECO:0000269\|PubMed:19052644, ECO:0000269\|PubMed:28659385}.
Q5VT52	RPRD2	S765	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VUA4	ZNF318	S1613	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q5VZ89	DENND4C	S1064	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q5VZ89	DENND4C	S1802	ochoa	DENN domain-containing protein 4C	Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269\|PubMed:20937701}.
Q63HK5	TSHZ3	S600	ochoa	Teashirt homolog 3 (Zinc finger protein 537)	Transcriptional regulator involved in developmental processes. Functions in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s) (PubMed:19343227). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter (By similarity). Involved in the modulation of glutamatergic synaptic transmission and long-term synaptic potentiation (By similarity). {ECO:0000250\|UniProtKB:Q8CGV9, ECO:0000269\|PubMed:19343227}.
Q66K74	MAP1S	S770	ochoa	Microtubule-associated protein 1S (MAP-1S) (BPY2-interacting protein 1) (Microtubule-associated protein 8) (Variable charge Y chromosome 2-interacting protein 1) (VCY2-interacting protein 1) (VCY2IP-1) [Cleaved into: MAP1S heavy chain; MAP1S light chain]	Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). {ECO:0000250, ECO:0000269\|PubMed:15899810, ECO:0000269\|PubMed:17234756}.
Q68D10	SPTY2D1	S321	ochoa	Protein SPT2 homolog (Protein KU002155) (SPT2 domain-containing protein 1)	Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Binds DNA and histones and promotes nucleosome assembly (in vitro) (PubMed:23378026, PubMed:26109053). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (PubMed:26109053). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (PubMed:23378026). {ECO:0000250\|UniProtKB:E1BUG7, ECO:0000269\|PubMed:23378026}.
Q68DQ2	CRYBG3	S350	ochoa	Very large A-kinase anchor protein (vlAKAP) (Beta/gamma crystallin domain-containing protein 3)	[Isoform vlAKAP]: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269\|PubMed:25097019}.
Q68DQ2	CRYBG3	S2104	ochoa	Very large A-kinase anchor protein (vlAKAP) (Beta/gamma crystallin domain-containing protein 3)	[Isoform vlAKAP]: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269\|PubMed:25097019}.
Q6IA17	SIGIRR	S383	ochoa	Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)	Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP. {ECO:0000269\|PubMed:12925853, ECO:0000269\|PubMed:14715412, ECO:0000269\|PubMed:15866876, ECO:0000269\|PubMed:25963006}.
Q6P0Q8	MAST2	S253	ochoa	Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1)	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.
Q6P0Q8	MAST2	S254	ochoa	Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1)	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.
Q6P2E9	EDC4	T738	ochoa	Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls)	In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269\|PubMed:16364915}.
Q6P4F7	ARHGAP11A	S585	ochoa	Rho GTPase-activating protein 11A (Rho-type GTPase-activating protein 11A)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000269\|PubMed:27957544}.
Q6PIJ6	FBXO38	S740	ochoa	F-box only protein 38	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of PDCD1/PD-1, thereby regulating T-cells-mediated immunity (PubMed:30487606). Required for anti-tumor activity of T-cells by promoting the degradation of PDCD1/PD-1; the PDCD1-mediated inhibitory pathway being exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (PubMed:30487606). May indirectly stimulate the activity of transcription factor KLF7, a regulator of neuronal differentiation, without promoting KLF7 ubiquitination (By similarity). {ECO:0000250\|UniProtKB:Q8BMI0, ECO:0000269\|PubMed:30487606}.
Q6PJE2	POMZP3	S36	ochoa	POM121 and ZP3 fusion protein (POM-ZP3)	None
Q6PKG0	LARP1	S853	ochoa	La-related protein 1 (La ribonucleoprotein domain family member 1)	RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543). {ECO:0000269\|PubMed:20430826, ECO:0000269\|PubMed:23711370, ECO:0000269\|PubMed:24532714, ECO:0000269\|PubMed:25940091, ECO:0000269\|PubMed:26206669, ECO:0000269\|PubMed:28379136, ECO:0000269\|PubMed:28650797, ECO:0000269\|PubMed:28673543, ECO:0000269\|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269\|PubMed:26735137}.
Q6PL18	ATAD2	S88	ochoa	ATPase family AAA domain-containing protein 2 (EC 3.6.1.-) (AAA nuclear coregulator cancer-associated protein) (ANCCA)	May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. {ECO:0000269\|PubMed:17998543}.
Q6R327	RICTOR	S1234	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1237	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6T4R5	NHS	S1480	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6VN20	RANBP10	S425	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6ZU35	CRACD	S1139	ochoa	Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics)	Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin. {ECO:0000269\|PubMed:30361697}.
Q6ZVL6	KIAA1549L	S1546	ochoa	UPF0606 protein KIAA1549L	None
Q70E73	RAPH1	S542	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q76L83	ASXL2	S142	ochoa	Putative Polycomb group protein ASXL2 (Additional sex combs-like protein 2)	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (PubMed:30664650, PubMed:36180891). The PR-DUB complex is an epigenetic regulator of gene expression and acts as a transcriptional coactivator, affecting genes involved in development, cell communication, signaling, cell proliferation and cell viability (PubMed:30664650, PubMed:36180891). ASXL1, ASXL2 and ASXL3 function redundantly in the PR-DUB complex (By similarity) (PubMed:30664650). The ASXL proteins are essential for chromatin recruitment and transcriptional activation of associated genes (By similarity). ASXL1 and ASXL2 are important for BAP1 protein stability (PubMed:30664650). {ECO:0000250, ECO:0000250\|UniProtKB:Q8BZ32, ECO:0000269\|PubMed:21047783, ECO:0000269\|PubMed:30664650, ECO:0000269\|PubMed:36180891}.
Q7KZI7	MARK2	S390	ochoa	Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:12429843, ECO:0000269\|PubMed:14976552, ECO:0000269\|PubMed:15158914, ECO:0000269\|PubMed:15324659, ECO:0000269\|PubMed:15365179, ECO:0000269\|PubMed:16775013, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:18626018, ECO:0000269\|PubMed:20194617, ECO:0000269\|PubMed:23666762}.
Q7Z3T8	ZFYVE16	S845	ochoa	Zinc finger FYVE domain-containing protein 16 (Endofin) (Endosome-associated FYVE domain protein)	May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes. {ECO:0000269\|PubMed:11546807, ECO:0000269\|PubMed:14613930}.
Q7Z422	SZRD1	S77	ochoa	SUZ RNA-binding domain-containing (SUZ domain-containing protein 1) (Putative MAPK-activating protein PM18/PM20/PM22)	None
Q7Z460	CLASP1	S559	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z478	DHX29	S75	ochoa	ATP-dependent RNA helicase DHX29 (EC 3.6.4.13) (DEAH box protein 29) (Nucleic acid helicase DDXx)	ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. {ECO:0000255\|HAMAP-Rule:MF_03068, ECO:0000269\|PubMed:19109895, ECO:0000269\|PubMed:23706745}.
Q7Z6B7	SRGAP1	Y944	ochoa	SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13)	GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269\|PubMed:11672528}.
Q7Z6J0	SH3RF1	S318	ochoa	E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING finger protein 142) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2)	Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination (PubMed:15659549, PubMed:20696164). Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis (PubMed:19710010). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). {ECO:0000250\|UniProtKB:Q69ZI1, ECO:0000269\|PubMed:15659549, ECO:0000269\|PubMed:19710010, ECO:0000269\|PubMed:20696164}.; FUNCTION: (Microbial infection) Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity. {ECO:0000269\|PubMed:15659549}.
Q7Z6Z7	HUWE1	S3380	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q86SQ0	PHLDB2	S351	ochoa	Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)	Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12376540}.
Q86SQ0	PHLDB2	S566	ochoa	Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)	Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12376540}.
Q86SQ4	ADGRG6	S1168	ochoa	Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: Adhesion G-protein coupled receptor G6, N-terminal fragment (ADGRG6 N-terminal fragment) (ADGRG6-NTF); Adhesion G-protein coupled receptor G6, C-terminal fragment (ADGRG6 C-terminal fragment) (ADGRG6-CTF)]	Adhesion G-protein coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (PubMed:35394864, PubMed:39884271). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:24227709, PubMed:35394864). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:24227709, PubMed:35394864). Also able to couple to G(q) G proteins (PubMed:24227709). Involved in myelination of the peripheral nervous system: required for differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Also acts as a regulator of body length and bone mass (PubMed:18391950). Acts as a regulator of blood-brain barrier formation in the central nervous system vie its association with LRP1 and ITGB1 (By similarity). {ECO:0000250\|UniProtKB:Q6F3F9, ECO:0000269\|PubMed:18391950, ECO:0000269\|PubMed:24227709, ECO:0000269\|PubMed:35394864, ECO:0000269\|PubMed:39884271}.
Q86TC9	MYPN	S258	ochoa	Myopalladin (145 kDa sarcomeric protein)	Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines. {ECO:0000269\|PubMed:11309420}.
Q86TV6	TTC7B	S681	ochoa	Tetratricopeptide repeat protein 7B (TPR repeat protein 7B) (Tetratricopeptide repeat protein 7-like-1) (TPR repeat protein 7-like-1)	Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and HYCC1, via direct interactions (PubMed:26571211). {ECO:0000269\|PubMed:23229899, ECO:0000269\|PubMed:26571211}.
Q86UU1	PHLDB1	S696	ochoa	Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha)	None
Q86UU1	PHLDB1	S988	ochoa	Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha)	None
Q86W92	PPFIBP1	S364	ochoa	Liprin-beta-1 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1) (PTPRF-interacting protein-binding protein 1) (hSGT2)	May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. {ECO:0000269\|PubMed:9624153}.
Q86X27	RALGPS2	S446	ochoa	Ras-specific guanine nucleotide-releasing factor RalGPS2 (Ral GEF with PH domain and SH3-binding motif 2) (RalA exchange factor RalGPS2)	Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion (By similarity). {ECO:0000250}.
Q86X29	LSR	S385	ochoa	Lipolysis-stimulated lipoprotein receptor (Angulin-1)	Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (By similarity). {ECO:0000250\|UniProtKB:Q99KG5, ECO:0000250\|UniProtKB:Q9WU74}.
Q86XA9	HEATR5A	S830	ochoa	HEAT repeat-containing protein 5A	None
Q86YD5	LDLRAD3	S313	ochoa	Low-density lipoprotein receptor class A domain-containing protein 3 (LDLR class A domain-containing protein 3)	May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (PubMed:26854353). {ECO:0000250, ECO:0000269\|PubMed:26854353}.; FUNCTION: (Microbial infection) Acts as a receptor for Venezuelan equine encephalitis virus. {ECO:0000269\|PubMed:33208938, ECO:0000269\|PubMed:34646020, ECO:0000269\|PubMed:34646021}.
Q8IU85	CAMK1D	S330	ochoa	Calcium/calmodulin-dependent protein kinase type 1D (EC 2.7.11.17) (CaM kinase I delta) (CaM kinase ID) (CaM-KI delta) (CaMKI delta) (CaMKID) (CaMKI-like protein kinase) (CKLiK)	Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta. {ECO:0000269\|PubMed:11050006, ECO:0000269\|PubMed:15840691, ECO:0000269\|PubMed:16324104, ECO:0000269\|PubMed:17056143}.
Q8IXZ2	ZC3H3	S880	ochoa	Zinc finger CCCH domain-containing protein 3 (Smad-interacting CPSF-like factor)	Required for the export of polyadenylated mRNAs from the nucleus (PubMed:19364924). Enhances ACVR1B-induced SMAD-dependent transcription. Binds to single-stranded DNA but not to double-stranded DNA in vitro. Involved in RNA cleavage (By similarity). {ECO:0000250\|UniProtKB:Q8CHP0, ECO:0000269\|PubMed:19364924}.
Q8IXZ2	ZC3H3	S881	ochoa	Zinc finger CCCH domain-containing protein 3 (Smad-interacting CPSF-like factor)	Required for the export of polyadenylated mRNAs from the nucleus (PubMed:19364924). Enhances ACVR1B-induced SMAD-dependent transcription. Binds to single-stranded DNA but not to double-stranded DNA in vitro. Involved in RNA cleavage (By similarity). {ECO:0000250\|UniProtKB:Q8CHP0, ECO:0000269\|PubMed:19364924}.
Q8IY26	PLPP6	S22	ochoa	Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 (EC 3.1.3.-) (EC 3.6.1.-) (EC 3.6.1.68) (Lipid phosphatase-related protein-B) (LPRP-B) (PA-PSP) (Phosphatidic acid phosphatase type 2 domain-containing protein 2) (PPAP2 domain-containing protein 2) (Phospholipid phosphatase 6) (Presqualene diphosphate phosphatase) (Type 1 polyisoprenoid diphosphate phosphatase)	Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269\|PubMed:16464866, ECO:0000269\|PubMed:18930839, ECO:0000269\|PubMed:19220020, ECO:0000269\|PubMed:20110354, ECO:0000269\|PubMed:23568778}.
Q8IY26	PLPP6	S23	ochoa	Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 (EC 3.1.3.-) (EC 3.6.1.-) (EC 3.6.1.68) (Lipid phosphatase-related protein-B) (LPRP-B) (PA-PSP) (Phosphatidic acid phosphatase type 2 domain-containing protein 2) (PPAP2 domain-containing protein 2) (Phospholipid phosphatase 6) (Presqualene diphosphate phosphatase) (Type 1 polyisoprenoid diphosphate phosphatase)	Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269\|PubMed:16464866, ECO:0000269\|PubMed:18930839, ECO:0000269\|PubMed:19220020, ECO:0000269\|PubMed:20110354, ECO:0000269\|PubMed:23568778}.
Q8IY92	SLX4	S960	ochoa	Structure-specific endonuclease subunit SLX4 (BTB/POZ domain-containing protein 12)	Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. Interacts with the structure-specific ERCC4-ERCC1 endonuclease and promotes the cleavage of bubble structures. Interacts with the structure-specific MUS81-EME1 endonuclease and promotes the cleavage of 3'-flap and replication fork-like structures. SLX4 is required for recovery from alkylation-induced DNA damage and is involved in the resolution of DNA double-strand breaks. {ECO:0000269\|PubMed:19595721, ECO:0000269\|PubMed:19595722, ECO:0000269\|PubMed:19596235, ECO:0000269\|PubMed:19596236}.
Q8IZP0	ABI1	S330	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8IZP0	ABI1	Y333	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8N3F8	MICALL1	S562	ochoa	MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13)	Lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, acts as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation (PubMed:19864458, PubMed:20801876, PubMed:23596323, PubMed:34100897). Involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking (PubMed:21795389). Alternatively, regulates slow endocytic recycling of endocytosed proteins back to the plasma membrane (PubMed:19864458). Also involved in cargo protein delivery to the plasma membrane (PubMed:34100897). Plays a role in ciliogenesis coordination, recruits EHD1 to primary cilium where it is anchored to the centriole through interaction with tubulins (PubMed:31615969). May indirectly play a role in neurite outgrowth (By similarity). {ECO:0000250\|UniProtKB:Q8BGT6, ECO:0000269\|PubMed:19864458, ECO:0000269\|PubMed:20801876, ECO:0000269\|PubMed:21795389, ECO:0000269\|PubMed:23596323, ECO:0000269\|PubMed:31615969, ECO:0000269\|PubMed:34100897}.
Q8N3U4	STAG2	S1068	ochoa	Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2)	Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269\|PubMed:12034751}.
Q8N3Z6	ZCCHC7	S485	ochoa	Zinc finger CCHC domain-containing protein 7 (TRAMP-like complex RNA-binding factor ZCCHC7)	None
Q8N6N3	C1orf52	S23	ochoa	UPF0690 protein C1orf52 (BCL10-associated gene protein)	None
Q8NCP5	ZBTB44	S168	ochoa	Zinc finger and BTB domain-containing protein 44 (BTB/POZ domain-containing protein 15) (Zinc finger protein 851)	May be involved in transcriptional regulation. {ECO:0000250}.
Q8ND30	PPFIBP2	S479	ochoa	Liprin-beta-2 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 2) (PTPRF-interacting protein-binding protein 2)	May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. {ECO:0000269\|PubMed:9624153}.
Q8ND83	SLAIN1	S250	ochoa	SLAIN motif-containing protein 1	Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269\|PubMed:21646404}.
Q8NDF8	TENT4B	S52	ochoa	Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)	Terminal nucleotidyltransferase that catalyzes preferentially the transfer of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:21788334, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro) (PubMed:21788334, PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation (PubMed:22442037). {ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:21788334, ECO:0000269\|PubMed:21855801, ECO:0000269\|PubMed:22442037, ECO:0000269\|PubMed:25049417, ECO:0000269\|PubMed:28383716, ECO:0000269\|PubMed:30026317}.
Q8NEY8	PPHLN1	Y154	ochoa	Periphilin-1 (CDC7 expression repressor) (CR) (Gastric cancer antigen Ga50)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269\|PubMed:15474462, ECO:0000269\|PubMed:17963697, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:30487602, ECO:0000305\|PubMed:12853457}.
Q8NEZ4	KMT2C	S3758	ochoa	Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.364) (Homologous to ALR protein) (Myeloid/lymphoid or mixed-lineage leukemia protein 3)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738). Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:22266653, PubMed:24081332, PubMed:25561738). Likely plays a redundant role with KMT2D in enriching H3K4me1 mark on primed and active enhancer elements (PubMed:24081332). {ECO:0000269\|PubMed:22266653, ECO:0000269\|PubMed:24081332, ECO:0000269\|PubMed:25561738}.
Q8NF91	SYNE1	S8258	ochoa	Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)	Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus-centrosome attachment and nuclear migration in neural progenitors implicating LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes; SYNE1 and SYNE2 may act redundantly. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250\|UniProtKB:Q6ZWR6, ECO:0000269\|PubMed:11792814, ECO:0000269\|PubMed:18396275}.
Q8NG31	KNL1	S1849	ochoa	Outer kinetochore KNL1 complex subunit KNL1 (ALL1-fused gene from chromosome 15q14 protein) (AF15q14) (Bub-linking kinetochore protein) (Blinkin) (Cancer susceptibility candidate gene 5 protein) (Cancer/testis antigen 29) (CT29) (Kinetochore scaffold 1) (Kinetochore-null protein 1) (Protein CASC5) (Protein D40/AF15q14)	Acts as a component of the outer kinetochore KNL1 complex that serves as a docking point for spindle assembly checkpoint components and mediates microtubule-kinetochore interactions (PubMed:15502821, PubMed:17981135, PubMed:18045986, PubMed:19893618, PubMed:21199919, PubMed:22000412, PubMed:22331848, PubMed:27881301, PubMed:30100357). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules (PubMed:18045986, PubMed:19893618, PubMed:27881301). The outer kinetochore is made up of the ten-subunit KMN network, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle (PubMed:17981135, PubMed:19893618, PubMed:22000412, PubMed:38459127, PubMed:38459128). Required for kinetochore binding by a distinct subset of kMAPs (kinetochore-bound microtubule-associated proteins) and motors (PubMed:19893618). Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore (PubMed:18045986, PubMed:27881301). Can bind either to microtubules or to the protein phosphatase 1 (PP1) catalytic subunits PPP1CA and PPP1CC (via overlapping binding sites), it has higher affinity for PP1 (PubMed:30100357). Recruits MAD2L1 to the kinetochore and also directly links BUB1 and BUB1B to the kinetochore (PubMed:17981135, PubMed:19893618, PubMed:22000412, PubMed:22331848, PubMed:25308863). In addition to orienting mitotic chromosomes, it is also essential for alignment of homologous chromosomes during meiotic metaphase I (By similarity). In meiosis I, required to activate the spindle assembly checkpoint at unattached kinetochores to correct erroneous kinetochore-microtubule attachments (By similarity). {ECO:0000250\|UniProtKB:Q66JQ7, ECO:0000269\|PubMed:15502821, ECO:0000269\|PubMed:17981135, ECO:0000269\|PubMed:18045986, ECO:0000269\|PubMed:19893618, ECO:0000269\|PubMed:21199919, ECO:0000269\|PubMed:22000412, ECO:0000269\|PubMed:22331848, ECO:0000269\|PubMed:25308863, ECO:0000269\|PubMed:27881301, ECO:0000269\|PubMed:30100357, ECO:0000269\|PubMed:38459127, ECO:0000269\|PubMed:38459128}.
Q8NHH9	ATL2	S38	ochoa	Atlastin-2 (ATL-2) (EC 3.6.5.-) (ADP-ribosylation factor-like protein 6-interacting protein 2)	Atlastin-2 (ATL2) is a membrane-anchored GTPase that mediates the GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the continuous ER network. It facilitates the formation of three-way junctions where ER tubules intersect (PubMed:18270207, PubMed:19665976, PubMed:22065636, PubMed:27619977, PubMed:34817557). Two atlastin-2 on neighboring ER tubules bind GTP and form loose homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon GTP hydrolysis, the 3HB regions tighten, pulling the membranes together to drive their fusion. After fusion, the homodimer disassembles upon release of inorganic phosphate (Pi). Subsequently, GDP dissociates, resetting the monomers to a conformation ready for a new fusion cycle (By similarity). {ECO:0000250\|UniProtKB:Q8WXF7, ECO:0000269\|PubMed:18270207, ECO:0000269\|PubMed:19665976, ECO:0000269\|PubMed:22065636, ECO:0000269\|PubMed:27619977, ECO:0000269\|PubMed:34817557}.
Q8TBP0	TBC1D16	S263	ochoa	TBC1 domain family member 16	May act as a GTPase-activating protein for Rab family protein(s).
Q8TCJ2	STT3B	S21	ochoa	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18) (Source of immunodominant MHC-associated peptides homolog)	Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). STT3B is present in a small subset of OST complexes (OST-B) and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A (PubMed:19167329, PubMed:22607976, PubMed:31296534, PubMed:39509507). STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins (PubMed:19167329, PubMed:22607976, PubMed:39509507). Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation (PubMed:19167329, PubMed:22607976). Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation (PubMed:19167329, PubMed:22607976). {ECO:0000269\|PubMed:19167329, ECO:0000269\|PubMed:22607976, ECO:0000269\|PubMed:31296534, ECO:0000269\|PubMed:31831667, ECO:0000269\|PubMed:39509507}.
Q8TEQ6	GEMIN5	S624	ochoa	Gem-associated protein 5 (Gemin5)	The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:16857593, PubMed:18984161, PubMed:20513430, PubMed:33963192). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex (PubMed:11714716, PubMed:16314521, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601). Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.27). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887). {ECO:0000269\|PubMed:11714716, ECO:0000269\|PubMed:16314521, ECO:0000269\|PubMed:16857593, ECO:0000269\|PubMed:18984161, ECO:0000269\|PubMed:19377484, ECO:0000269\|PubMed:19750007, ECO:0000269\|PubMed:20513430, ECO:0000269\|PubMed:25911097, ECO:0000269\|PubMed:27507887, ECO:0000269\|PubMed:27834343, ECO:0000269\|PubMed:27881600, ECO:0000269\|PubMed:27881601, ECO:0000269\|PubMed:33963192, ECO:0000269\|Ref.27}.
Q8WUA4	GTF3C2	S776	ochoa	General transcription factor 3C polypeptide 2 (TF3C-beta) (Transcription factor IIIC 110 kDa subunit) (TFIIIC 110 kDa subunit) (TFIIIC110) (Transcription factor IIIC subunit beta)	Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1.
Q8WUM0	NUP133	S60	ochoa	Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133)	Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269\|PubMed:11684705, ECO:0000269\|PubMed:30179222}.
Q8WWI1	LMO7	S972	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWM7	ATXN2L	S276	ochoa	Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein)	Involved in the regulation of stress granule and P-body formation. {ECO:0000269\|PubMed:23209657}.
Q8WXG6	MADD	S833	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S1202	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q92545	TMEM131	S1345	ochoa	Transmembrane protein 131 (Protein RW1)	Collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII (PubMed:32095531). May play a role in the immune response to viral infection. {ECO:0000250, ECO:0000269\|PubMed:32095531}.
Q92545	TMEM131	S1630	ochoa	Transmembrane protein 131 (Protein RW1)	Collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII (PubMed:32095531). May play a role in the immune response to viral infection. {ECO:0000250, ECO:0000269\|PubMed:32095531}.
Q92576	PHF3	S345	ochoa	PHD finger protein 3	None
Q92793	CREBBP	S980	ochoa	CREB-binding protein (Histone lysine acetyltransferase CREBBP) (EC 2.3.1.48) (Protein lactyltransferas CREBBP) (EC 2.3.1.-) (Protein-lysine acetyltransferase CREBBP) (EC 2.3.1.-)	Acetylates histones, giving a specific tag for transcriptional activation (PubMed:21131905, PubMed:24616510). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, PubMed:24207024, PubMed:28790157, PubMed:30540930, PubMed:35675826, PubMed:9707565). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (PubMed:14645221). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:24207024). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (PubMed:28790157). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed:30540930). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as lactoyl-CoA, and is able to mediate protein lactylation (PubMed:38128537). Catalyzes lactylation of MRE11 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38128537). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493). {ECO:0000269\|PubMed:10490106, ECO:0000269\|PubMed:11154691, ECO:0000269\|PubMed:12738767, ECO:0000269\|PubMed:12929931, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:21131905, ECO:0000269\|PubMed:24207024, ECO:0000269\|PubMed:24616510, ECO:0000269\|PubMed:24939902, ECO:0000269\|PubMed:25514493, ECO:0000269\|PubMed:28790157, ECO:0000269\|PubMed:30540930, ECO:0000269\|PubMed:35675826, ECO:0000269\|PubMed:38128537, ECO:0000269\|PubMed:9707565}.
Q92841	DDX17	S675	ochoa	Probable ATP-dependent RNA helicase DDX17 (EC 3.6.4.13) (DEAD box protein 17) (DEAD box protein p72) (DEAD box protein p82) (RNA-dependent helicase p72)	As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features (PubMed:12138182, PubMed:22266867, PubMed:23022728, PubMed:24910439). For instance, promotes the inclusion of AC-rich alternative exons in CD44 transcripts (PubMed:12138182). This function requires the RNA helicase activity (PubMed:12138182, PubMed:22266867, PubMed:23022728, PubMed:24910439). Affects NFAT5 and histone macro-H2A.1/MACROH2A1 alternative splicing in a CDK9-dependent manner (PubMed:22266867, PubMed:26209609). In NFAT5, promotes the introduction of alternative exon 4, which contains 2 stop codons and may target NFAT5 exon 4-containing transcripts to nonsense-mediated mRNA decay, leading to the down-regulation of NFAT5 protein (PubMed:22266867). Affects splicing of mediators of steroid hormone signaling pathway, including kinases that phosphorylates ESR1, such as CDK2, MAPK1 and GSK3B, and transcriptional regulators, such as CREBBP, MED1, NCOR1 and NCOR2. By affecting GSK3B splicing, participates in ESR1 and AR stabilization (PubMed:24275493). In myoblasts and epithelial cells, cooperates with HNRNPH1 to control the splicing of specific subsets of exons (PubMed:24910439). In addition to binding mature mRNAs, also interacts with certain pri-microRNAs, including MIR663/miR-663a, MIR99B/miR-99b, and MIR6087/miR-6087 (PubMed:25126784). Binds pri-microRNAs on the 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3' consensus sequence (PubMed:24581491). Required for the production of subsets of microRNAs, including MIR21 and MIR125B1 (PubMed:24581491, PubMed:27478153). May be involved not only in microRNA primary transcript processing, but also stabilization (By similarity). Participates in MYC down-regulation at high cell density through the production of MYC-targeting microRNAs (PubMed:24581491). Along with DDX5, may be involved in the processing of the 32S intermediate into the mature 28S ribosomal RNA (PubMed:17485482). Promoter-specific transcription regulator, functioning as a coactivator or corepressor depending on the context of the promoter and the transcriptional complex in which it exists (PubMed:15298701). Enhances NFAT5 transcriptional activity (PubMed:22266867). Synergizes with TP53 in the activation of the MDM2 promoter; this activity requires acetylation on lysine residues (PubMed:17226766, PubMed:19995069, PubMed:20663877). May also coactivate MDM2 transcription through a TP53-independent pathway (PubMed:17226766). Coactivates MMP7 transcription (PubMed:17226766). Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1 transcription (PubMed:17699760). Alone or in combination with DDX5 and/or SRA1 non-coding RNA, plays a critical role in promoting the assembly of proteins required for the formation of the transcription initiation complex and chromatin remodeling leading to coactivation of MYOD1-dependent transcription. This helicase-independent activity is required for skeletal muscle cells to properly differentiate into myotubes (PubMed:17011493, PubMed:24910439). During epithelial-to-mesenchymal transition, coregulates SMAD-dependent transcriptional activity, directly controlling key effectors of differentiation, including miRNAs which in turn directly repress its expression (PubMed:24910439). Plays a role in estrogen and testosterone signaling pathway at several levels. Mediates the use of alternative promoters in estrogen-responsive genes and regulates transcription and splicing of a large number of steroid hormone target genes (PubMed:19995069, PubMed:20406972, PubMed:20663877, PubMed:24275493). Contrary to splicing regulation activity, transcriptional coregulation of the estrogen receptor ESR1 is helicase-independent (PubMed:19718048, PubMed:24275493). Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner (PubMed:25126784). Binds to RVFV RNA, likely via structured viral RNA elements (PubMed:25126784). Promotes mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in an ATPase-dependent manner (PubMed:18334637). {ECO:0000250\|UniProtKB:Q501J6, ECO:0000269\|PubMed:12138182, ECO:0000269\|PubMed:15298701, ECO:0000269\|PubMed:17011493, ECO:0000269\|PubMed:17226766, ECO:0000269\|PubMed:17485482, ECO:0000269\|PubMed:17699760, ECO:0000269\|PubMed:18334637, ECO:0000269\|PubMed:19718048, ECO:0000269\|PubMed:19995069, ECO:0000269\|PubMed:20406972, ECO:0000269\|PubMed:20663877, ECO:0000269\|PubMed:22266867, ECO:0000269\|PubMed:23022728, ECO:0000269\|PubMed:24275493, ECO:0000269\|PubMed:24581491, ECO:0000269\|PubMed:24910439, ECO:0000269\|PubMed:25126784, ECO:0000269\|PubMed:26209609, ECO:0000269\|PubMed:27478153, ECO:0000305}.
Q92994	BRF1	S436	ochoa	Transcription factor IIIB 90 kDa subunit (TFIIIB90) (hTFIIIB90) (B-related factor 1) (BRF-1) (hBRF) (TAF3B2) (TATA box-binding protein-associated factor, RNA polymerase III, subunit 2)	General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.
Q969R2	OSBP2	S766	ochoa\|psp	Oxysterol-binding protein 2 (Oxysterol-binding protein-related protein 4) (ORP-4) (OSBP-related protein 4)	Binds 7-ketocholesterol (PubMed:11278871). Acts during spermatid development where its function is required prior to the removal of cytoplasm from the sperm head (By similarity). {ECO:0000250\|UniProtKB:Q8CF21, ECO:0000269\|PubMed:11278871}.
Q96AP7	ESAM	S371	ochoa	Endothelial cell-selective adhesion molecule	Can mediate aggregation most likely through a homophilic molecular interaction. {ECO:0000250\|UniProtKB:Q925F2}.
Q96B97	SH3KBP1	S502	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96B97	SH3KBP1	S503	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96CV9	OPTN	S174	ochoa	Optineurin (E3-14.7K-interacting protein) (FIP-2) (Huntingtin yeast partner L) (Huntingtin-interacting protein 7) (HIP-7) (Huntingtin-interacting protein L) (NEMO-related protein) (Optic neuropathy-inducing protein) (Transcription factor IIIA-interacting protein) (TFIIIA-IntP)	Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269\|PubMed:11834836, ECO:0000269\|PubMed:15837803, ECO:0000269\|PubMed:20085643, ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:21617041, ECO:0000269\|PubMed:22854040, ECO:0000269\|PubMed:27534431, ECO:0000269\|PubMed:27538435}.; FUNCTION: (Microbial infection) May constitute a cellular target for various viruses, such as adenovirus E3 14.7 or Bluetongue virus, to inhibit innate immune response (PubMed:27538435, PubMed:9488477). During RNA virus infection, such as that of Sendai virus, negatively regulates the induction of IFNB1 (PubMed:20174559). {ECO:0000269\|PubMed:20174559, ECO:0000269\|PubMed:27538435, ECO:0000269\|PubMed:9488477}.
Q96HA1	POM121	S301	ochoa	Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
Q96HA1	POM121	S396	ochoa	Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
Q96HI0	SENP5	S363	ochoa	Sentrin-specific protease 5 (EC 3.4.22.-) (Sentrin/SUMO-specific protease SENP5)	Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division. {ECO:0000269\|PubMed:16608850, ECO:0000269\|PubMed:16738315}.
Q96JT2	SLC45A3	S426	ochoa	Solute carrier family 45 member 3 (Prostate cancer-associated protein 6) (Prostein)	Proton-associated sucrose transporter. May be able to transport also glucose and fructose. {ECO:0000250\|UniProtKB:Q8K0H7}.
Q96JY6	PDLIM2	S206	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96K76	USP47	S968	ochoa	Ubiquitin carboxyl-terminal hydrolase 47 (EC 3.4.19.12) (Deubiquitinating enzyme 47) (Ubiquitin thioesterase 47) (Ubiquitin-specific-processing protease 47)	Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulate CDC25A expression at a transcriptional level. {ECO:0000269\|PubMed:19966869, ECO:0000269\|PubMed:21362556}.
Q96NE9	FRMD6	S429	ochoa	FERM domain-containing protein 6 (Willin)	None
Q96QD8	SLC38A2	S22	ochoa	Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Protein 40-9-1) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)	Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10930503, PubMed:15774260, PubMed:15922329, PubMed:16621798). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (PubMed:10930503, PubMed:15774260). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250\|UniProtKB:Q8CFE6, ECO:0000250\|UniProtKB:Q9JHE5, ECO:0000269\|PubMed:10930503, ECO:0000269\|PubMed:15774260, ECO:0000269\|PubMed:15922329, ECO:0000269\|PubMed:16621798}.
Q96QE3	ATAD5	S141	ochoa	ATPase family AAA domain-containing protein 5 (Chromosome fragility-associated gene 1 protein)	Has an important role in DNA replication and in maintaining genome integrity during replication stress (PubMed:15983387, PubMed:19755857). Involved in a RAD9A-related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis (PubMed:15983387). Modulates the RAD9A interaction with BCL2 and thereby induces DNA damage-induced apoptosis (PubMed:15983387). Promotes PCNA deubiquitination by recruiting the ubiquitin-specific protease 1 (USP1) and WDR48 thereby down-regulating the error-prone damage bypass pathway (PubMed:20147293). As component of the ATAD5 RFC-like complex, regulates the function of the DNA polymerase processivity factor PCNA by unloading the ring-shaped PCNA homotrimer from DNA after replication during the S phase of the cell cycle (PubMed:23277426, PubMed:23937667). This seems to be dependent on its ATPase activity (PubMed:23277426). Plays important roles in restarting stalled replication forks under replication stress, by unloading the PCNA homotrimer from DNA and recruiting RAD51 possibly through an ATR-dependent manner (PubMed:31844045). Ultimately this enables replication fork regression, breakage, and eventual fork restart (PubMed:31844045). Both the PCNA unloading activity and the interaction with WDR48 are required to efficiently recruit RAD51 to stalled replication forks (PubMed:31844045). Promotes the generation of MUS81-mediated single-stranded DNA-associated breaks in response to replication stress, which is an alternative pathway to restart stalled/regressed replication forks (PubMed:31844045). {ECO:0000269\|PubMed:15983387, ECO:0000269\|PubMed:19755857, ECO:0000269\|PubMed:20147293, ECO:0000269\|PubMed:23277426, ECO:0000269\|PubMed:23937667, ECO:0000269\|PubMed:31844045}.
Q96RS0	TGS1	S310	ochoa	Trimethylguanosine synthase (EC 2.1.1.-) (CLL-associated antigen KW-2) (Cap-specific guanine-N(2) methyltransferase) (Hepatocellular carcinoma-associated antigen 137) (Nuclear receptor coactivator 6-interacting protein) (PRIP-interacting protein with methyltransferase motif) (PIMT) (PIPMT)	Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation. {ECO:0000269\|PubMed:11517327, ECO:0000269\|PubMed:11912212, ECO:0000269\|PubMed:16687569, ECO:0000269\|PubMed:18775984}.
Q96RU2	USP28	S521	ochoa	Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)	Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells (PubMed:24623306). {ECO:0000269\|PubMed:16901786, ECO:0000269\|PubMed:17558397, ECO:0000269\|PubMed:17873522, ECO:0000269\|PubMed:18662541, ECO:0000269\|PubMed:24623306}.
Q96TA1	NIBAN2	S728	ochoa	Protein Niban 2 (Meg-3) (Melanoma invasion by ERK) (MINERVA) (Niban-like protein 1) (Protein FAM129B)	May play a role in apoptosis suppression. May promote melanoma cell invasion in vitro. {ECO:0000269\|PubMed:19362540, ECO:0000269\|PubMed:21148485}.
Q99081	TCF12	S47	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	Y307	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99683	MAP3K5	S1231	ochoa	Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269\|PubMed:10411906, ECO:0000269\|PubMed:10688666, ECO:0000269\|PubMed:10849426, ECO:0000269\|PubMed:11029458, ECO:0000269\|PubMed:11154276, ECO:0000269\|PubMed:11689443, ECO:0000269\|PubMed:11920685, ECO:0000269\|PubMed:14688258, ECO:0000269\|PubMed:14749717, ECO:0000269\|PubMed:15023544, ECO:0000269\|PubMed:16129676, ECO:0000269\|PubMed:17220297, ECO:0000269\|PubMed:23102700, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:8940179, ECO:0000269\|PubMed:8974401, ECO:0000269\|PubMed:9564042, ECO:0000269\|PubMed:9774977}.
Q99698	LYST	S2170	ochoa	Lysosomal-trafficking regulator (Beige homolog)	Adapter protein that regulates and/or fission of intracellular vesicles such as lysosomes (PubMed:11984006, PubMed:25216107). Might regulate trafficking of effectors involved in exocytosis (PubMed:25425525). In cytotoxic T-cells and natural killer (NK) cells, has role in the regulation of size, number and exocytosis of lytic granules (PubMed:26478006). In macrophages and dendritic cells, regulates phagosome maturation by controlling the conversion of early phagosomal compartments into late phagosomes (By similarity). In macrophages and dendritic cells, specifically involved in TLR3- and TLR4-induced production of pro-inflammatory cytokines by regulating the endosomal TLR3- TICAM1/TRIF and TLR4- TICAM1/TRIF signaling pathways (PubMed:27881733). {ECO:0000250\|UniProtKB:P97412, ECO:0000269\|PubMed:11984006, ECO:0000269\|PubMed:25216107, ECO:0000269\|PubMed:25425525, ECO:0000269\|PubMed:26478006, ECO:0000269\|PubMed:27881733}.
Q99728	BARD1	S367	ochoa	BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1)	E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. {ECO:0000269\|PubMed:12890688, ECO:0000269\|PubMed:14976165, ECO:0000269\|PubMed:20351172}.
Q99755	PIP5K1A	S479	ochoa	Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha)	Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:21477596, PubMed:22942276, PubMed:8955136). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (PubMed:19158393, PubMed:20660631). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (PubMed:22942276). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup (By similarity). Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (PubMed:19158393). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane (PubMed:20660631). Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (PubMed:18288197). {ECO:0000250\|UniProtKB:P70182, ECO:0000269\|PubMed:18288197, ECO:0000269\|PubMed:19158393, ECO:0000269\|PubMed:20660631, ECO:0000269\|PubMed:21477596, ECO:0000269\|PubMed:22942276, ECO:0000269\|PubMed:8955136}.
Q99959	PKP2	S135	ochoa	Plakophilin-2	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:25208567). Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (PubMed:23884246). Required to maintain gingival epithelial barrier function (PubMed:34368962). Important component of the desmosome that is also required for localization of desmosome component proteins such as DSC2, DSG2 and JUP to the desmosome cell-cell junction (PubMed:22781308, PubMed:25208567). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (By similarity). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes, via ANK3 stabilization and modulation of SCN5A/Nav1.5 localization to cell-cell junctions (By similarity). Required for mitochondrial function, nuclear envelope integrity and positive regulation of SIRT3 transcription via maintaining DES localization at its nuclear envelope and cell tip anchoring points, and thereby preserving regulation of the transcriptional program (PubMed:35959657). Maintenance of nuclear envelope integrity protects against DNA damage and transcriptional dysregulation of genes, especially those involved in the electron transport chain, thereby preserving mitochondrial function and protecting against superoxide radical anion generation (PubMed:35959657). Binds single-stranded DNA (ssDNA) (PubMed:20613778). May regulate the localization of GJA1 to gap junctions in intercalated disks of the heart (PubMed:18662195). Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297). Acts as a host restriction factor for IAV viral propagation, potentially via disrupting the interaction of IAV polymerase complex proteins (PubMed:28169297). {ECO:0000250\|UniProtKB:F1M7L9, ECO:0000250\|UniProtKB:Q9CQ73, ECO:0000269\|PubMed:18662195, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:22781308, ECO:0000269\|PubMed:23884246, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:28169297, ECO:0000269\|PubMed:34368962, ECO:0000269\|PubMed:35959657}.
Q99959	PKP2	S297	ochoa	Plakophilin-2	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:25208567). Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (PubMed:23884246). Required to maintain gingival epithelial barrier function (PubMed:34368962). Important component of the desmosome that is also required for localization of desmosome component proteins such as DSC2, DSG2 and JUP to the desmosome cell-cell junction (PubMed:22781308, PubMed:25208567). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (By similarity). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes, via ANK3 stabilization and modulation of SCN5A/Nav1.5 localization to cell-cell junctions (By similarity). Required for mitochondrial function, nuclear envelope integrity and positive regulation of SIRT3 transcription via maintaining DES localization at its nuclear envelope and cell tip anchoring points, and thereby preserving regulation of the transcriptional program (PubMed:35959657). Maintenance of nuclear envelope integrity protects against DNA damage and transcriptional dysregulation of genes, especially those involved in the electron transport chain, thereby preserving mitochondrial function and protecting against superoxide radical anion generation (PubMed:35959657). Binds single-stranded DNA (ssDNA) (PubMed:20613778). May regulate the localization of GJA1 to gap junctions in intercalated disks of the heart (PubMed:18662195). Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297). Acts as a host restriction factor for IAV viral propagation, potentially via disrupting the interaction of IAV polymerase complex proteins (PubMed:28169297). {ECO:0000250\|UniProtKB:F1M7L9, ECO:0000250\|UniProtKB:Q9CQ73, ECO:0000269\|PubMed:18662195, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:22781308, ECO:0000269\|PubMed:23884246, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:28169297, ECO:0000269\|PubMed:34368962, ECO:0000269\|PubMed:35959657}.
Q9BVC5	C2orf49	S150	ochoa	Ashwin	None
Q9BW04	SARG	S39	ochoa	Specifically androgen-regulated gene protein	Putative androgen-specific receptor. {ECO:0000269\|PubMed:15525603}.
Q9BW04	SARG	S313	ochoa	Specifically androgen-regulated gene protein	Putative androgen-specific receptor. {ECO:0000269\|PubMed:15525603}.
Q9BXB4	OSBPL11	S181	ochoa	Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11)	Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:23028956, ECO:0000269\|PubMed:39106189}.
Q9BZ67	FRMD8	S24	ochoa	FERM domain-containing protein 8 (Band4.1 inhibitor LRP interactor) (Bili) (iRhom tail-associated protein) (iTAP)	Promotes the cell surface stability of iRhom1/RHBDF1 and iRhom2/RHBDF2 and prevents their degradation via the endolysosomal pathway. By acting on iRhoms, involved in ADAM17-mediated shedding of TNF, amphiregulin/AREG, HBEGF and TGFA from the cell surface (PubMed:29897333, PubMed:29897336). Negatively regulates Wnt signaling, possibly by antagonizing the recruitment of AXIN1 to LRP6 (PubMed:19572019). {ECO:0000269\|PubMed:19572019, ECO:0000269\|PubMed:29897333, ECO:0000269\|PubMed:29897336}.
Q9BZ68	FRMD8P1	S24	ochoa	Putative FERM domain-containing protein FRMD8P1 (FERM domain-containing 8 pseudogene 1)	None
Q9BZB8	CPEB1	S184	ochoa	Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (h-CPEB) (hCPEB-1)	Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (PubMed:24990967). In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry (PubMed:26398195). {ECO:0000250\|UniProtKB:P70166, ECO:0000269\|PubMed:15731006, ECO:0000269\|PubMed:15966895, ECO:0000269\|PubMed:24990967, ECO:0000269\|PubMed:26398195}.
Q9C0B0	UNK	S378	ochoa\|psp	RING finger protein unkempt homolog (Zinc finger CCCH domain-containing protein 5)	Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280). {ECO:0000269\|PubMed:25737280}.
Q9C0B0	UNK	S479	psp	RING finger protein unkempt homolog (Zinc finger CCCH domain-containing protein 5)	Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280). {ECO:0000269\|PubMed:25737280}.
Q9C0B5	ZDHHC5	S432	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0D0	PHACTR1	S190	ochoa	Phosphatase and actin regulator 1	Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity (PubMed:21798305, PubMed:21939755). Involved in the regulation of cortical neuron migration and dendrite arborization (By similarity). {ECO:0000250\|UniProtKB:Q2M3X8, ECO:0000269\|PubMed:21798305, ECO:0000269\|PubMed:21939755}.
Q9C0D5	TANC1	S217	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9H1H9	KIF13A	S1763	ochoa	Kinesin-like protein KIF13A (Kinesin-like protein RBKIN)	Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abscission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269\|PubMed:19841138, ECO:0000269\|PubMed:20208530}.
Q9H201	EPN3	S192	ochoa	Epsin-3 (EPS-15-interacting protein 3)	None
Q9H4A3	WNK1	S34	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4L5	OSBPL3	S330	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H6A9	PCNX3	S711	ochoa	Pecanex-like protein 3 (Pecanex homolog protein 3)	None
Q9H6K5	PRR36	S1128	ochoa	Proline-rich protein 36	None
Q9H6U6	BCAS3	S161	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H706	GAREM1	S625	ochoa	GRB2-associated and regulator of MAPK protein 1 (GRB2-associated and regulator of MAPK1)	[Isoform 1]: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation. {ECO:0000269\|PubMed:19509291}.
Q9H7S9	ZNF703	S216	ochoa	Zinc finger protein 703 (Zinc finger elbow-related proline domain protein 1)	Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development. {ECO:0000269\|PubMed:21328542, ECO:0000269\|PubMed:21337521}.
Q9H7S9	ZNF703	S217	ochoa	Zinc finger protein 703 (Zinc finger elbow-related proline domain protein 1)	Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development. {ECO:0000269\|PubMed:21328542, ECO:0000269\|PubMed:21337521}.
Q9H8G2	CAAP1	S96	ochoa	Caspase activity and apoptosis inhibitor 1 (Conserved anti-apoptotic protein) (CAAP)	Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop. {ECO:0000269\|PubMed:21980415}.
Q9HAW4	CLSPN	S774	ochoa	Claspin (hClaspin)	Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation (PubMed:12766152, PubMed:15190204, PubMed:15707391, PubMed:16123041). Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins (PubMed:12766152, PubMed:15096610, PubMed:15707391, PubMed:16123041). Also required to maintain normal rates of replication fork progression during unperturbed DNA replication. Binds directly to DNA, with particular affinity for branched or forked molecules and interacts with multiple protein components of the replisome such as the MCM2-7 complex and TIMELESS (PubMed:15226314, PubMed:34694004, PubMed:35585232). Important for initiation of DNA replication, recruits kinase CDC7 to phosphorylate MCM2-7 components (PubMed:27401717). {ECO:0000269\|PubMed:12766152, ECO:0000269\|PubMed:15096610, ECO:0000269\|PubMed:15190204, ECO:0000269\|PubMed:15226314, ECO:0000269\|PubMed:15707391, ECO:0000269\|PubMed:16123041, ECO:0000269\|PubMed:27401717, ECO:0000269\|PubMed:34694004, ECO:0000269\|PubMed:35585232}.
Q9HCD5	NCOA5	S381	ochoa	Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA)	Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). {ECO:0000269\|PubMed:15073177}.
Q9HDC5	JPH1	S577	ochoa	Junctophilin-1 (JP-1) (Junctophilin type 1)	Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Q9NP61	ARFGAP3	S457	ochoa	ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3)	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269\|PubMed:11172815}.
Q9NRY4	ARHGAP35	S773	ochoa	Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Glucocorticoid receptor repression factor 1) (GRF-1) (Rho GAP p190A) (p190-A)	Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492). This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (PubMed:1894621). {ECO:0000250\|UniProtKB:P81128, ECO:0000250\|UniProtKB:Q91YM2, ECO:0000269\|PubMed:1894621, ECO:0000269\|PubMed:19673492, ECO:0000269\|PubMed:28894085}.
Q9NSI8	SAMSN1	S347	ochoa	SAM domain-containing protein SAMSN-1 (Hematopoietic adaptor containing SH3 and SAM domains 1) (Nash1) (SAM domain, SH3 domain and nuclear localization signals protein 1) (SH3-SAM adaptor protein)	Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation (By similarity). {ECO:0000250, ECO:0000269\|PubMed:15381729}.
Q9NUQ6	SPATS2L	S120	ochoa	SPATS2-like protein (DNA polymerase-transactivated protein 6) (Stress granule and nucleolar protein) (SGNP)	None
Q9NWH9	SLTM	S1002	ochoa	SAFB-like transcription modulator (Modulator of estrogen-induced transcription)	When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000250}.
Q9NZB2	FAM120A	S1048	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9P0J7	KCMF1	S223	ochoa	E3 ubiquitin-protein ligase KCMF1 (EC 2.3.2.27) (FGF-induced in gastric cancer) (Potassium channel modulatory factor) (PCMF) (ZZ-type zinc finger-containing protein 1)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and then transfers it to targeted substrates, promoting their degradation by the proteasome (PubMed:15581609, PubMed:25582440, PubMed:34893540, PubMed:37891180, PubMed:38297121). Together with UBR4, component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (PubMed:34893540, PubMed:37891180). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:37891180). Together with UBR4, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy (PubMed:34893540). Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). {ECO:0000269\|PubMed:15581609, ECO:0000269\|PubMed:25582440, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:37891180, ECO:0000269\|PubMed:38297121}.
Q9P0K7	RAI14	S293	ochoa	Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14)	Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250\|UniProtKB:Q5U312}.
Q9P206	NHSL3	S342	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P206	NHSL3	S573	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P219	CCDC88C	S1584	ochoa	Protein Daple (Coiled-coil domain-containing protein 88C) (Dvl-associating protein with a high frequency of leucine residues) (hDaple) (Hook-related protein 2) (HkRP2)	Required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling (PubMed:26126266). Binds to ligand-activated Wnt receptor FZD7, displacing DVL1 from the FZD7 receptor and leading to inhibition of canonical Wnt signaling (PubMed:26126266). Acts as a non-receptor guanine nucleotide exchange factor by also binding to guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits, leading to their activation (PubMed:26126266). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex, triggering non-canonical Wnt responses such as activation of RAC1 and PI3K-AKT signaling (PubMed:26126266). Promotes apical constriction of cells via ARHGEF18 (PubMed:30948426). {ECO:0000269\|PubMed:26126266, ECO:0000269\|PubMed:30948426}.
Q9P265	DIP2B	S186	ochoa	Disco-interacting protein 2 homolog B (DIP2 homolog B)	Negatively regulates axonal outgrowth and is essential for normal synaptic transmission. Not required for regulation of axon polarity. Promotes acetylation of alpha-tubulin. {ECO:0000250\|UniProtKB:Q3UH60}.
Q9P270	SLAIN2	S254	ochoa	SLAIN motif-containing protein 2	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269\|PubMed:21646404}.
Q9P2B4	CTTNBP2NL	Y447	ochoa	CTTNBP2 N-terminal-like protein	Regulates lamellipodial actin dynamics in a CTTN-dependent manner (By similarity). Associates with core striatin-interacting phosphatase and kinase (STRIPAK) complex to form CTTNBP2NL-STRIPAK complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753). {ECO:0000250\|UniProtKB:Q8SX68, ECO:0000269\|PubMed:18782753}.
Q9P2P5	HECW2	S407	ochoa	E3 ubiquitin-protein ligase HECW2 (EC 2.3.2.26) (HECT, C2 and WW domain-containing protein 2) (HECT-type E3 ubiquitin transferase HECW2) (NEDD4-like E3 ubiquitin-protein ligase 2)	E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73 (PubMed:12890487). Involved in the regulation of mitotic metaphase/anaphase transition (PubMed:24163370). {ECO:0000269\|PubMed:12890487, ECO:0000269\|PubMed:24163370}.
Q9P2Q2	FRMD4A	S953	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9UBC2	EPS15L1	S250	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBW7	ZMYM2	S1064	psp	Zinc finger MYM-type protein 2 (Fused in myeloproliferative disorders protein) (Rearranged in atypical myeloproliferative disorder protein) (Zinc finger protein 198)	Involved in the negative regulation of transcription. {ECO:0000269\|PubMed:32891193}.
Q9UHB7	AFF4	S598	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UHB7	AFF4	S1074	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UHC7	MKRN1	S135	ochoa	E3 ubiquitin-protein ligase makorin-1 (EC 2.3.2.27) (RING finger protein 61) (RING-type E3 ubiquitin transferase makorin-1)	E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II-dependent transcription. {ECO:0000269\|PubMed:16785614, ECO:0000269\|PubMed:19536131}.
Q9UIG0	BAZ1B	S330	ochoa	Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor) (Williams-Beuren syndrome chromosomal region 10 protein) (Williams-Beuren syndrome chromosomal region 9 protein) (hWALp2)	Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator (PubMed:19092802). Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph) (PubMed:19092802, PubMed:19234442). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19092802, PubMed:19234442). Regulatory subunit of the ATP-dependent WICH-1 and WICH-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:11980720, PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The WICH-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the WICH-5 ISWI chromatin remodeling complex (PubMed:28801535). The WICH-5 ISWI chromatin-remodeling complex regulates the transcription of various genes, has a role in RNA polymerase I transcription (By similarity). Within the B-WICH complex has a role in RNA polymerase III transcription (PubMed:16603771). Mediates the recruitment of the WICH-5 ISWI chromatin remodeling complex to replication foci during DNA replication (PubMed:15543136). {ECO:0000250\|UniProtKB:Q9Z277, ECO:0000269\|PubMed:11980720, ECO:0000269\|PubMed:15543136, ECO:0000269\|PubMed:16603771, ECO:0000269\|PubMed:19092802, ECO:0000269\|PubMed:19234442, ECO:0000269\|PubMed:28801535}.
Q9UIW2	PLXNA1	S1635	ochoa	Plexin-A1 (Semaphorin receptor NOV)	Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. Acts as coreceptor of TREM2 for SEMA6D in dendritic cells and is involved in the generation of immune responses and skeletal homeostasis. {ECO:0000250\|UniProtKB:P70206}.
Q9UJF2	RASAL2	S928	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9UKE5	TNIK	S734	ochoa	TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)	Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269\|PubMed:10521462, ECO:0000269\|PubMed:15342639, ECO:0000269\|PubMed:19061864, ECO:0000269\|PubMed:19816403, ECO:0000269\|PubMed:20159449, ECO:0000269\|PubMed:21690388, ECO:0000269\|PubMed:26437443}.
Q9UKF7	PITPNC1	S277	ochoa	Cytoplasmic phosphatidylinositol transfer protein 1 (Mammalian rdgB homolog beta) (M-rdgB beta) (MrdgBbeta) (Retinal degeneration B homolog beta) (RdgBbeta)	[Isoform 1]: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidic acid (PA) between membranes (PubMed:10531358, PubMed:22822086). Binds PA derived from the phospholipase D signaling pathway and among the cellular PA species, preferably binds to the C16:0/16:1 and C16:1/18:1 PA species (PubMed:22822086). {ECO:0000269\|PubMed:10531358, ECO:0000269\|PubMed:22822086}.; FUNCTION: [Isoform 2]: Catalyzes the transfer of phosphatidylinositol between membranes. {ECO:0000269\|PubMed:22822086}.
Q9UKV3	ACIN1	Y668	ochoa	Apoptotic chromatin condensation inducer in the nucleus (Acinus)	Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269\|PubMed:10490026, ECO:0000269\|PubMed:12665594, ECO:0000269\|PubMed:18559500, ECO:0000269\|PubMed:22203037, ECO:0000269\|PubMed:22388736}.
Q9ULD2	MTUS1	S544	ochoa	Microtubule-associated tumor suppressor 1 (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Mitochondrial tumor suppressor 1)	Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269\|PubMed:12692079, ECO:0000269\|PubMed:19794912}.
Q9ULG1	INO80	S1515	ochoa	Chromatin-remodeling ATPase INO80 (hINO80) (EC 3.6.4.-) (DNA helicase-related INO80 complex homolog 1) (DNA helicase-related protein INO80) (INO80 complex subunit A)	ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair (PubMed:16230350, PubMed:16298340, PubMed:17721549, PubMed:20237820, PubMed:20855601). Binds DNA (PubMed:16298340, PubMed:21303910). As part of the INO80 complex, remodels chromatin by shifting nucleosomes (PubMed:16230350, PubMed:21303910). Regulates transcription upon recruitment by YY1 to YY1-activated genes, where it acts as an essential coactivator (PubMed:17721549). Involved in UV-damage excision DNA repair (PubMed:20855601). The contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation (PubMed:20687897). Involved in DNA replication (PubMed:20237820). Required for microtubule assembly during mitosis thereby regulating chromosome segregation cycle (PubMed:20237820). {ECO:0000269\|PubMed:16230350, ECO:0000269\|PubMed:16298340, ECO:0000269\|PubMed:17721549, ECO:0000269\|PubMed:20237820, ECO:0000269\|PubMed:20687897, ECO:0000269\|PubMed:20855601, ECO:0000269\|PubMed:21303910}.
Q9ULH0	KIDINS220	S1426	ochoa	Kinase D-interacting substrate of 220 kDa (Ankyrin repeat-rich membrane-spanning protein)	Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269\|PubMed:18089783}.
Q9ULH1	ASAP1	S820	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879). {ECO:0000250, ECO:0000269\|PubMed:20393563, ECO:0000269\|PubMed:25673879}.
Q9ULH7	MRTFB	S550	ochoa	Myocardin-related transcription factor B (MRTF-B) (MKL/myocardin-like protein 2) (Megakaryoblastic leukemia 2)	Acts as a transcriptional coactivator of serum response factor (SRF). Required for skeletal myogenic differentiation. {ECO:0000269\|PubMed:14565952}.
Q9ULT8	HECTD1	S1533	ochoa	E3 ubiquitin-protein ligase HECTD1 (EC 2.3.2.26) (E3 ligase for inhibin receptor) (EULIR) (HECT domain-containing protein 1)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:33711283). Mediates 'Lys-63'-linked polyubiquitination of HSP90AA1 which leads to its intracellular localization and reduced secretion (By similarity). Negatively regulating HSP90AA1 secretion in cranial mesenchyme cells may impair their emigration and may be essential for the correct development of the cranial neural folds and neural tube closure (By similarity). Catalyzes ubiquitination and degradation of ZNF622, an assembly factor for the ribosomal 60S subunit, in hematopoietic cells, thereby promoting hematopoietic stem cell renewal (PubMed:33711283). {ECO:0000250\|UniProtKB:Q69ZR2, ECO:0000269\|PubMed:33711283}.
Q9UMZ2	SYNRG	S789	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UMZ2	SYNRG	S1013	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UN79	SOX13	S338	ochoa	Transcription factor SOX-13 (Islet cell antigen 12) (SRY (Sex determining region Y)-box 13) (Type 1 diabetes autoantigen ICA12)	Transcription factor that binds to DNA at the consensus sequence 5'-AACAAT-3' (PubMed:10871192). Binds to the proximal promoter region of the myelin protein MPZ gene, and may thereby be involved in the differentiation of oligodendroglia in the developing spinal tube (By similarity). Binds to the gene promoter of MBP and acts as a transcriptional repressor (By similarity). Binds to and modifies the activity of TCF7/TCF1, thereby inhibiting transcription and modulates normal gamma-delta T-cell development and differentiation of IL17A expressing gamma-delta T-cells (By similarity). Regulates expression of BLK in the differentiation of IL17A expressing gamma-delta T-cells (By similarity). Promotes brown adipocyte differentiation (By similarity). Inhibitor of WNT signaling (PubMed:20028982). {ECO:0000250\|UniProtKB:Q04891, ECO:0000269\|PubMed:10871192, ECO:0000269\|PubMed:20028982}.
Q9UPN9	TRIM33	S812	ochoa	E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RET-fused gene 7 protein) (Protein Rfg7) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33)	Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade). {ECO:0000250, ECO:0000269\|PubMed:10022127, ECO:0000269\|PubMed:15820681, ECO:0000269\|PubMed:16751102, ECO:0000269\|PubMed:19135894}.
Q9UPS6	SETD1B	S1770	ochoa	Histone-lysine N-methyltransferase SETD1B (EC 2.1.1.364) (Lysine N-methyltransferase 2G) (SET domain-containing protein 1B) (hSET1B)	Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:17355966, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17355966, PubMed:25561738). Plays an essential role in regulating the transcriptional programming of multipotent hematopoietic progenitor cells and lymphoid lineage specification during hematopoiesis (By similarity). {ECO:0000250\|UniProtKB:Q8CFT2, ECO:0000269\|PubMed:17355966, ECO:0000269\|PubMed:25561738}.
Q9UPU5	USP24	S1139	ochoa	Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)	Ubiquitin-specific protease that regulates cell survival in various contexts through modulating the protein stability of some of its substrates including DDB2, MCL1 or TP53. Plays a positive role on ferritinophagy where ferritin is degraded in lysosomes and releases free iron. {ECO:0000269\|PubMed:23159851, ECO:0000269\|PubMed:29695420}.
Q9UPZ3	HPS5	S440	ochoa	BLOC-2 complex member HPS5 (Alpha-integrin-binding protein 63) (Hermansky-Pudlak syndrome 5 protein) (Ruby-eye protein 2 homolog) (Ru2)	May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269\|PubMed:15296495, ECO:0000269\|PubMed:17301833}.
Q9Y250	LZTS1	S181	ochoa	Leucine zipper putative tumor suppressor 1 (F37/esophageal cancer-related gene-coding leucine-zipper motif) (Fez1)	Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor. {ECO:0000269\|PubMed:10097140, ECO:0000269\|PubMed:11464283, ECO:0000269\|PubMed:11504921}.
Q9Y263	PLAA	S485	ochoa	Phospholipase A-2-activating protein (PLA2P) (PLAP)	Plays a role in protein ubiquitination, sorting and degradation through its association with VCP (PubMed:27753622). Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (By similarity). May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (PubMed:27753622). Plays a role in cerebellar Purkinje cell development (By similarity). Positively regulates cytosolic and calcium-independent phospholipase A2 activities in a tumor necrosis factor alpha (TNF-alpha)- or lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2 biosynthesis (PubMed:18291623, PubMed:28007986). {ECO:0000250\|UniProtKB:P27612, ECO:0000269\|PubMed:18291623, ECO:0000269\|PubMed:27753622, ECO:0000269\|PubMed:28007986}.
Q9Y2H0	DLGAP4	S732	ochoa	Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)	May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Q9Y2H2	INPP5F	S914	ochoa	Phosphatidylinositide phosphatase SAC2 (EC 3.1.3.25) (Inositol polyphosphate 5-phosphatase F) (Sac domain-containing inositol phosphatase 2) (Sac domain-containing phosphoinositide 4-phosphatase 2) (hSAC2)	Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling (PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (PubMed:25869669). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus (PubMed:25476455). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (By similarity). May play a role as negative regulator of axon regeneration after central nervous system injuries (By similarity). {ECO:0000250\|UniProtKB:Q8CDA1, ECO:0000269\|PubMed:17322895, ECO:0000269\|PubMed:25476455, ECO:0000269\|PubMed:25869669}.
Q9Y2J4	AMOTL2	S183	ochoa	Angiomotin-like protein 2 (Leman coiled-coil protein) (LCCP)	Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Plays a role in coupling actin fibers to cell junctions in endothelial cells and is therefore required for correct endothelial cell morphology via facilitating transcellular transmission of mechanical force resulting in endothelial cell elongation (By similarity). Required for the anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane which facilitates organization of radial actin fiber structure and cellular response to contractile forces (PubMed:28842668). This contributes to maintenance of cell area, size, shape, epithelial sheet organization and trophectoderm cell properties that facilitate blastocyst zona hatching (PubMed:28842668). Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. Activates the Hippo signaling pathway in response to cell contact inhibition via interaction with and ubiquitination by Crumbs complex-bound WWP1 (PubMed:34404733). Ubiquitinated AMOTL2 then interacts with LATS2 which in turn phosphorylates YAP1, excluding it from the nucleus and localizing it to the cytoplasm and tight junctions, therefore ultimately repressing YAP1-driven transcription of target genes (PubMed:17293535, PubMed:21205866, PubMed:26598551). Acts to inhibit WWTR1/TAZ transcriptional coactivator activity via sequestering WWTR1/TAZ in the cytoplasm and at tight junctions (PubMed:23911299). Regulates the size and protein composition of the podosome cortex and core at myofibril neuromuscular junctions (PubMed:23525008). Selectively promotes FGF-induced MAPK activation through SRC (PubMed:17293535). May play a role in the polarity, proliferation and migration of endothelial cells. {ECO:0000250\|UniProtKB:Q8K371, ECO:0000269\|PubMed:17293535, ECO:0000269\|PubMed:21205866, ECO:0000269\|PubMed:21937427, ECO:0000269\|PubMed:22362771, ECO:0000269\|PubMed:23525008, ECO:0000269\|PubMed:23911299, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:28842668, ECO:0000269\|PubMed:34404733}.
Q9Y2K5	R3HDM2	S333	ochoa	R3H domain-containing protein 2	None
Q9Y2X7	GIT1	S417	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y3R5	DOP1B	S720	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y3R5	DOP1B	S721	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y5P4	CERT1	S380	ochoa	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y6R4	MAP3K4	T1271	ochoa	Mitogen-activated protein kinase kinase kinase 4 (EC 2.7.11.25) (MAP three kinase 1) (MAPK/ERK kinase kinase 4) (MEK kinase 4) (MEKK 4)	Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269\|PubMed:12052864, ECO:0000269\|PubMed:9305639}.
Q9NP61	ARFGAP3	S458	Sugiyama	ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3)	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269\|PubMed:11172815}.
P55795	HNRNPH2	S285	Sugiyama	Heterogeneous nuclear ribonucleoprotein H2 (hnRNP H2) (FTP-3) (Heterogeneous nuclear ribonucleoprotein H') (hnRNP H') [Cleaved into: Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed]	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).
O94768	STK17B	S351	Sugiyama	Serine/threonine-protein kinase 17B (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 2)	Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269\|PubMed:9786912}.
Q9BRS2	RIOK1	S507	Sugiyama	Serine/threonine-protein kinase RIO1 (EC 2.7.11.1) (EC 3.6.1.-) (RIO kinase 1)	Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor (PubMed:22072790). The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit (By similarity). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). The catalytic activity regulates its dynamic association with the 40S subunit (By similarity). In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation (PubMed:21081503). {ECO:0000250\|UniProtKB:G0S3J5, ECO:0000250\|UniProtKB:Q12196, ECO:0000269\|PubMed:21081503, ECO:0000269\|PubMed:22072790}.
P24046	GABRR1	S447	SIGNOR\|iPTMNet\|EPSD	Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABAAR subunit rho-1) (GABA(C) receptor)	Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain (PubMed:37659407). Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (PubMed:37659407). When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:37659407). Rho-1 subunits are primarily expressed in retina where rho-1-containing GABAARs may play a role in retinal neurotransmission (PubMed:1849271). Rho-1 GABAARs are also involved in neuronal tonic (extrasynaptic) and phasic (synaptic) transmission in the Purkinje neurons of the cerebellum (By similarity). Rho-1 GABAARs may also contribute to the regulation of glial development in the cerebellum by controlling extrasynaptic transmission (By similarity). {ECO:0000250\|UniProtKB:P56475, ECO:0000269\|PubMed:1849271, ECO:0000269\|PubMed:37659407}.
O75122	CLASP2	S1016	Sugiyama	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
Q9UQ80	PA2G4	S44	Sugiyama	Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1)	May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250\|UniProtKB:P50580, ECO:0000250\|UniProtKB:Q6AYD3, ECO:0000269\|PubMed:11268000, ECO:0000269\|PubMed:12682367, ECO:0000269\|PubMed:15064750, ECO:0000269\|PubMed:15583694, ECO:0000269\|PubMed:16832058}.
Q06187	BTK	S557	Sugiyama	Tyrosine-protein kinase BTK (EC 2.7.10.2) (Agammaglobulinemia tyrosine kinase) (ATK) (B-cell progenitor kinase) (BPK) (Bruton tyrosine kinase)	Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling (PubMed:19290921). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (PubMed:19290921). After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members (PubMed:11606584). PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK (PubMed:11606584). BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways (PubMed:16517732, PubMed:17932028). Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway (PubMed:16517732). The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense (PubMed:16517732). Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells (PubMed:16517732, PubMed:17932028). Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation (PubMed:16415872). BTK also plays a critical role in transcription regulation (PubMed:19290921). Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes (PubMed:19290921). BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B (PubMed:19290921). Acts as an activator of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (PubMed:34554188). Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR (PubMed:9012831). GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression (PubMed:9012831). ARID3A and NFAT are other transcriptional target of BTK (PubMed:16738337). BTK is required for the formation of functional ARID3A DNA-binding complexes (PubMed:16738337). There is however no evidence that BTK itself binds directly to DNA (PubMed:16738337). BTK has a dual role in the regulation of apoptosis (PubMed:9751072). Plays a role in STING1-mediated induction of type I interferon (IFN) response by phosphorylating DDX41 (PubMed:25704810). {ECO:0000269\|PubMed:11606584, ECO:0000269\|PubMed:16415872, ECO:0000269\|PubMed:16517732, ECO:0000269\|PubMed:16738337, ECO:0000269\|PubMed:17932028, ECO:0000269\|PubMed:25704810, ECO:0000269\|PubMed:34554188, ECO:0000269\|PubMed:9012831, ECO:0000303\|PubMed:19290921, ECO:0000303\|PubMed:9751072}.
Q6P0Q8	MAST2	S996	Sugiyama	Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1)	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.
Q8N568	DCLK2	S185	Sugiyama	Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin domain-containing protein 3B) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2)	Protein kinase with a significantly reduced C(a2+)/CAM affinity and dependence compared to other members of the CaMK family. May play a role in the down-regulation of CRE-dependent gene activation probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the resulting retention of TORC2 in the cytoplasm (By similarity). {ECO:0000250}.
A8CG34	POM121C	S277	ochoa	Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
F5H5P2	None	Y379	ochoa	2-oxoisovalerate dehydrogenase subunit alpha (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain)	Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction. {ECO:0000256\|ARBA:ARBA00037052, ECO:0000256\|RuleBase:RU365014}.
O14639	ABLIM1	Y461	ochoa	Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin)	May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269\|PubMed:9245787}.
O14641	DVL2	S597	psp	Segment polarity protein dishevelled homolog DVL-2 (Dishevelled-2) (DSH homolog 2)	Plays a role in the signal transduction pathways mediated by multiple Wnt genes (PubMed:24616100). Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. {ECO:0000250\|UniProtKB:Q60838, ECO:0000269\|PubMed:19252499, ECO:0000269\|PubMed:24616100}.
O14646	CHD1	S1387	ochoa	Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.-) (ATP-dependent helicase CHD1)	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250\|UniProtKB:P40201, ECO:0000269\|PubMed:18042460, ECO:0000269\|PubMed:28866611}.
O14920	IKBKB	S692	ochoa	Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697). {ECO:0000250\|UniProtKB:O88351, ECO:0000269\|PubMed:11297557, ECO:0000269\|PubMed:14673179, ECO:0000269\|PubMed:15084260, ECO:0000269\|PubMed:17213322, ECO:0000269\|PubMed:19716809, ECO:0000269\|PubMed:20410276, ECO:0000269\|PubMed:20434986, ECO:0000269\|PubMed:20797629, ECO:0000269\|PubMed:21138416, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:30337470, ECO:0000269\|PubMed:32209697, ECO:0000269\|PubMed:38621137, ECO:0000269\|PubMed:9346484}.
O15075	DCLK1	S355	ochoa	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
O43566	RGS14	S48	ochoa	Regulator of G-protein signaling 14 (RGS14)	Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. May be involved in visual memory processing capacity and hippocampal-based learning and memory. {ECO:0000269\|PubMed:15917656, ECO:0000269\|PubMed:17635935}.
O75122	CLASP2	Y1019	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75152	ZC3H11A	S497	ochoa	Zinc finger CCCH domain-containing protein 11A	Through its association with TREX complex components, may participate in the export and post-transcriptional coordination of selected mRNA transcripts, including those required to maintain the metabolic processes in embryonic cells (PubMed:22928037, PubMed:37356722). Binds RNA (PubMed:29610341, PubMed:37356722). {ECO:0000269\|PubMed:22928037, ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.; FUNCTION: (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA export (PubMed:29610341). May be required for proper polyadenylation of adenovirus type 5/HAdV-5 capsid mRNA (PubMed:37356722). {ECO:0000269\|PubMed:29610341, ECO:0000269\|PubMed:37356722}.
O75381	PEX14	S274	ochoa	Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14)	Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:24235149, PubMed:28765278, PubMed:9653144). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role for peroxisome movement through a direct interaction with tubulin (PubMed:21525035). {ECO:0000250\|UniProtKB:P53112, ECO:0000269\|PubMed:21525035, ECO:0000269\|PubMed:24235149, ECO:0000269\|PubMed:28765278, ECO:0000269\|PubMed:9653144}.
O94875	SORBS2	S304	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O95071	UBR5	S621	ochoa	E3 ubiquitin-protein ligase UBR5 (EC 2.3.2.26) (E3 ubiquitin-protein ligase, HECT domain-containing 1) (Hyperplastic discs protein homolog) (hHYD) (Progestin-induced protein)	E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm and nucleus (PubMed:29033132, PubMed:33208877, PubMed:37478846, PubMed:37478862). Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates (PubMed:29033132, PubMed:37409633). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (By similarity). Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His) (By similarity). Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4 (PubMed:29033132). Together with ITCH, catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP, leading to its degradation: UBR5 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by ITCH (PubMed:29378950). Catalytic component of a nuclear protein quality control pathway that mediates ubiquitination and degradation of unpaired transcription factors (i.e. transcription factors that are not assembled into functional multiprotein complexes): specifically recognizes and binds degrons that are not accessible when transcription regulators are associated with their coactivators (PubMed:37478846, PubMed:37478862). Ubiquitinates various unpaired transcription regulator (MYC, SUPT4H1, SUPT5H, CDC20 and MCRS1), as well as ligand-bound nuclear receptors (ESR1, NR1H3, NR3C1, PGR, RARA, RXRA AND VDR) that are not associated with their nuclear receptor coactivators (NCOAs) (PubMed:33208877, PubMed:37478846, PubMed:37478862). Involved in maturation and/or transcriptional regulation of mRNA by mediating polyubiquitination and activation of CDK9 (PubMed:21127351). Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response (PubMed:11714696). Ubiquitinates acetylated PCK1 (PubMed:21726808). Acts as a positive regulator of the canonical Wnt signaling pathway by mediating (1) ubiquitination and stabilization of CTNNB1, and (2) 'Lys-48'-linked ubiquitination and degradation of TLE3 (PubMed:21118991, PubMed:28689657). Promotes disassembly of the mitotic checkpoint complex (MCC) from the APC/C complex by catalyzing ubiquitination of BUB1B, BUB3 and CDC20 (PubMed:35217622). Plays an essential role in extraembryonic development (By similarity). Required for the maintenance of skeletal tissue homeostasis by acting as an inhibitor of hedgehog (HH) signaling (By similarity). {ECO:0000250\|UniProtKB:Q80TP3, ECO:0000269\|PubMed:11714696, ECO:0000269\|PubMed:21118991, ECO:0000269\|PubMed:21127351, ECO:0000269\|PubMed:21726808, ECO:0000269\|PubMed:22884692, ECO:0000269\|PubMed:28689657, ECO:0000269\|PubMed:29033132, ECO:0000269\|PubMed:29378950, ECO:0000269\|PubMed:33208877, ECO:0000269\|PubMed:35217622, ECO:0000269\|PubMed:37409633, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:37478862}.
P02545	LMNA	S429	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P08493	MGP	S28	psp	Matrix Gla protein (MGP) (Cell growth-inhibiting gene 36 protein)	Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation.
P08581	MET	Y1003	ochoa\|psp	Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (By similarity). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity). {ECO:0000250\|UniProtKB:P16056}.; FUNCTION: (Microbial infection) Acts as a receptor for Listeria monocytogenes internalin InlB, mediating entry of the pathogen into cells. {ECO:0000269\|PubMed:11081636, ECO:0000305\|PubMed:17662939, ECO:0000305\|PubMed:19900460}.
P10451	SPP1	S123	psp	Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin)	Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250\|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. {ECO:0000250\|UniProtKB:P10923}.
P11274	BCR	S377	ochoa	Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)	Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119). {ECO:0000250\|UniProtKB:Q6PAJ1, ECO:0000269\|PubMed:1657398, ECO:0000269\|PubMed:17116687, ECO:0000269\|PubMed:1903516, ECO:0000269\|PubMed:23940119, ECO:0000269\|PubMed:7479768}.
P12694	BCKDHA	Y345	ochoa	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha)	Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction. {ECO:0000269\|PubMed:10745006, ECO:0000269\|PubMed:7883996, ECO:0000269\|PubMed:9582350}.
P14859	POU2F1	S366	ochoa	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P14921	ETS1	S288	ochoa	Protein C-ets-1 (p54)	Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269\|PubMed:10698492, ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000303\|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269\|PubMed:19377509}.
P16220	CREB1	S100	psp	Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1)	Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation (PubMed:14536081). Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells (By similarity). Regulates the expression of apoptotic and inflammatory response factors in cardiomyocytes in response to ERFE-mediated activation of AKT signaling (By similarity). {ECO:0000250\|UniProtKB:P27925, ECO:0000250\|UniProtKB:Q01147, ECO:0000269\|PubMed:14536081}.
P17302	GJA1	S328	ochoa\|psp	Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein)	Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity). {ECO:0000250\|UniProtKB:P08050, ECO:0000250\|UniProtKB:P23242}.
P43243	MATR3	Y214	ochoa	Matrin-3	May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269\|PubMed:11525732, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:32245947}.
P51114	FXR1	S409	ochoa	RNA-binding protein FXR1 (FMR1 autosomal homolog 1) (hFXR1p)	mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis (PubMed:17382880, PubMed:20417602, PubMed:30067974, PubMed:34731628, PubMed:35989368, PubMed:36306353). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:17382880, PubMed:34731628). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity). Required to activate translation of stored mRNAs during late spermatogenesis: acts by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules that recruit translation initiation factor EIF4G3 to activate translation of stored mRNAs in late spermatids (By similarity). Promotes translation of MYC transcripts by recruiting the eIF4F complex to the translation start site (PubMed:34731628). Acts as a negative regulator of inflammation in response to IL19 by promoting destabilization of pro-inflammatory transcripts (PubMed:30067974). Also acts as an inhibitor of inflammation by binding to TNF mRNA, decreasing TNF protein production (By similarity). Acts as a negative regulator of AMPA receptor GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting its translation (By similarity). Regulates proliferation of adult neural stem cells by binding to CDKN1A mRNA and promoting its expression (By similarity). Acts as a regulator of sleep and synaptic homeostasis by regulating translation of transcripts in neurons (By similarity). Required for embryonic and postnatal development of muscle tissue by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules (PubMed:30770808). Involved in the nuclear pore complex localization to the nuclear envelope by preventing cytoplasmic aggregation of nucleoporins: acts by preventing ectopic phase separation of nucleoporins in the cytoplasm via a microtubule-dependent mechanism (PubMed:32706158). Plays a role in the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with PKP3 (PubMed:25225333). May also do the same for PKP2, PKP3 and DSP via its interaction with PKP1 (PubMed:25225333). Forms a cytoplasmic messenger ribonucleoprotein (mRNP) network by packaging long mRNAs, serving as a scaffold that recruits proteins and signaling molecules. This network facilitates signaling reactions by maintaining proximity between kinases and substrates, crucial for processes like actomyosin reorganization (PubMed:39106863). {ECO:0000250\|UniProtKB:Q61584, ECO:0000269\|PubMed:17382880, ECO:0000269\|PubMed:20417602, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:30067974, ECO:0000269\|PubMed:30770808, ECO:0000269\|PubMed:32706158, ECO:0000269\|PubMed:34731628, ECO:0000269\|PubMed:35989368, ECO:0000269\|PubMed:36306353, ECO:0000269\|PubMed:39106863}.
P56945	BCAR1	S440	ochoa	Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12432078, PubMed:12832404). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). {ECO:0000250\|UniProtKB:Q61140, ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:12832404, ECO:0000269\|PubMed:17038317}.
P61925	PKIA	S35	ochoa	cAMP-dependent protein kinase inhibitor alpha (PKI-alpha) (cAMP-dependent protein kinase inhibitor, muscle/brain isoform)	Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
P78559	MAP1A	S1160	ochoa	Microtubule-associated protein 1A (MAP-1A) (Proliferation-related protein p80) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]	Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.
Q07157	TJP1	S329	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q08174	PCDH1	Y1017	ochoa	Protocadherin-1 (Cadherin-like protein 1) (Protocadherin-42) (PC42)	May be involved in cell-cell interaction processes and in cell adhesion.
Q08357	SLC20A2	S259	ochoa	Sodium-dependent phosphate transporter 2 (Gibbon ape leukemia virus receptor 2) (GLVR-2) (Phosphate transporter 2) (PiT-2) (Pit2) (hPit2) (Solute carrier family 20 member 2)	Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:12205090, PubMed:15955065, PubMed:16790504, PubMed:17494632, PubMed:22327515, PubMed:28722801, PubMed:30704756). Plays a critical role in the determination of bone quality and strength by providing phosphate for bone mineralization (By similarity). Required to maintain normal cerebrospinal fluid phosphate levels (By similarity). Mediates phosphate-induced calcification of vascular smooth muscle cells (VCMCs) and can functionally compensate for loss of SLC20A1 in VCMCs (By similarity). {ECO:0000250\|UniProtKB:Q80UP8, ECO:0000269\|PubMed:12205090, ECO:0000269\|PubMed:15955065, ECO:0000269\|PubMed:16790504, ECO:0000269\|PubMed:17494632, ECO:0000269\|PubMed:22327515, ECO:0000269\|PubMed:28722801, ECO:0000269\|PubMed:30704756}.; FUNCTION: (Microbial infection) Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. {ECO:0000269\|PubMed:11435563, ECO:0000269\|PubMed:12205090, ECO:0000269\|PubMed:15955065, ECO:0000269\|PubMed:8302848}.
Q13136	PPFIA1	S1174	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13480	GAB1	Y259	ochoa\|psp	GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1)	Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway (PubMed:29408807). {ECO:0000269\|PubMed:29408807}.
Q14005	IL16	S1080	ochoa	Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]	Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: [Isoform 1]: May act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Q14157	UBAP2L	Y858	ochoa	Ubiquitin-associated protein 2-like (Protein NICE-4) (RNA polymerase II degradation factor UBAP2L)	Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled nucleotide excision repair (TC-NER) machinery fails to resolve DNA damage (PubMed:35633597). Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs) (By similarity). Is a regulator of stress granule assembly, required for their efficient formation (PubMed:29395067, PubMed:35977029). Required for proper brain development and neocortex lamination (By similarity). {ECO:0000250\|UniProtKB:Q80X50, ECO:0000269\|PubMed:29395067, ECO:0000269\|PubMed:35633597}.
Q14161	GIT2	S421	ochoa	ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. {ECO:0000269\|PubMed:10896954}.
Q14980	NUMA1	Y1836	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q16594	TAF9	S155	ochoa	Transcription initiation factor TFIID subunit 9 (RNA polymerase II TBP-associated factor subunit G) (STAF31/32) (Transcription initiation factor TFIID 31 kDa subunit) (TAFII-31) (TAFII31) (Transcription initiation factor TFIID 32 kDa subunit) (TAFII-32) (TAFII32)	The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF9 is also a component of the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex (PubMed:15899866). TAF9 and its paralog TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes (PubMed:15899866). Essential for cell viability (PubMed:15899866). May have a role in gene regulation associated with apoptosis (PubMed:15899866). {ECO:0000269\|PubMed:15899866, ECO:0000269\|PubMed:33795473}.
Q3KQU3	MAP7D1	S460	ochoa	MAP7 domain-containing protein 1 (Arginine/proline-rich coiled-coil domain-containing protein 1) (Proline/arginine-rich coiled-coil domain-containing protein 1)	Microtubule-stabilizing protein involved in the control of cell motility and neurite outgrowth. Facilitate microtubule stabilization through the maintenance of acetylated stable microtubules. {ECO:0000250\|UniProtKB:A2AJI0}.
Q53GG5	PDLIM3	S151	ochoa	PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein)	May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
Q5T200	ZC3H13	S341	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T200	ZC3H13	Y851	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T5X7	BEND3	S39	ochoa	BEN domain-containing protein 3	Transcriptional repressor which associates with the NoRC (nucleolar remodeling complex) complex and plays a key role in repressing rDNA transcription. The sumoylated form modulates the stability of the NoRC complex component BAZ2A/TIP5 by controlling its USP21-mediated deubiquitination (PubMed:21914818, PubMed:26100909). Binds to unmethylated major satellite DNA and is involved in the recruitment of the Polycomb repressive complex 2 (PRC2) to major satellites (By similarity). Stimulates the ERCC6L translocase and ATPase activities (PubMed:28977671). {ECO:0000250\|UniProtKB:Q6PAL0, ECO:0000269\|PubMed:21914818, ECO:0000269\|PubMed:26100909, ECO:0000269\|PubMed:28977671}.
Q5VZ18	SHE	S107	ochoa	SH2 domain-containing adapter protein E	None
Q6GQQ9	OTUD7B	S63	ochoa	OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Cezanne) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne)	Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses (PubMed:18178551). In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B (By similarity). Negatively regulates mucosal immunity against infections (By similarity). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B (PubMed:26903241). Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (By similarity). Mediates deubiquitination of EGFR (PubMed:22179831). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains (PubMed:11463333, PubMed:20622874, PubMed:23827681, PubMed:27732584). Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure (PubMed:27732584). Hydrolyzes both linear and branched forms of polyubiquitin (PubMed:12682062). Acts as a regulator of mTORC1 and mTORC2 assembly by mediating 'Lys-63'-linked deubiquitination of MLST8, thereby promoting assembly of the mTORC2 complex, while inibiting formation of the mTORC1 complex (PubMed:28489822). {ECO:0000250\|UniProtKB:B2RUR8, ECO:0000269\|PubMed:11463333, ECO:0000269\|PubMed:12682062, ECO:0000269\|PubMed:18178551, ECO:0000269\|PubMed:20622874, ECO:0000269\|PubMed:22179831, ECO:0000269\|PubMed:23827681, ECO:0000269\|PubMed:26903241, ECO:0000269\|PubMed:27732584, ECO:0000269\|PubMed:28489822}.
Q6NUJ5	PWWP2B	S456	ochoa	PWWP domain-containing protein 2B	Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260). Plays a role in facilitating transcriptional elongation through regulation of histone acetylation (By similarity). Negatively regulates brown adipocyte thermogenesis by interacting with and stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone deacetylation at the promoter leading to the repression of UCP1 expression (By similarity). {ECO:0000250\|UniProtKB:Q69Z61, ECO:0000269\|PubMed:30228260}.
Q6P1L5	FAM117B	S410	ochoa	Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein)	None
Q6PJE2	POMZP3	S35	ochoa	POM121 and ZP3 fusion protein (POM-ZP3)	None
Q71RC2	LARP4	S597	ochoa	La-related protein 4 (La ribonucleoprotein domain family member 4)	RNA binding protein that binds to the poly-A tract of mRNA molecules (PubMed:21098120). Associates with the 40S ribosomal subunit and with polysomes (PubMed:21098120). Plays a role in the regulation of mRNA translation (PubMed:21098120). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987, PubMed:27615744). {ECO:0000269\|PubMed:21098120, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:27615744}.
Q7Z6Z7	HUWE1	S3122	ochoa	E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) (ARF-binding protein 1) (ARF-BP1) (HECT, UBA and WWE domain-containing protein 1) (HECT-type E3 ubiquitin transferase HUWE1) (Homologous to E6AP carboxyl terminus homologous protein 9) (HectH9) (Large structure of UREB1) (LASU1) (Mcl-1 ubiquitin ligase E3) (Mule) (Upstream regulatory element-binding protein 1) (URE-B1) (URE-binding protein 1)	E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15567145, PubMed:15767685, PubMed:15989957, PubMed:17567951, PubMed:18488021, PubMed:19037095, PubMed:19713937, PubMed:20534529, PubMed:30217973). Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957). Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937). Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956). Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738). Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973). Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021). May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951). Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095). Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity). Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling (PubMed:35776542). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by mediating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: HUWE1 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by TRAF6 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Ubiquitinates PPARA in hepatocytes (By similarity). {ECO:0000250\|UniProtKB:P51593, ECO:0000250\|UniProtKB:Q7TMY8, ECO:0000269\|PubMed:15567145, ECO:0000269\|PubMed:15767685, ECO:0000269\|PubMed:15989956, ECO:0000269\|PubMed:15989957, ECO:0000269\|PubMed:17567951, ECO:0000269\|PubMed:18488021, ECO:0000269\|PubMed:19037095, ECO:0000269\|PubMed:19713937, ECO:0000269\|PubMed:20534529, ECO:0000269\|PubMed:26214738, ECO:0000269\|PubMed:27746020, ECO:0000269\|PubMed:30217973, ECO:0000269\|PubMed:35776542}.
Q86TC9	MYPN	Y260	ochoa	Myopalladin (145 kDa sarcomeric protein)	Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines. {ECO:0000269\|PubMed:11309420}.
Q8IVT2	MISP	S400	ochoa\|psp	Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein)	Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus. {ECO:0000269\|PubMed:23509069, ECO:0000269\|PubMed:23574715}.
Q8N5C8	TAB3	Y512	ochoa	TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 3) (NF-kappa-B-activating protein 1) (TAK1-binding protein 3) (TAB-3) (TGF-beta-activated kinase 1-binding protein 3)	Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF) (PubMed:14633987, PubMed:14766965, PubMed:15327770, PubMed:22158122). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains (PubMed:14633987, PubMed:14766965, PubMed:15327770, PubMed:22158122, PubMed:36593296). The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1 and RIPK2: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (PubMed:15327770, PubMed:18079694, PubMed:22158122). {ECO:0000269\|PubMed:14633987, ECO:0000269\|PubMed:14766965, ECO:0000269\|PubMed:15327770, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:22158122, ECO:0000269\|PubMed:36593296}.; FUNCTION: [Isoform 2]: May be an oncogenic factor. {ECO:0000269\|PubMed:14766965}.
Q8NEG4	FAM83F	Y107	ochoa	Protein FAM83F	None
Q8TB45	DEPTOR	Y289	ochoa\|psp	DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6)	Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269\|PubMed:19446321, ECO:0000269\|PubMed:22017875, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:22017877, ECO:0000269\|PubMed:25936805, ECO:0000269\|PubMed:29382726, ECO:0000269\|PubMed:34519268, ECO:0000269\|PubMed:34519269}.
Q8TDJ6	DMXL2	S1143	ochoa	DmX-like protein 2 (Rabconnectin-3)	May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763). Plays a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity). {ECO:0000250\|UniProtKB:Q8BPN8, ECO:0000269\|PubMed:11809763}.
Q8WZ73	RFFL	S232	ochoa	E3 ubiquitin-protein ligase rififylin (EC 2.3.2.27) (Caspase regulator CARP2) (Caspases-8 and -10-associated RING finger protein 2) (CARP-2) (FYVE-RING finger protein Sakura) (Fring) (RING finger and FYVE-like domain-containing protein 1) (RING finger protein 189) (RING finger protein 34-like) (RING-type E3 ubiquitin transferase rififylin)	E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269\|PubMed:15069192, ECO:0000269\|PubMed:17121812, ECO:0000269\|PubMed:18382127, ECO:0000269\|PubMed:18450452, ECO:0000269\|PubMed:22609986}.
Q96BY6	DOCK10	S1295	ochoa	Dedicator of cytokinesis protein 10 (Zizimin-3)	Guanine nucleotide-exchange factor (GEF) that activates CDC42 and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic spine morphogenesis in Purkinje cells and in hippocampal neurons, via a CDC42-mediated pathway. Sustains B-cell lymphopoiesis in secondary lymphoid tissues and regulates FCER2/CD23 expression. {ECO:0000250\|UniProtKB:Q8BZN6}.
Q96E39	RBMXL1	Y335	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96HA1	POM121	S300	ochoa	Nuclear envelope pore membrane protein POM 121 (Nuclear envelope pore membrane protein POM 121A) (Nucleoporin Nup121) (Pore membrane protein of 121 kDa)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
Q99704	DOK1	Y449	ochoa\|psp	Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok)) (pp62)	DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269\|PubMed:18156175}.
Q9BXK1	KLF16	S111	ochoa	Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Novel Sp1-like zinc finger transcription factor 2) (Transcription factor BTEB4) (Transcription factor NSLP2)	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.
Q9BXW9	FANCD2	S1407	ochoa\|psp	Fanconi anemia group D2 protein (Protein FACD2)	Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250\|UniProtKB:Q68Y81, ECO:0000269\|PubMed:11239453, ECO:0000269\|PubMed:11239454, ECO:0000269\|PubMed:12086603, ECO:0000269\|PubMed:12239151, ECO:0000269\|PubMed:14517836, ECO:0000269\|PubMed:15115758, ECO:0000269\|PubMed:15314022, ECO:0000269\|PubMed:15377654, ECO:0000269\|PubMed:15454491, ECO:0000269\|PubMed:15650050, ECO:0000269\|PubMed:15661754, ECO:0000269\|PubMed:15671039, ECO:0000269\|PubMed:19465921, ECO:0000269\|PubMed:30335751, ECO:0000269\|PubMed:36385258}.
Q9BYW2	SETD2	S1891	ochoa	Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.359) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)	Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (PubMed:19332550). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (PubMed:23622243). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (PubMed:24843002). Acts as a tumor suppressor (PubMed:24509477). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (PubMed:27317772). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (PubMed:21792193). Required during angiogenesis (By similarity). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (By similarity). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565, PubMed:28753426). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (PubMed:28753426). {ECO:0000250\|UniProtKB:E9Q5F9, ECO:0000269\|PubMed:16118227, ECO:0000269\|PubMed:19141475, ECO:0000269\|PubMed:21526191, ECO:0000269\|PubMed:21792193, ECO:0000269\|PubMed:23043551, ECO:0000269\|PubMed:23325844, ECO:0000269\|PubMed:23622243, ECO:0000269\|PubMed:24509477, ECO:0000269\|PubMed:24843002, ECO:0000269\|PubMed:27317772, ECO:0000269\|PubMed:27474439, ECO:0000269\|PubMed:27518565, ECO:0000269\|PubMed:28753426}.; FUNCTION: (Microbial infection) Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. {ECO:0000269\|PubMed:11461154}.
Q9C0C2	TNKS1BP1	S1054	ochoa	182 kDa tankyrase-1-binding protein	None
Q9H0D6	XRN2	S485	ochoa	5'-3' exoribonuclease 2 (EC 3.1.13.-) (DHM1-like protein) (DHP protein)	Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (PubMed:21700224). {ECO:0000250, ECO:0000269\|PubMed:15565158, ECO:0000269\|PubMed:16648491, ECO:0000269\|PubMed:21700224}.
Q9H4L5	OSBPL3	S326	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H9C1	VIPAS39	S96	ochoa	Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction)	Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity). {ECO:0000250\|UniProtKB:Q23288, ECO:0000269\|PubMed:19109425, ECO:0000269\|PubMed:20190753}.
Q9P1Y5	CAMSAP3	S382	ochoa	Calmodulin-regulated spectrin-associated protein 3 (Protein Nezha)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742, PubMed:27802168). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). {ECO:0000250\|UniProtKB:Q80VC9, ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:26715742, ECO:0000269\|PubMed:27693509, ECO:0000269\|PubMed:27802168, ECO:0000269\|PubMed:28089391, ECO:0000269\|PubMed:28386021}.
Q9UHB6	LIMA1	S371	ochoa	LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)	Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250\|UniProtKB:Q9ERG0, ECO:0000269\|PubMed:12566430, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:33999101}.
Q9Y3M8	STARD13	S336	ochoa	StAR-related lipid transfer protein 13 (46H23.2) (Deleted in liver cancer 2 protein) (DLC-2) (Rho GTPase-activating protein) (START domain-containing protein 13) (StARD13)	GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells. {ECO:0000269\|PubMed:14697242, ECO:0000269\|PubMed:16217026}.
Q9Y4H2	IRS2	Y675	ochoa\|psp	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
A6ND36	FAM83G	Y619	Sugiyama	Protein FAM83G (Protein associated with SMAD1)	Substrate for type I BMP receptor kinase involved in regulation of some target genes of the BMP signaling pathway. Also regulates the expression of several non-BMP target genes, suggesting a role in other signaling pathways. {ECO:0000269\|PubMed:24554596}.
A0FGR8	ESYT2	S691	ochoa	Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)	Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:27044890). {ECO:0000269\|PubMed:17360437, ECO:0000269\|PubMed:20833364, ECO:0000269\|PubMed:23791178, ECO:0000269\|PubMed:24847877, ECO:0000269\|PubMed:27044890}.
O15403	SLC16A6	S240	ochoa	Monocarboxylate transporter 7 (MCT 7) (Monocarboxylate transporter 6) (MCT 6) (Solute carrier family 16 member 6)	Monocarboxylate transporter selective for taurine. May associate with BSG/CD147 or EMB/GP70 ancillary proteins to mediate facilitative efflux or influx of taurine across the plasma membrane. The transport is pH- and sodium-independent. Rather low-affinity, is likely effective for taurine transport in tissues where taurine is present at high concentrations. {ECO:0000250\|UniProtKB:Q7TMR7}.
O75334	PPFIA2	S263	ochoa	Liprin-alpha-2 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2) (PTPRF-interacting protein alpha-2)	Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. In neuronal cells, is a scaffolding protein in the dendritic spines which acts as immobile postsynaptic post able to recruit KIF1A-driven dense core vesicles to dendritic spines (PubMed:30021165). {ECO:0000269\|PubMed:30021165, ECO:0000269\|PubMed:9624153}.
O75674	TOM1L1	S314	ochoa	TOM1-like protein 1 (Src-activating and signaling molecule protein) (Target of Myb-like protein 1)	Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.
O75970	MPDZ	S1827	ochoa	Multiple PDZ domain protein (Multi-PDZ domain protein 1)	Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250\|UniProtKB:O55164, ECO:0000269\|PubMed:11150294, ECO:0000269\|PubMed:15312654}.
O94763	URI1	S378	ochoa	Unconventional prefoldin RPB5 interactor 1 (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein)	Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination.
O94989	ARHGEF15	S93	ochoa	Rho guanine nucleotide exchange factor 15 (Ephexin-5) (E5) (Vsm-RhoGEF)	Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. {ECO:0000269\|PubMed:12775584}.
O95696	BRD1	S505	ochoa	Bromodomain-containing protein 1 (BR140-like protein) (Bromodomain and PHD finger-containing protein 2)	Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a regulator of hematopoiesis (PubMed:16387653, PubMed:21753189, PubMed:21880731). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby promoting erythroid differentiation (PubMed:21753189). {ECO:0000269\|PubMed:16387653, ECO:0000269\|PubMed:21753189, ECO:0000269\|PubMed:21880731}.
P55317	FOXA1	S307	ochoa	Hepatocyte nuclear factor 3-alpha (HNF-3-alpha) (HNF-3A) (Forkhead box protein A1) (Transcription factor 3A) (TCF-3A)	Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promoter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis. {ECO:0000250, ECO:0000269\|PubMed:16087863, ECO:0000269\|PubMed:16331276, ECO:0000269\|PubMed:18358809, ECO:0000269\|PubMed:19127412, ECO:0000269\|PubMed:19917725}.
Q05519	SRSF11	S215	ochoa	Serine/arginine-rich splicing factor 11 (Arginine-rich 54 kDa nuclear protein) (p54) (Splicing factor, arginine/serine-rich 11)	May function in pre-mRNA splicing.
Q13905	RAPGEF1	Y341	ochoa	Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G)	Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1 (PubMed:12432078). Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:7806500}.
Q96GA3	LTV1	S358	ochoa	Protein LTV1 homolog	Essential for ribosome biogenesis. {ECO:0000250\|UniProtKB:Q5U3J8}.
Q96HB5	CCDC120	S286	ochoa	Coiled-coil domain-containing protein 120	Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth. {ECO:0000269\|PubMed:25326380}.
Q9H4L7	SMARCAD1	S245	ochoa	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1) (EC 3.6.4.12) (ATP-dependent helicase 1) (hHEL1)	DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing. {ECO:0000269\|PubMed:21549307, ECO:0000269\|PubMed:22960744}.
Q9UKV3	ACIN1	S990	ochoa	Apoptotic chromatin condensation inducer in the nucleus (Acinus)	Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269\|PubMed:10490026, ECO:0000269\|PubMed:12665594, ECO:0000269\|PubMed:18559500, ECO:0000269\|PubMed:22203037, ECO:0000269\|PubMed:22388736}.
Q9UPN4	CEP131	S453	ochoa	Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Pre-acrosome localization protein 1)	Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation (PubMed:17954613, PubMed:24185901). In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation (PubMed:24121310). In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner (PubMed:24121310, PubMed:26616734). Also acts as a negative regulator of BBSome ciliary trafficking (PubMed:24550735). Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells (PubMed:22797915, PubMed:26297806). Involved in centriole duplication (By similarity). Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). Essential for maintaining proper centriolar satellite integrity (PubMed:30804208). {ECO:0000250\|UniProtKB:Q62036, ECO:0000269\|PubMed:17954613, ECO:0000269\|PubMed:22797915, ECO:0000269\|PubMed:24121310, ECO:0000269\|PubMed:24185901, ECO:0000269\|PubMed:24550735, ECO:0000269\|PubMed:26297806, ECO:0000269\|PubMed:26616734, ECO:0000269\|PubMed:30804208}.
A0A0C4DFX4	None	S255	ochoa	Snf2 related CREBBP activator protein	None
O00418	EEF2K	S78	ochoa\|psp	Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269\|PubMed:14709557, ECO:0000269\|PubMed:9144159}.
O00418	EEF2K	Y468	ochoa	Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269\|PubMed:14709557, ECO:0000269\|PubMed:9144159}.
O00472	ELL2	S420	ochoa	RNA polymerase II elongation factor ELL2	Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:22195968, ECO:0000269\|PubMed:23251033}.
O00571	DDX3X	S82	ochoa\|psp	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O14646	CHD1	S1677	ochoa	Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.-) (ATP-dependent helicase CHD1)	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250\|UniProtKB:P40201, ECO:0000269\|PubMed:18042460, ECO:0000269\|PubMed:28866611}.
O14874	BCKDK	T37	ochoa	Branched-chain alpha-ketoacid dehydrogenase kinase (BCKDH kinase) (BCKDHKIN) (BDK) (EC 2.7.11.1) ([3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial) (EC 2.7.11.4)	Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:24449431, PubMed:29779826, PubMed:37558654). Phosphorylates and inactivates mitochondrial BCKDH complex a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Associates with the E2 component of BCKDH complex and phosphorylates BCKDHA on Ser-337, leading to conformational changes that interrupt substrate channeling between E1 and E2 and inactivates the BCKDH complex (PubMed:29779826, PubMed:37558654). Phosphorylates ACLY on Ser-455 in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and glucogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxxE/D canonical motif (PubMed:29779826). {ECO:0000269\|PubMed:24449431, ECO:0000269\|PubMed:29779826, ECO:0000269\|PubMed:37558654}.
O15013	ARHGEF10	S1295	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15040	TECPR2	T416	ochoa	Tectonin beta-propeller repeat-containing protein 2 (WD repeat-containing protein KIAA0329/KIAA0297)	Probably plays a role as positive regulator of autophagy. {ECO:0000269\|PubMed:23176824}.
O15211	RGL2	S584	ochoa	Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) (RalGDS-like factor) (Ras-associated protein RAB2L)	Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity). {ECO:0000250}.
O15344	MID1	S96	ochoa\|psp	E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (Putative transcription factor XPRF) (RING finger protein 59) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)	Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269\|PubMed:10400985, ECO:0000269\|PubMed:11685209, ECO:0000269\|PubMed:22613722}.
O43194	GPR39	S427	ochoa	G-protein coupled receptor 39	Zinc-sensing receptor that can sense changes in extracellular Zn(2+), mediate Zn(2+) signal transmission, and participates in the regulation of numerous physiological processes including glucose homeostasis regulation, gastrointestinal mobility, hormone secretion and cell death (PubMed:18180304). Activation by Zn(2+) in keratinocytes increases the intracellular concentration of Ca(2+) and activates the ERK/MAPK and PI3K/AKT signaling pathways leading to epithelial repair (PubMed:20522546). Plays an essential role in normal wound healing by inducing the production of cytokines including the major inflammatory cytokine IL6 via the PKC/MAPK/CEBPB pathway (By similarity). Regulates adipose tissue metabolism, especially lipolysis, and regulates the function of lipases, such as hormone-sensitive lipase and adipose triglyceride lipase (By similarity). Plays a role in the inhibition of cell death and protects against oxidative, endoplasmic reticulum and mitochondrial stress by inducing secretion of the cytoprotective pigment epithelium-derived growth factor (PEDF) and probably other protective transcripts in a GNA13/RHOA/SRE-dependent manner (PubMed:18180304). Forms dynamic heteroreceptor complexes with HTR1A and GALR1 depending on cell type or specific physiological states, resulting in signaling diversity: HTR1A-GPR39 shows additive increase in signaling along the serum response element (SRE) and NF-kappa-B pathways while GALR1 acts as an antagonist blocking SRE (PubMed:26365466). {ECO:0000250\|UniProtKB:Q5U431, ECO:0000269\|PubMed:18180304, ECO:0000269\|PubMed:20522546, ECO:0000269\|PubMed:26365466}.
O43353	RIPK2	S361	ochoa	Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)	Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269\|PubMed:14638696, ECO:0000269\|PubMed:17054981, ECO:0000269\|PubMed:17562858, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:21123652, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:22607974, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:28545134, ECO:0000269\|PubMed:28656966, ECO:0000269\|PubMed:29452636, ECO:0000269\|PubMed:30026309, ECO:0000269\|PubMed:30279485, ECO:0000269\|PubMed:30478312, ECO:0000269\|PubMed:9575181, ECO:0000269\|PubMed:9642260}.
O43602	DCX	S310	ochoa	Neuronal migration protein doublecortin (Doublin) (Lissencephalin-X) (Lis-X)	Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration. {ECO:0000269\|PubMed:22359282}.
O43896	KIF1C	S680	ochoa	Kinesin-like protein KIF1C	Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. {ECO:0000269\|PubMed:9685376}.
O60293	ZFC3H1	S655	ochoa	Zinc finger C3H1 domain-containing protein (Coiled-coil domain-containing protein 131) (Proline/serine-rich coiled-coil protein 2)	Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. {ECO:0000269\|PubMed:27871484}.
O60315	ZEB2	S364	ochoa	Zinc finger E-box-binding homeobox 2 (Smad-interacting protein 1) (SMADIP1) (Zinc finger homeobox protein 1b)	Transcriptional inhibitor that binds to DNA sequence 5'-CACCT-3' in different promoters (PubMed:16061479, PubMed:20516212). Represses transcription of E-cadherin (PubMed:16061479). Represses expression of MEOX2 (PubMed:20516212). {ECO:0000269\|PubMed:16061479, ECO:0000269\|PubMed:20516212}.
O60508	CDC40	S26	ochoa	Pre-mRNA-processing factor 17 (Cell division cycle 40 homolog) (EH-binding protein 3) (Ehb3) (PRP17 homolog) (hPRP17)	Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:33220177). Plays an important role in embryonic brain development; this function does not require proline isomerization (PubMed:33220177). {ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:33220177, ECO:0000269\|PubMed:9830021}.
O60885	BRD4	S498	psp	Bromodomain-containing protein 4 (Protein HUNK1)	Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250\|UniProtKB:Q9ESU6, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:19103749, ECO:0000269\|PubMed:19596240, ECO:0000269\|PubMed:22334664, ECO:0000269\|PubMed:22509028, ECO:0000269\|PubMed:23086925, ECO:0000269\|PubMed:23317504, ECO:0000269\|PubMed:23589332, ECO:0000269\|PubMed:24360279, ECO:0000269\|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269\|PubMed:23728299}.
O75427	LRCH4	S517	ochoa	Leucine-rich repeat and calponin homology domain-containing protein 4 (Leucine-rich repeat neuronal protein 4) (Leucine-rich neuronal protein)	Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250\|UniProtKB:Q921G6}.
O94915	FRYL	S1945	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94988	FAM13A	Y656	ochoa	Protein FAM13A	None
O95544	NADK	S50	ochoa	NAD kinase (EC 2.7.1.23) (Poly(P)/ATP NAD kinase)	None
O95644	NFATC1	S245	ochoa\|psp	Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc)	Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (PubMed:10358178). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (By similarity). {ECO:0000250\|UniProtKB:O88942, ECO:0000269\|PubMed:10358178}.
O95810	CAVIN2	S370	ochoa	Caveolae-associated protein 2 (Cavin-2) (PS-p68) (Phosphatidylserine-binding protein) (Serum deprivation-response protein)	Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity). {ECO:0000250\|UniProtKB:Q66H98, ECO:0000269\|PubMed:19525939}.
P02671	FGA	T555	ochoa	Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]	Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250\|UniProtKB:E9PV24}.
P04049	RAF1	S291	ochoa\|psp	RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269\|PubMed:11427728, ECO:0000269\|PubMed:11719507, ECO:0000269\|PubMed:15385642, ECO:0000269\|PubMed:15618521, ECO:0000269\|PubMed:15849194, ECO:0000269\|PubMed:16892053, ECO:0000269\|PubMed:16924233, ECO:0000269\|PubMed:9360956}.
P06748	NPM1	S143	ochoa	Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)	Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250\|UniProtKB:Q61937, ECO:0000269\|PubMed:12882984, ECO:0000269\|PubMed:16107701, ECO:0000269\|PubMed:17015463, ECO:0000269\|PubMed:18809582, ECO:0000269\|PubMed:19188445, ECO:0000269\|PubMed:20352051, ECO:0000269\|PubMed:21084279, ECO:0000269\|PubMed:22002061, ECO:0000269\|PubMed:22528486, ECO:0000269\|PubMed:25956029}.
P07910	HNRNPC	S119	ochoa	Heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2)	Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). {ECO:0000269\|PubMed:12509468, ECO:0000269\|PubMed:16010978, ECO:0000269\|PubMed:25719671, ECO:0000269\|PubMed:7567451, ECO:0000269\|PubMed:8264621}.
P08670	VIM	Y53	ochoa	Vimentin	Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250\|UniProtKB:A0A8C0N8E3, ECO:0000250\|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269\|PubMed:21746880}.
P08670	VIM	S55	ochoa\|psp	Vimentin	Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250\|UniProtKB:A0A8C0N8E3, ECO:0000250\|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269\|PubMed:21746880}.
P11831	SRF	S83	psp	Serum response factor (SRF)	SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation. {ECO:0000250\|UniProtKB:Q9JM73}.
P13807	GYS1	S653	ochoa\|psp	Glycogen [starch] synthase, muscle (EC 2.4.1.11) (Glycogen synthase 1)	Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. {ECO:0000269\|PubMed:35835870}.
P14859	POU2F1	S147	psp	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P15822	HIVEP1	S1147	ochoa	Zinc finger protein 40 (Cirhin interaction protein) (CIRIP) (Gate keeper of apoptosis-activating protein) (GAAP) (Human immunodeficiency virus type I enhancer-binding protein 1) (HIV-EP1) (Major histocompatibility complex-binding protein 1) (MBP-1) (Positive regulatory domain II-binding factor 1) (PRDII-BF1)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.
P15924	DSP	S2833	ochoa\|psp	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2837	psp	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2849	ochoa\|psp	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P17676	CEBPB	S227	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P25101	EDNRA	S397	psp	Endothelin-1 receptor (Endothelin receptor type A) (ET-A) (ETA-R) (hET-AR)	Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.
P35568	IRS1	S274	ochoa	Insulin receptor substrate 1 (IRS-1)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:7541045, PubMed:33991522, PubMed:38625937). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:19639489). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:11171109, PubMed:8265614). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:11171109, ECO:0000269\|PubMed:16878150, ECO:0000269\|PubMed:19639489, ECO:0000269\|PubMed:38625937, ECO:0000269\|PubMed:7541045, ECO:0000269\|PubMed:8265614}.
P38159	RBMX	Y255	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P42166	TMPO	T172	ochoa	Lamina-associated polypeptide 2, isoform alpha (Thymopoietin isoform alpha) (TP alpha) (Thymopoietin-related peptide isoform alpha) (TPRP isoform alpha) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)]	May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
P42331	ARHGAP25	S407	ochoa	Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.
P42858	HTT	S463	psp	Huntingtin (Huntington disease protein) (HD protein) [Cleaved into: Huntingtin, myristoylated N-terminal fragment]	[Huntingtin]: May play a role in microtubule-mediated transport or vesicle function.; FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the formation of autophagic vesicles. {ECO:0000269\|PubMed:24459296}.
P46100	ATRX	S54	ochoa	Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked helicase II) (X-linked nuclear protein) (XNP) (Znf-HX)	Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as a negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610). {ECO:0000269\|PubMed:12953102, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:21029860, ECO:0000269\|PubMed:22391447, ECO:0000269\|PubMed:22829774, ECO:0000269\|PubMed:24500201, ECO:0000269\|PubMed:27029610}.
P46100	ATRX	S1996	ochoa	Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked helicase II) (X-linked nuclear protein) (XNP) (Znf-HX)	Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as a negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610). {ECO:0000269\|PubMed:12953102, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:21029860, ECO:0000269\|PubMed:22391447, ECO:0000269\|PubMed:22829774, ECO:0000269\|PubMed:24500201, ECO:0000269\|PubMed:27029610}.
P46108	CRK	S125	ochoa	Adapter molecule crk (Proto-oncogene c-Crk) (p38)	Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1. {ECO:0000269\|PubMed:12432078}.; FUNCTION: [Isoform Crk-II]: Regulates cell adhesion, spreading and migration (PubMed:31311869). Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4 (PubMed:19004829). May regulate the EFNA5-EPHA3 signaling (By similarity). {ECO:0000250\|UniProtKB:Q64010, ECO:0000269\|PubMed:11870224, ECO:0000269\|PubMed:1630456, ECO:0000269\|PubMed:17515907, ECO:0000269\|PubMed:19004829, ECO:0000269\|PubMed:31311869}.
P46821	MAP1B	Y1921	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	Y1923	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P49757	NUMB	S244	ochoa	Protein numb homolog (h-Numb) (Protein S171)	Regulates clathrin-mediated receptor endocytosis (PubMed:18657069). Plays a role in the process of neurogenesis (By similarity). Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate (By similarity). Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity (By similarity). May also mediate local repair of brain ventricular wall damage (By similarity). {ECO:0000250\|UniProtKB:Q9QZS3, ECO:0000269\|PubMed:18657069}.
P50402	EMD	S66	ochoa	Emerin	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:32923640}.
P53671	LIMK2	S293	ochoa\|psp	LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics (PubMed:10436159, PubMed:11018042). Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11018042). Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP (PubMed:22328514). Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro (PubMed:8537403). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). {ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:11018042, ECO:0000269\|PubMed:22328514, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:8537403}.
P54646	PRKAA2	S515	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (PubMed:7959015). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation (By similarity). Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity). Upon glucose starvation, promotes ARF6 activation in a kinase-independent manner leading to cell migration (PubMed:36017701). Upon glucose deprivation mediates the phosphorylation of ACSS2 at 'Ser-659', which exposes the nuclear localization signal of ACSS2, required for its interaction with KPNA1 and nuclear translocation (PubMed:28552616). Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:Q09137, ECO:0000250\|UniProtKB:Q8BRK8, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:25687571, ECO:0000269\|PubMed:28552616, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36017701, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:7959015, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
P62995	TRA2B	S20	ochoa	Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B)	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:9546399}.
P80723	BASP1	S176	ochoa	Brain acid soluble protein 1 (22 kDa neuronal tissue-enriched acidic protein) (Neuronal axonal membrane protein NAP-22)	None
Q00987	MDM2	S246	psp	E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Hdm2) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)	E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903). {ECO:0000250\|UniProtKB:P23804, ECO:0000269\|PubMed:12821780, ECO:0000269\|PubMed:15053880, ECO:0000269\|PubMed:15195100, ECO:0000269\|PubMed:15632057, ECO:0000269\|PubMed:16337594, ECO:0000269\|PubMed:17290220, ECO:0000269\|PubMed:19098711, ECO:0000269\|PubMed:19219073, ECO:0000269\|PubMed:19837670, ECO:0000269\|PubMed:19965871, ECO:0000269\|PubMed:20173098, ECO:0000269\|PubMed:20385133, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:22128911, ECO:0000269\|PubMed:29681526, ECO:0000269\|PubMed:30879903}.
Q01484	ANK2	S2661	ochoa	Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) (Non-erythroid ankyrin)	Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:12571597). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity). {ECO:0000250\|UniProtKB:Q8C8R3, ECO:0000269\|PubMed:12571597}.
Q02952	AKAP12	S392	ochoa	A-kinase anchor protein 12 (AKAP-12) (A-kinase anchor protein 250 kDa) (AKAP 250) (Gravin) (Myasthenia gravis autoantigen)	Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Q03111	MLLT1	S444	ochoa	Protein ENL (YEATS domain-containing protein 1)	Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948). Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated (PubMed:27105114). Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20) (PubMed:27105114). {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:27105114}.; FUNCTION: Acts as a key chromatin reader in acute myeloid leukemia by recognizing and binding to acetylated histones via its YEATS domain, thereby regulating oncogenic gene transcription. {ECO:0000269\|PubMed:28241139, ECO:0000269\|PubMed:28241141}.
Q04727	TLE4	S210	ochoa	Transducin-like enhancer protein 4 (Grg-4) (Groucho-related protein 4)	Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Essential for the transcriptional repressor activity of SIX3 during retina and lens development and for SIX3 transcriptional auto-repression (By similarity). Involved in transcriptional repression of GNRHR and enhances MSX1-mediated transcriptional repression of CGA/alpha-GSU (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:Q62441}.
Q08AD1	CAMSAP2	S1325	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q12959	DLG1	Y108	ochoa	Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97) (hDlg)	Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). May also play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. During long-term depression in hippocampal neurons, it recruits ADAM10 to the plasma membrane (PubMed:23676497). {ECO:0000250\|UniProtKB:A0A8C0TYJ0, ECO:0000250\|UniProtKB:Q811D0, ECO:0000269\|PubMed:10656683, ECO:0000269\|PubMed:12445884, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15263016, ECO:0000269\|PubMed:19213956, ECO:0000269\|PubMed:20605917, ECO:0000269\|PubMed:23676497}.
Q13136	PPFIA1	S238	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13242	SRSF9	S199	ochoa	Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:10196175, ECO:0000269\|PubMed:11875052, ECO:0000269\|PubMed:12024014, ECO:0000269\|PubMed:12604611, ECO:0000269\|PubMed:15009090, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:15695522, ECO:0000269\|PubMed:7556075}.
Q13425	SNTB2	S228	ochoa	Beta-2-syntrophin (59 kDa dystrophin-associated protein A1 basic component 2) (Syntrophin-3) (SNT3) (Syntrophin-like) (SNTL)	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.
Q13501	SQSTM1	S288	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13796	SHROOM2	T925	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13835	PKP1	S69	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q14161	GIT2	S574	ochoa	ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. {ECO:0000269\|PubMed:10896954}.
Q14162	SCARF1	S753	ochoa	Scavenger receptor class F member 1 (Acetyl LDL receptor) (Scavenger receptor expressed by endothelial cells 1) (SREC-I)	Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). {ECO:0000250}.
Q14980	NUMA1	S1187	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q15283	RASA2	S559	ochoa	Ras GTPase-activating protein 2 (GTPase-activating protein 1m) (GAP1m)	Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).
Q15555	MAPRE2	S234	ochoa	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15642	TRIP10	T302	ochoa	Cdc42-interacting protein 4 (Protein Felic) (Salt tolerant protein) (hSTP) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10)	Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269\|PubMed:11069762, ECO:0000269\|PubMed:16318909, ECO:0000269\|PubMed:16326391}.
Q16204	CCDC6	S367	ochoa	Coiled-coil domain-containing protein 6 (Papillary thyroid carcinoma-encoded protein) (Protein H4)	None
Q16513	PKN2	S366	ochoa	Serine/threonine-protein kinase N2 (EC 2.7.11.13) (PKN gamma) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2)	PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (PubMed:27104747). {ECO:0000269\|PubMed:10226025, ECO:0000269\|PubMed:10926925, ECO:0000269\|PubMed:11777936, ECO:0000269\|PubMed:11781095, ECO:0000269\|PubMed:15123640, ECO:0000269\|PubMed:15364941, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:20974804, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:27104747, ECO:0000269\|PubMed:9121475}.; FUNCTION: (Microbial infection) Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. {ECO:0000269\|PubMed:15364941}.
Q4KMP7	TBC1D10B	S322	ochoa	TBC1 domain family member 10B (Rab27A-GAP-beta)	Acts as a GTPase-activating protein for RAB3A, RAB22A, RAB27A, and RAB35. Does not act on RAB2A and RAB6A. {ECO:0000269\|PubMed:16923811, ECO:0000269\|PubMed:19077034}.
Q5JSH3	WDR44	T578	ochoa	WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11)	Downstream effector for Rab11 which regulates Rab11 intracellular membrane trafficking functions such as endocytic recycling, intracellular ciliogenesis and protein export (PubMed:31204173, PubMed:32344433). ATK1-mediated phosphorylation of WDR44 induces binding to Rab11 which activates endocytic recycling of transferrin receptor back to the plasma membrane (PubMed:31204173). When bound to Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-RAB11FIP3 complex, therefore inhibiting preciliary trafficking and ciliogenesis (PubMed:31204173). Participates in neo-synthesized protein export by connecting the endoplasmic reticulum (ER) with the endosomal tubule via direct interactions with the integral ER proteins VAPA or VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route (PubMed:32344433). {ECO:0000269\|PubMed:31204173, ECO:0000269\|PubMed:32344433}.
Q5QJE6	DNTTIP2	S92	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5T481	RBM20	S660	ochoa	RNA-binding protein 20 (RNA-binding motif protein 20)	RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH (PubMed:22466703, PubMed:24960161, PubMed:26604136, PubMed:27496873, PubMed:27531932, PubMed:29895960, PubMed:30948719, PubMed:32840935, PubMed:34732726, PubMed:35427468). Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts (PubMed:24960161, PubMed:30948719, PubMed:34732726). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (PubMed:27531932, PubMed:30948719). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (PubMed:27531932, PubMed:34732726). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity). {ECO:0000250\|UniProtKB:E9PT37, ECO:0000269\|PubMed:22466703, ECO:0000269\|PubMed:24960161, ECO:0000269\|PubMed:26604136, ECO:0000269\|PubMed:27496873, ECO:0000269\|PubMed:27531932, ECO:0000269\|PubMed:29895960, ECO:0000269\|PubMed:30948719, ECO:0000269\|PubMed:32840935, ECO:0000269\|PubMed:34732726, ECO:0000269\|PubMed:35427468}.
Q6DN14	MCTP1	S169	ochoa	Multiple C2 and transmembrane domain-containing protein 1	Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity. {ECO:0000250\|UniProtKB:A1ZBD6}.
Q6ICG6	KIAA0930	S328	ochoa	Uncharacterized protein KIAA0930	None
Q6KC79	NIPBL	S305	ochoa	Nipped-B-like protein (Delangin) (SCC2 homolog)	Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodimeric complex (also known as cohesin loading complex) with MAU2/SCC4 which mediates the loading of the cohesin complex onto chromatin (PubMed:22628566, PubMed:28914604). Plays a role in cohesin loading at sites of DNA damage. Its recruitment to double-strand breaks (DSBs) sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its recruitment to UV irradiation-induced DNA damage sites occurs in a ATM-, ATR-, RNF8- and RNF168-dependent manner (PubMed:28167679). Along with ZNF609, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (By similarity). {ECO:0000250\|UniProtKB:Q6KCD5, ECO:0000269\|PubMed:22628566, ECO:0000269\|PubMed:28167679, ECO:0000269\|PubMed:28914604}.
Q6NT76	HMBOX1	S152	ochoa	Homeobox-containing protein 1 (Homeobox telomere-binding protein 1) (Telomere-associated homeobox-containing protein 1)	Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA (PubMed:23685356, PubMed:23813958). Associates with the telomerase complex at sites of active telomere processing and positively regulates telomere elongation (PubMed:23685356). Important for TERT binding to chromatin, indicating a role in recruitment of the telomerase complex to telomeres (By similarity). Also plays a role in the alternative lengthening of telomeres (ALT) pathway in telomerase-negative cells where it promotes formation and/or maintenance of ALT-associated promyelocytic leukemia bodies (APBs) (PubMed:23813958). Enhances formation of telomere C-circles in ALT cells, suggesting a possible role in telomere recombination (PubMed:23813958). Might also be involved in the DNA damage response at telomeres (PubMed:23813958). {ECO:0000250\|UniProtKB:Q8BJA3, ECO:0000269\|PubMed:23685356, ECO:0000269\|PubMed:23813958}.
Q6P0Q8	MAST2	S1260	ochoa	Microtubule-associated serine/threonine-protein kinase 2 (EC 2.7.11.1)	Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity). {ECO:0000250}.
Q6PCB5	RSBN1L	S102	ochoa	Lysine-specific demethylase RSBN1L (EC 1.14.11.-) (Round spermatid basic protein 1-like protein)	Lysine-specific demethylase that specifically demethylates methylated lysine residues of proteins. {ECO:0000250\|UniProtKB:Q80T69}.
Q6PD62	CTR9	S1021	ochoa	RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1)	Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity). {ECO:0000250\|UniProtKB:Q62018, ECO:0000269\|PubMed:16024656, ECO:0000269\|PubMed:16307923, ECO:0000269\|PubMed:19345177, ECO:0000269\|PubMed:19952111, ECO:0000269\|PubMed:20178742, ECO:0000269\|PubMed:20541477, ECO:0000269\|PubMed:21329879}.
Q6T4R5	NHS	S1194	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6WKZ4	RAB11FIP1	S190	ochoa	Rab11 family-interacting protein 1 (Rab11-FIP1) (Rab-coupling protein)	A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Interaction with RAB14 may function in the process of neurite formation (PubMed:26032412). {ECO:0000269\|PubMed:11786538, ECO:0000269\|PubMed:15181150, ECO:0000269\|PubMed:15355514, ECO:0000269\|PubMed:16920206, ECO:0000269\|PubMed:26032412}.
Q6XZF7	DNMBP	S1365	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6ZRS2	SRCAP	S274	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q7KZI7	MARK2	S483	ochoa	Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:12429843, ECO:0000269\|PubMed:14976552, ECO:0000269\|PubMed:15158914, ECO:0000269\|PubMed:15324659, ECO:0000269\|PubMed:15365179, ECO:0000269\|PubMed:16775013, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:18626018, ECO:0000269\|PubMed:20194617, ECO:0000269\|PubMed:23666762}.
Q7Z460	CLASP1	S594	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z6L1	TECPR1	S390	ochoa	Tectonin beta-propeller repeat-containing protein 1	Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. {ECO:0000269\|PubMed:21575909, ECO:0000269\|PubMed:22342342}.
Q86TV6	TTC7B	S629	ochoa	Tetratricopeptide repeat protein 7B (TPR repeat protein 7B) (Tetratricopeptide repeat protein 7-like-1) (TPR repeat protein 7-like-1)	Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and HYCC1, via direct interactions (PubMed:26571211). {ECO:0000269\|PubMed:23229899, ECO:0000269\|PubMed:26571211}.
Q86UE4	MTDH	S533	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q8IWS0	PHF6	T187	ochoa	PHD finger protein 6 (PHD-like zinc finger protein)	Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269\|PubMed:23229552}.
Q8IZA0	KIAA0319L	S1009	ochoa	Dyslexia-associated protein KIAA0319-like protein (Adeno-associated virus receptor) (AAVR)	Possible role in axon guidance through interaction with RTN4R. {ECO:0000269\|PubMed:20697954}.; FUNCTION: (Microbial infection) Acts as a receptor for adeno-associated virus and is involved in adeno-associated virus infection through endocytosis system. {ECO:0000269\|PubMed:26814968}.
Q8IZD2	KMT2E	S1297	ochoa	Inactive histone-lysine N-methyltransferase 2E (Inactive lysine N-methyltransferase 2E) (Myeloid/lymphoid or mixed-lineage leukemia protein 5)	Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (PubMed:23629655, PubMed:23798402, PubMed:24130829). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (PubMed:23798402, PubMed:24130829). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation (By similarity). Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages including G1/S transition, S phase progression and mitotic entry (PubMed:14718661, PubMed:18573682, PubMed:19264965, PubMed:23629655). Recruited to E2F1 responsive promoters by HCFC1 where it stimulates tri-methylation of histone H3 at 'Lys-4' and transcriptional activation and thereby facilitates G1 to S phase transition (PubMed:23629655). During myoblast differentiation, required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells (By similarity). {ECO:0000250\|UniProtKB:Q3UG20, ECO:0000269\|PubMed:14718661, ECO:0000269\|PubMed:18573682, ECO:0000269\|PubMed:23629655, ECO:0000269\|PubMed:23798402, ECO:0000269\|PubMed:24130829}.; FUNCTION: [Isoform NKp44L]: Cellular ligand for NCR2/NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity. {ECO:0000269\|PubMed:23958951}.
Q8N3V7	SYNPO	S899	ochoa	Synaptopodin	Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.
Q8N488	RYBP	S185	ochoa	RING1 and YY1-binding protein (Apoptin-associating protein 1) (APAP-1) (Death effector domain-associated factor) (DED-associated factor) (YY1 and E4TF1-associated factor 1)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:25519132). Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (By similarity). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (PubMed:19098711). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis (PubMed:14765135, PubMed:27060496). May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (PubMed:11953439). May bind to DNA (By similarity). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3 (PubMed:27748911). {ECO:0000250\|UniProtKB:Q8CCI5, ECO:0000269\|PubMed:11953439, ECO:0000269\|PubMed:14765135, ECO:0000269\|PubMed:19098711, ECO:0000269\|PubMed:27060496, ECO:0000269\|PubMed:27748911}.
Q8NEM7	SUPT20H	S432	ochoa	Transcription factor SPT20 homolog (p38-interacting protein) (p38IP)	Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail (By similarity). Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000250, ECO:0000269\|PubMed:19893488}.
Q8NG31	KNL1	S633	ochoa	Outer kinetochore KNL1 complex subunit KNL1 (ALL1-fused gene from chromosome 15q14 protein) (AF15q14) (Bub-linking kinetochore protein) (Blinkin) (Cancer susceptibility candidate gene 5 protein) (Cancer/testis antigen 29) (CT29) (Kinetochore scaffold 1) (Kinetochore-null protein 1) (Protein CASC5) (Protein D40/AF15q14)	Acts as a component of the outer kinetochore KNL1 complex that serves as a docking point for spindle assembly checkpoint components and mediates microtubule-kinetochore interactions (PubMed:15502821, PubMed:17981135, PubMed:18045986, PubMed:19893618, PubMed:21199919, PubMed:22000412, PubMed:22331848, PubMed:27881301, PubMed:30100357). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules (PubMed:18045986, PubMed:19893618, PubMed:27881301). The outer kinetochore is made up of the ten-subunit KMN network, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle (PubMed:17981135, PubMed:19893618, PubMed:22000412, PubMed:38459127, PubMed:38459128). Required for kinetochore binding by a distinct subset of kMAPs (kinetochore-bound microtubule-associated proteins) and motors (PubMed:19893618). Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore (PubMed:18045986, PubMed:27881301). Can bind either to microtubules or to the protein phosphatase 1 (PP1) catalytic subunits PPP1CA and PPP1CC (via overlapping binding sites), it has higher affinity for PP1 (PubMed:30100357). Recruits MAD2L1 to the kinetochore and also directly links BUB1 and BUB1B to the kinetochore (PubMed:17981135, PubMed:19893618, PubMed:22000412, PubMed:22331848, PubMed:25308863). In addition to orienting mitotic chromosomes, it is also essential for alignment of homologous chromosomes during meiotic metaphase I (By similarity). In meiosis I, required to activate the spindle assembly checkpoint at unattached kinetochores to correct erroneous kinetochore-microtubule attachments (By similarity). {ECO:0000250\|UniProtKB:Q66JQ7, ECO:0000269\|PubMed:15502821, ECO:0000269\|PubMed:17981135, ECO:0000269\|PubMed:18045986, ECO:0000269\|PubMed:19893618, ECO:0000269\|PubMed:21199919, ECO:0000269\|PubMed:22000412, ECO:0000269\|PubMed:22331848, ECO:0000269\|PubMed:25308863, ECO:0000269\|PubMed:27881301, ECO:0000269\|PubMed:30100357, ECO:0000269\|PubMed:38459127, ECO:0000269\|PubMed:38459128}.
Q8NI27	THOC2	S1223	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8TC26	TMEM163	S61	ochoa	Transmembrane protein 163	Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (PubMed:25130899, PubMed:31697912, PubMed:36204728). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (PubMed:32492420). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (PubMed:35455965). {ECO:0000250\|UniProtKB:A9CMA6, ECO:0000269\|PubMed:25130899, ECO:0000269\|PubMed:31697912, ECO:0000269\|PubMed:32492420, ECO:0000269\|PubMed:35455965, ECO:0000269\|PubMed:36204728}.
Q8TEW0	PARD3	S807	ochoa	Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)	Adapter protein involved in asymmetrical cell division and cell polarization processes (PubMed:10954424, PubMed:27925688). Seems to play a central role in the formation of epithelial tight junctions (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (PubMed:10934474). Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (PubMed:19812038, PubMed:27925688). {ECO:0000250\|UniProtKB:Q99NH2, ECO:0000250\|UniProtKB:Q9Z340, ECO:0000269\|PubMed:10934474, ECO:0000269\|PubMed:10954424, ECO:0000269\|PubMed:19812038, ECO:0000269\|PubMed:27925688}.
Q8TF44	C2CD4C	S268	ochoa	C2 calcium-dependent domain-containing protein 4C (Nuclear-localized factor 3) (Protein FAM148C)	None
Q8WUA7	TBC1D22A	S171	ochoa	TBC1 domain family member 22A	May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000250}.
Q8WWI1	LMO7	S1597	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WXG6	MADD	S830	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q92613	JADE3	S780	ochoa	Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16)	Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. {ECO:0000269\|PubMed:16387653}.
Q92738	USP6NL	Y804	ochoa	USP6 N-terminal-like protein (Related to the N-terminus of tre) (RN-tre)	Acts as a GTPase-activating protein for RAB5A and RAB43. Involved in receptor trafficking. In complex with EPS8 inhibits internalization of EGFR. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for structural integrity of the Golgi complex. {ECO:0000269\|PubMed:11099046, ECO:0000269\|PubMed:17562788, ECO:0000269\|PubMed:17684057}.
Q92903	CDS1	T41	ochoa	Phosphatidate cytidylyltransferase 1 (EC 2.7.7.41) (CDP-DAG synthase 1) (CDP-DG synthase 1) (CDP-diacylglycerol synthase 1) (CDS 1) (CDP-diglyceride pyrophosphorylase 1) (CDP-diglyceride synthase 1) (CTP:phosphatidate cytidylyltransferase 1)	Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (PubMed:25375833, PubMed:9407135). Exhibits almost no acyl chain preference for PA, showing no discrimination for the sn-1/sn-2 acyl chain composition of PAs (PubMed:25375833). Plays an important role in regulating the growth of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540, PubMed:31548309). Positively regulates the differentiation and development of adipocytes (By similarity). {ECO:0000250\|UniProtKB:P98191, ECO:0000269\|PubMed:25375833, ECO:0000269\|PubMed:26946540, ECO:0000269\|PubMed:31548309, ECO:0000269\|PubMed:9407135}.
Q92974	ARHGEF2	S133	ochoa	Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40)	Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250\|UniProtKB:Q60875, ECO:0000250\|UniProtKB:Q865S3, ECO:0000269\|PubMed:19043560, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:28453519, ECO:0000269\|PubMed:9857026}.
Q92985	IRF7	S483	psp	Interferon regulatory factor 7 (IRF-7)	Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:28342865, PubMed:28768858). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:17574024, PubMed:32972995). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (By similarity). Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages (By similarity) (PubMed:11073981, PubMed:12374802, PubMed:15361868, PubMed:17404045). {ECO:0000250\|UniProtKB:P70434, ECO:0000269\|PubMed:11073981, ECO:0000269\|PubMed:12374802, ECO:0000269\|PubMed:15361868, ECO:0000269\|PubMed:17404045, ECO:0000269\|PubMed:17574024, ECO:0000269\|PubMed:28342865, ECO:0000269\|PubMed:28768858, ECO:0000269\|PubMed:32972995}.
Q96B97	SH3KBP1	S499	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96E39	RBMXL1	Y255	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96EZ8	MCRS1	S91	ochoa	Microspherule protein 1 (58 kDa microspherule protein) (Cell cycle-regulated factor p78) (INO80 complex subunit J) (MCRS2)	Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus (PubMed:11948183). As part of the NSL complex, may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. May also be an inhibitor of TERT telomerase activity (PubMed:15044100). Binds to G-quadruplex structures in mRNA (PubMed:16571602). Binds to RNA homomer poly(G) and poly(U) (PubMed:16571602). Maintains RHEB at the lysosome in its active GTP-bound form and prevents its interaction with the mTORC1 complex inhibitor TSC2, ensuring activation of the mTORC1 complex by RHEB (PubMed:25816988). Stabilizes the minus ends of kinetochore fibers by protecting them from depolymerization, ensuring functional spindle assembly during mitosis (PubMed:22081094, PubMed:27192185). Following phosphorylation by TTK/MPS1, enhances recruitment of KIF2A to the minus ends of mitotic spindle microtubules which promotes chromosome alignment (PubMed:30785839). Regulates the morphology of microtubule minus ends in mitotic spindle by maintaining them in a closed conformation characterized by the presence of an electron-dense cap (PubMed:36350698). Regulates G2/M transition and spindle assembly during oocyte meiosis (By similarity). Mediates histone modifications and transcriptional regulation in germinal vesicle oocytes which are required for meiotic progression (By similarity). Also regulates microtubule nucleation and spindle assembly by activating aurora kinases during oocyte meiosis (By similarity). Contributes to the establishment of centriolar satellites and also plays a role in primary cilium formation by recruiting TTBK2 to the mother centriole which is necessary for removal of the CP110 cap from the mother centriole, an early step in ciliogenesis (PubMed:27263857). Required for epiblast development during early embryogenesis (By similarity). Essential for cell viability (PubMed:16547491). {ECO:0000250\|UniProtKB:Q99L90, ECO:0000269\|PubMed:11948183, ECO:0000269\|PubMed:15044100, ECO:0000269\|PubMed:16547491, ECO:0000269\|PubMed:16571602, ECO:0000269\|PubMed:20018852, ECO:0000269\|PubMed:22081094, ECO:0000269\|PubMed:25816988, ECO:0000269\|PubMed:27192185, ECO:0000269\|PubMed:27263857, ECO:0000269\|PubMed:30785839, ECO:0000269\|PubMed:36350698}.
Q96HP0	DOCK6	S884	ochoa	Dedicator of cytokinesis protein 6	Acts as a guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity). {ECO:0000250, ECO:0000269\|PubMed:17196961}.
Q96N67	DOCK7	S900	ochoa	Dedicator of cytokinesis protein 7	Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250\|UniProtKB:Q8R1A4, ECO:0000269\|PubMed:16982419, ECO:0000269\|PubMed:29467281}.
Q96PK6	RBM14	S527	ochoa	RNA-binding protein 14 (Paraspeckle protein 2) (PSP2) (RNA-binding motif protein 14) (RRM-containing coactivator activator/modulator) (Synaptotagmin-interacting protein) (SYT-interacting protein)	Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1 (PubMed:11443112). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CPAP complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CPAP (PubMed:25385835). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also involved in the regulation of pre-mRNA alternative splicing (PubMed:37548402). {ECO:0000269\|PubMed:11443112, ECO:0000269\|PubMed:25385835, ECO:0000269\|PubMed:28712728, ECO:0000269\|PubMed:37548402}.
Q96Q89	KIF20B	S1592	ochoa	Kinesin-like protein KIF20B (Cancer/testis antigen 90) (CT90) (Kinesin family member 20B) (Kinesin-related motor interacting with PIN1) (M-phase phosphoprotein 1) (MPP1)	Plus-end-directed motor enzyme that is required for completion of cytokinesis (PubMed:11470801, PubMed:12740395). Required for proper midbody organization and abscission in polarized cortical stem cells. Plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. Participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in cerebral cortex growth (By similarity). Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000250\|UniProtKB:Q80WE4, ECO:0000269\|PubMed:11470801, ECO:0000269\|PubMed:12740395, ECO:0000269\|PubMed:17409436}.
Q96RU2	USP28	S494	ochoa	Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)	Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells (PubMed:24623306). {ECO:0000269\|PubMed:16901786, ECO:0000269\|PubMed:17558397, ECO:0000269\|PubMed:17873522, ECO:0000269\|PubMed:18662541, ECO:0000269\|PubMed:24623306}.
Q99504	EYA3	S266	ochoa\|psp	Protein phosphatase EYA3 (EC 3.1.3.48) (Eyes absent homolog 3)	Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (PubMed:19234442, PubMed:19351884). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity (By similarity). May be involved in development of the eye. {ECO:0000250\|UniProtKB:P97480, ECO:0000269\|PubMed:19234442, ECO:0000269\|PubMed:19351884}.
Q99569	PKP4	Y157	ochoa	Plakophilin-4 (p0071)	Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques. {ECO:0000269\|PubMed:17115030}.
Q99700	ATXN2	S867	ochoa	Ataxin-2 (Spinocerebellar ataxia type 2 protein) (Trinucleotide repeat-containing gene 13 protein)	Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269\|PubMed:18602463}.
Q9BQE9	BCL7B	S118	ochoa	B-cell CLL/lymphoma 7 protein family member B (allergen Hom s 3)	Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (PubMed:25569233). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (PubMed:25569233). May play a role in lung tumor development or progression (By similarity). {ECO:0000250\|UniProtKB:Q921K9, ECO:0000269\|PubMed:25569233}.
Q9BXK1	KLF16	S230	ochoa	Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Novel Sp1-like zinc finger transcription factor 2) (Transcription factor BTEB4) (Transcription factor NSLP2)	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.
Q9BXK1	KLF16	S234	ochoa	Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Novel Sp1-like zinc finger transcription factor 2) (Transcription factor BTEB4) (Transcription factor NSLP2)	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.
Q9BYW2	SETD2	S327	ochoa	Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.359) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)	Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (PubMed:19332550). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (PubMed:23622243). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (PubMed:24843002). Acts as a tumor suppressor (PubMed:24509477). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (PubMed:27317772). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (PubMed:21792193). Required during angiogenesis (By similarity). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (By similarity). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565, PubMed:28753426). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (PubMed:28753426). {ECO:0000250\|UniProtKB:E9Q5F9, ECO:0000269\|PubMed:16118227, ECO:0000269\|PubMed:19141475, ECO:0000269\|PubMed:21526191, ECO:0000269\|PubMed:21792193, ECO:0000269\|PubMed:23043551, ECO:0000269\|PubMed:23325844, ECO:0000269\|PubMed:23622243, ECO:0000269\|PubMed:24509477, ECO:0000269\|PubMed:24843002, ECO:0000269\|PubMed:27317772, ECO:0000269\|PubMed:27474439, ECO:0000269\|PubMed:27518565, ECO:0000269\|PubMed:28753426}.; FUNCTION: (Microbial infection) Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. {ECO:0000269\|PubMed:11461154}.
Q9BZF1	OSBPL8	S97	ochoa	Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)	Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:17991739, ECO:0000269\|PubMed:21698267, ECO:0000269\|PubMed:26206935}.
Q9BZF1	OSBPL8	S99	ochoa	Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)	Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:17991739, ECO:0000269\|PubMed:21698267, ECO:0000269\|PubMed:26206935}.
Q9C0D5	TANC1	S67	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9H019	MTFR1L	S238	ochoa	Mitochondrial fission regulator 1-like	Mitochondrial protein required for adaptation of miochondrial dynamics to metabolic changes. Regulates mitochondrial morphology at steady state and mediates AMPK-dependent stress-induced mitochondrial fragmentation via the control of OPA1 levels. {ECO:0000269\|PubMed:36367943}.
Q9H1Z4	WDR13	Y117	ochoa	WD repeat-containing protein 13	None
Q9H4L7	SMARCAD1	Y217	ochoa	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1) (EC 3.6.4.12) (ATP-dependent helicase 1) (hHEL1)	DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing. {ECO:0000269\|PubMed:21549307, ECO:0000269\|PubMed:22960744}.
Q9H6Z4	RANBP3	S359	ochoa	Ran-binding protein 3 (RanBP3)	Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. {ECO:0000269\|PubMed:11425870, ECO:0000269\|PubMed:11571268, ECO:0000269\|PubMed:11932251, ECO:0000269\|PubMed:19289081, ECO:0000269\|PubMed:9637251}.
Q9H7U1	CCSER2	S227	ochoa	Serine-rich coiled-coil domain-containing protein 2 (Coiled-coil serine-rich protein 2) (Protein GCAP14 homolog)	Microtubule-binding protein which might play a role in microtubule bundling. {ECO:0000250\|UniProtKB:Q3UHI0}.
Q9H813	PACC1	S54	ochoa	Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206)	Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269\|PubMed:31023925, ECO:0000269\|PubMed:31318332}.
Q9HCD6	TANC2	S1744	ochoa	Protein TANC2 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2)	Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines. {ECO:0000269\|PubMed:30021165}.
Q9NRA8	EIF4ENIF1	S353	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRA8	EIF4ENIF1	T357	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NS91	RAD18	S409	ochoa\|psp	E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (Postreplication repair protein RAD18) (hHR18) (hRAD18) (RING finger protein 73) (RING-type E3 ubiquitin transferase RAD18)	E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. {ECO:0000269\|PubMed:17108083, ECO:0000269\|PubMed:21659603}.
Q9NSI6	BRWD1	S1611	ochoa	Bromodomain and WD repeat-containing protein 1 (WD repeat-containing protein 9)	May be a transcriptional activator. May be involved in chromatin remodeling (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000250, ECO:0000269\|PubMed:21834987}.
Q9NTI5	PDS5B	S1165	ochoa	Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3)	Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269\|PubMed:10963680, ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19696148}.
Q9NW97	TMEM51	Y161	ochoa	Transmembrane protein 51	None
Q9NYF8	BCLAF1	S209	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYL2	MAP3K20	Y641	ochoa	Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase 7) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)	Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation (PubMed:10924358, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15350844, PubMed:15737997, PubMed:18331592, PubMed:20559024, PubMed:26999302, PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways (PubMed:11042189, PubMed:11836244, PubMed:12220515, PubMed:14521931, PubMed:15172994, PubMed:15737997, PubMed:32289254, PubMed:32610081, PubMed:35857590). Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6 (PubMed:11836244, PubMed:12220515). Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (PubMed:15350844, PubMed:21224381, PubMed:27859413). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (PubMed:15342622). {ECO:0000269\|PubMed:10924358, ECO:0000269\|PubMed:11042189, ECO:0000269\|PubMed:11836244, ECO:0000269\|PubMed:12220515, ECO:0000269\|PubMed:14521931, ECO:0000269\|PubMed:15172994, ECO:0000269\|PubMed:15342622, ECO:0000269\|PubMed:15350844, ECO:0000269\|PubMed:15737997, ECO:0000269\|PubMed:18331592, ECO:0000269\|PubMed:20559024, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:26999302, ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKalpha]: Key component of the stress-activated protein kinase signaling cascade in response to ribotoxic stress or UV-B irradiation (PubMed:32289254, PubMed:32610081, PubMed:35857590). Acts as the proximal sensor of ribosome collisions during the ribotoxic stress response (RSR): directly binds to the ribosome by inserting its flexible C-terminus into the ribosomal intersubunit space, thereby acting as a sentinel for colliding ribosomes (PubMed:32289254, PubMed:32610081). Upon ribosome collisions, activates either the stress-activated protein kinase signal transduction cascade or the integrated stress response (ISR), leading to programmed cell death or cell survival, respectively (PubMed:32610081). Dangerous levels of ribosome collisions trigger the autophosphorylation and activation of MAP3K20, which dissociates from colliding ribosomes and phosphorylates MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways that promote programmed cell death (PubMed:32289254, PubMed:32610081). Less dangerous levels of ribosome collisions trigger the integrated stress response (ISR): MAP3K20 activates EIF2AK4/GCN2 independently of its protein-kinase activity, promoting EIF2AK4/GCN2-mediated phosphorylation of EIF2S1/eIF-2-alpha (PubMed:32610081). Also part of the stress-activated protein kinase signaling cascade triggering the NLRP1 inflammasome in response to UV-B irradiation: ribosome collisions activate MAP3K20, which directly phosphorylates NLRP1, leading to activation of the NLRP1 inflammasome and subsequent pyroptosis (PubMed:35857590). NLRP1 is also phosphorylated by MAP kinase p38 downstream of MAP3K20 (PubMed:35857590). Also acts as a histone kinase by phosphorylating histone H3 at 'Ser-28' (H3S28ph) (PubMed:15684425). {ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.; FUNCTION: [Isoform ZAKbeta]: Isoform that lacks the C-terminal region that mediates ribosome-binding: does not act as a sensor of ribosome collisions in response to ribotoxic stress (PubMed:32289254, PubMed:32610081, PubMed:35857590). May act as an antagonist of isoform ZAKalpha: interacts with isoform ZAKalpha, leading to decrease the expression of isoform ZAKalpha (PubMed:27859413). {ECO:0000269\|PubMed:27859413, ECO:0000269\|PubMed:32289254, ECO:0000269\|PubMed:32610081, ECO:0000269\|PubMed:35857590}.
Q9NYV4	CDK12	S338	ochoa	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q9NZN8	CNOT2	S165	ochoa	CCR4-NOT transcription complex subunit 2 (CCR4-associated factor 2)	Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269\|PubMed:14707134, ECO:0000269\|PubMed:16712523, ECO:0000269\|PubMed:21299754, ECO:0000269\|PubMed:22367759}.
Q9P206	NHSL3	T410	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9UBN1	CACNG4	S259	ochoa	Voltage-dependent calcium channel gamma-4 subunit (Neuronal voltage-gated calcium channel gamma-4 subunit) (Transmembrane AMPAR regulatory protein gamma-4) (TARP gamma-4)	Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (PubMed:21127204). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs), including GRIA1 and GRIA4. Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization (PubMed:21172611). {ECO:0000269\|PubMed:21127204, ECO:0000269\|PubMed:21172611}.
Q9UBW5	BIN2	S294	ochoa	Bridging integrator 2 (Breast cancer-associated protein 1)	Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis. {ECO:0000269\|PubMed:23285027}.
Q9UGP4	LIMD1	S352	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UHB7	AFF4	S314	ochoa	AF4/FMR2 family member 4 (ALL1-fused gene from chromosome 5q31 protein) (Protein AF-5q31) (Major CDK9 elongation factor-associated protein)	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:23251033}.
Q9UJV3	MID2	S116	ochoa	Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midin-2) (Midline defect 2) (Midline-2) (RING finger protein 60) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1)	E3 ubiquitin ligase that plays a role in microtubule stabilization. Mediates the 'Lys-48'-linked polyubiquitination of LRRK2 to drive its localization to microtubules and its proteasomal degradation in neurons. This ubiquitination inhibits LRRK2 kinase activation by RAB29 (PubMed:35266954). {ECO:0000269\|PubMed:35266954, ECO:0000303\|PubMed:24115387}.
Q9UKE5	TNIK	S898	ochoa	TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)	Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269\|PubMed:10521462, ECO:0000269\|PubMed:15342639, ECO:0000269\|PubMed:19061864, ECO:0000269\|PubMed:19816403, ECO:0000269\|PubMed:20159449, ECO:0000269\|PubMed:21690388, ECO:0000269\|PubMed:26437443}.
Q9UKI8	TLK1	S109	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UMD9	COL17A1	S118	ochoa	Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen (120 kDa linear IgA dermatosis antigen) (Linear IgA disease antigen 1) (LAD-1); 97 kDa linear IgA disease antigen (97 kDa linear IgA bullous dermatosis antigen) (97 kDa LAD antigen) (97-LAD) (Linear IgA bullous disease antigen of 97 kDa) (LABD97)]	May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; FUNCTION: The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies.
Q9UMZ2	SYNRG	S473	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UN36	NDRG2	S350	ochoa\|psp	Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Syld709613)	Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. {ECO:0000269\|PubMed:12845671, ECO:0000269\|PubMed:16103061, ECO:0000269\|PubMed:21247902}.
Q9UPN3	MACF1	S7322	psp	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPQ0	LIMCH1	S303	ochoa	LIM and calponin homology domains-containing protein 1	Actin stress fibers-associated protein that activates non-muscle myosin IIa. Activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. Through the activation of non-muscle myosin IIa, positively regulates actin stress fibers assembly and stabilizes focal adhesions. It therefore negatively regulates cell spreading and cell migration. {ECO:0000269\|PubMed:28228547}.
Q9UQ35	SRRM2	S914	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S994	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2421	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2694	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9Y2H5	PLEKHA6	S459	ochoa	Pleckstrin homology domain-containing family A member 6 (PH domain-containing family A member 6) (Phosphoinositol 3-phosphate-binding protein 3) (PEPP-3)	None
Q9Y2U5	MAP3K2	T318	ochoa	Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2)	Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. {ECO:0000250, ECO:0000269\|PubMed:10713157, ECO:0000269\|PubMed:16001074}.
Q9Y2W1	THRAP3	S312	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y3R5	DOP1B	S556	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y490	TLN1	S429	ochoa	Talin-1	High molecular weight cytoskeletal protein concentrated at regions of cell-matrix and cell-cell contacts. Involved in connections of major cytoskeletal structures to the plasma membrane. With KANK1 co-organize the assembly of cortical microtubule stabilizing complexes (CMSCs) positioned to control microtubule-actin crosstalk at focal adhesions (FAs) rims. {ECO:0000250\|UniProtKB:P26039}.
Q9Y4F3	MARF1	S957	ochoa	Meiosis regulator and mRNA stability factor 1 (Limkain-b1) (Meiosis arrest female protein 1)	Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks (By similarity). {ECO:0000250}.
Q9Y4H2	IRS2	Y598	ochoa	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
P08238	HSP90AB1	S474	Sugiyama	Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3)	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269\|PubMed:16478993, ECO:0000269\|PubMed:18239673, ECO:0000269\|PubMed:19696785, ECO:0000269\|PubMed:20353823, ECO:0000269\|PubMed:24613385, ECO:0000269\|PubMed:32272059, ECO:0000303\|PubMed:25973397, ECO:0000303\|PubMed:26991466, ECO:0000303\|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269\|PubMed:21949862, ECO:0000305\|PubMed:22066472}.
P23381	WARS1	S357	Sugiyama	Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Interferon-induced protein 53) (IFP53) (Tryptophanyl-tRNA synthetase) (TrpRS) (hWRS) [Cleaved into: T1-TrpRS; T2-TrpRS]	Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). {ECO:0000269\|PubMed:1373391, ECO:0000269\|PubMed:1761529, ECO:0000269\|PubMed:28369220}.; FUNCTION: [Isoform 1]: Has no angiostatic activity. {ECO:0000269\|PubMed:11773625, ECO:0000269\|PubMed:11773626}.; FUNCTION: [T2-TrpRS]: Possesses an angiostatic activity but has no aminoacylation activity (PubMed:11773625, PubMed:11773626, PubMed:14630953). Inhibits fluid shear stress-activated responses of endothelial cells (PubMed:14630953). Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (PubMed:14630953). {ECO:0000269\|PubMed:11773625, ECO:0000269\|PubMed:11773626, ECO:0000269\|PubMed:14630953}.; FUNCTION: [Isoform 2]: Has an angiostatic activity. {ECO:0000269\|PubMed:11773625, ECO:0000269\|PubMed:11773626}.
O95835	LATS1	S876	Sugiyama	Serine/threonine-protein kinase LATS1 (EC 2.7.11.1) (Large tumor suppressor homolog 1) (WARTS protein kinase) (h-warts)	Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:10518011, PubMed:10831611, PubMed:18158288, PubMed:26437443, PubMed:28068668). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288, PubMed:26437443, PubMed:28068668). Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288, PubMed:26437443, PubMed:28068668). Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint (PubMed:15122335, PubMed:19927127). Negatively regulates G2/M transition by down-regulating CDK1 kinase activity (PubMed:9988268). Involved in the control of p53 expression (PubMed:15122335). Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1 (PubMed:15220930). May also play a role in endocrine function. Plays a role in mammary gland epithelial cell differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1 (PubMed:28068668). Acts as an activator of the NLRP3 inflammasome by mediating phosphorylation of 'Ser-265' of NLRP3 following NLRP3 palmitoylation, promoting NLRP3 activation by NEK7 (PubMed:39173637). {ECO:0000269\|PubMed:10518011, ECO:0000269\|PubMed:10831611, ECO:0000269\|PubMed:15122335, ECO:0000269\|PubMed:15220930, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:19927127, ECO:0000269\|PubMed:26437443, ECO:0000269\|PubMed:28068668, ECO:0000269\|PubMed:39173637, ECO:0000269\|PubMed:9988268}.
Q9ULD2	MTUS1	Y205	Sugiyama	Microtubule-associated tumor suppressor 1 (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Mitochondrial tumor suppressor 1)	Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269\|PubMed:12692079, ECO:0000269\|PubMed:19794912}.
Q00987	MDM2	S192	iPTMNet	E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Hdm2) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)	E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903). {ECO:0000250\|UniProtKB:P23804, ECO:0000269\|PubMed:12821780, ECO:0000269\|PubMed:15053880, ECO:0000269\|PubMed:15195100, ECO:0000269\|PubMed:15632057, ECO:0000269\|PubMed:16337594, ECO:0000269\|PubMed:17290220, ECO:0000269\|PubMed:19098711, ECO:0000269\|PubMed:19219073, ECO:0000269\|PubMed:19837670, ECO:0000269\|PubMed:19965871, ECO:0000269\|PubMed:20173098, ECO:0000269\|PubMed:20385133, ECO:0000269\|PubMed:20858735, ECO:0000269\|PubMed:22128911, ECO:0000269\|PubMed:29681526, ECO:0000269\|PubMed:30879903}.
Q14152	EIF3A	S1262	Sugiyama	Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185)	RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:11169732, PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773, PubMed:27462815). {ECO:0000255\|HAMAP-Rule:MF_03000, ECO:0000269\|PubMed:11169732, ECO:0000269\|PubMed:17581632, ECO:0000269\|PubMed:25849773, ECO:0000269\|PubMed:27462815}.; FUNCTION: (Microbial infection) Essential for the initiation of translation on type-1 viral ribosomal entry sites (IRESs), like for HCV, PV, EV71 or BEV translation (PubMed:23766293, PubMed:24357634). {ECO:0000269\|PubMed:23766293, ECO:0000269\|PubMed:24357634}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269\|PubMed:18056426}.
P08151	GLI1	T527	GPS6	Zinc finger protein GLI1 (Glioma-associated oncogene) (Oncogene GLI)	Acts as a transcriptional activator (PubMed:10806483, PubMed:19706761, PubMed:19878745, PubMed:24076122, PubMed:24217340, PubMed:24311597). Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456, PubMed:24217340, PubMed:8378770). Regulates the transcription of specific genes during normal development (PubMed:19706761). Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling (PubMed:19706761, PubMed:28973407). Plays a role in cell proliferation and differentiation via its role in SHH signaling (PubMed:11238441, PubMed:28973407). {ECO:0000269\|PubMed:10806483, ECO:0000269\|PubMed:11238441, ECO:0000269\|PubMed:19706761, ECO:0000269\|PubMed:19878745, ECO:0000269\|PubMed:2105456, ECO:0000269\|PubMed:24076122, ECO:0000269\|PubMed:24217340, ECO:0000269\|PubMed:24311597, ECO:0000269\|PubMed:28973407, ECO:0000269\|PubMed:8378770}.; FUNCTION: [Isoform 2]: Acts as a transcriptional activator, but activates a different set of genes than isoform 1. Activates expression of CD24, unlike isoform 1. Mediates SHH signaling. Promotes cancer cell migration. {ECO:0000269\|PubMed:19706761}.
Q86VM9	ZC3H18	S607	Sugiyama	Zinc finger CCCH domain-containing protein 18 (Nuclear protein NHN1)	None
Q14C86	GAPVD1	S746	Sugiyama	GTPase-activating protein and VPS9 domain-containing protein 1 (GAPex-5) (Rab5-activating protein 6)	Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras. {ECO:0000269\|PubMed:16410077}.
Q8WVC0	LEO1	S72	Sugiyama	RNA polymerase-associated protein LEO1 (Replicative senescence down-regulated leo1-like protein)	Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling. {ECO:0000269\|PubMed:15632063, ECO:0000269\|PubMed:15791002, ECO:0000269\|PubMed:19345177, ECO:0000269\|PubMed:19952111, ECO:0000269\|PubMed:20178742}.
Q8TD08	MAPK15	S353	Sugiyama	Mitogen-activated protein kinase 15 (MAP kinase 15) (MAPK 15) (EC 2.7.11.24) (Extracellular signal-regulated kinase 7) (ERK-7) (Extracellular signal-regulated kinase 8) (ERK-8)	Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner (PubMed:20733054, PubMed:21847093, PubMed:22948227, PubMed:24618899, PubMed:29021280). Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation (PubMed:22948227). Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling (PubMed:29021280). Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar-coated proteins (PubMed:24618899). Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion (PubMed:21847093). Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA (PubMed:20733054). Regulates DA transporter (DAT) activity and protein expression via activation of RhoA (PubMed:28842414). In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression (PubMed:26595526). Also functions in a kinase activity-independent manner as a negative regulator of growth (By similarity). Phosphorylates in vitro FOS and MBP (PubMed:11875070, PubMed:16484222, PubMed:19166846, PubMed:20638370). During oocyte maturation, plays a key role in the microtubule organization and meiotic cell cycle progression in oocytes, fertilized eggs, and early embryos (By similarity). Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity (PubMed:21190936). {ECO:0000250\|UniProtKB:Q80Y86, ECO:0000250\|UniProtKB:Q9Z2A6, ECO:0000269\|PubMed:11875070, ECO:0000269\|PubMed:16484222, ECO:0000269\|PubMed:19166846, ECO:0000269\|PubMed:20638370, ECO:0000269\|PubMed:20733054, ECO:0000269\|PubMed:21190936, ECO:0000269\|PubMed:21847093, ECO:0000269\|PubMed:22948227, ECO:0000269\|PubMed:24618899, ECO:0000269\|PubMed:26595526, ECO:0000269\|PubMed:28842414, ECO:0000269\|PubMed:29021280}.
P13667	PDIA4	S130	Sugiyama	Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72)	None
Q9H093	NUAK2	S331	Sugiyama	NUAK family SNF1-like kinase 2 (EC 2.7.11.1) (Omphalocele kinase 2) (SNF1/AMP kinase-related kinase) (SNARK)	Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube closure during embryonic development through LATS2 phosphorylation and regulation of the nuclear localization of YAP1 a critical downstream regulatory target in the Hippo signaling pathway (PubMed:32845958). {ECO:0000269\|PubMed:14575707, ECO:0000269\|PubMed:14976552, ECO:0000269\|PubMed:15345718, ECO:0000269\|PubMed:19927127, ECO:0000269\|PubMed:32845958}.
Q9NRM7	LATS2	S839	Sugiyama	Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm) (Warts-like kinase)	Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:18158288, PubMed:26437443, PubMed:26598551, PubMed:34404733). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:26437443, PubMed:26598551, PubMed:34404733). Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:26598551, PubMed:34404733). Also phosphorylates YAP1 in response to cell contact inhibition-driven WWP1 ubiquitination of AMOTL2, which results in LATS2 activation (PubMed:34404733). Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability (PubMed:10871863). Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity (PubMed:12853976). Negative regulator of the androgen receptor (PubMed:15131260). Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities (PubMed:21952048). This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ (PubMed:21952048). Acts as an activator of the NLRP3 inflammasome by mediating phosphorylation of 'Ser-265' of NLRP3 following NLRP3 palmitoylation, promoting NLRP3 activation by NEK7 (PubMed:39173637). {ECO:0000269\|PubMed:10871863, ECO:0000269\|PubMed:12853976, ECO:0000269\|PubMed:15131260, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:21952048, ECO:0000269\|PubMed:26437443, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:34404733, ECO:0000269\|PubMed:39173637}.
O43663	PRC1	Y560	ochoa	Protein regulator of cytokinesis 1	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269\|PubMed:12082078, ECO:0000269\|PubMed:15297875, ECO:0000269\|PubMed:15625105, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:17409436, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:20691902, ECO:0000269\|PubMed:9885575}.
O95336	PGLS	S52	ochoa	6-phosphogluconolactonase (6PGL) (EC 3.1.1.31)	Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. {ECO:0000269\|PubMed:10518023}.
P17029	ZKSCAN1	T365	ochoa	Zinc finger protein with KRAB and SCAN domains 1 (Zinc finger protein 139) (Zinc finger protein 36) (Zinc finger protein KOX18)	May be involved in transcriptional regulation.
P35269	GTF2F1	S224	ochoa	General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74)	TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269\|PubMed:10428810}.
Q13950	RUNX2	S240	ochoa	Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)	Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis (PubMed:28505335, PubMed:28703881, PubMed:28738062). Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Inhibits KAT6B-dependent transcriptional activation. {ECO:0000250, ECO:0000269\|PubMed:11965546, ECO:0000269\|PubMed:28505335, ECO:0000269\|PubMed:28703881, ECO:0000269\|PubMed:28738062}.
Q14938	NFIX	S271	ochoa	Nuclear factor 1 X-type (NF1-X) (Nuclear factor 1/X) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/X) (NF-I/X) (NFI-X) (TGGCA-binding protein)	Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Q5T1M5	FKBP15	S1161	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q6ZSR9	None	Y293	ochoa	Uncharacterized protein FLJ45252	None
Q86US8	SMG6	S264	ochoa	Telomerase-binding protein EST1A (EC 3.1.-.-) (Ever shorter telomeres 1A) (hEST1A) (Nonsense mediated mRNA decay factor SMG6) (Smg-6 homolog) (hSmg5/7a)	Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (PubMed:19179534). May have a general role in telomere regulation (PubMed:12676087, PubMed:12699629). Promotes in vitro the ability of TERT to elongate telomeres (PubMed:12676087, PubMed:12699629). Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization (PubMed:12676087, PubMed:12699629). Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER) (PubMed:12676087, PubMed:12699629). {ECO:0000269\|PubMed:12676087, ECO:0000269\|PubMed:12699629, ECO:0000269\|PubMed:19179534}.; FUNCTION: Plays a role in nonsense-mediated mRNA decay (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030). {ECO:0000269\|PubMed:17053788, ECO:0000269\|PubMed:18974281, ECO:0000269\|PubMed:19060897, ECO:0000269\|PubMed:20930030}.
Q86YT6	MIB1	S411	ochoa	E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1) (Zinc finger ZZ type with ankyrin repeat domain protein 2)	E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity). Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation. {ECO:0000250, ECO:0000269\|PubMed:24121310}.; FUNCTION: (Microbial infection) During adenovirus infection, mediates ubiquitination of Core-capsid bridging protein. This allows viral genome delivery into nucleus for infection. {ECO:0000269\|PubMed:31851912}.
Q8IZH2	XRN1	S1656	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8N680	ZBTB2	S491	ochoa	Zinc finger and BTB domain-containing protein 2	May be involved in transcriptional regulation.
Q8NEY1	NAV1	S311	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8WUZ0	BCL7C	S103	ochoa	B-cell CLL/lymphoma 7 protein family member C	May play an anti-apoptotic role. {ECO:0000250}.
Q92614	MYO18A	S160	ochoa	Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)	May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250\|UniProtKB:Q9JMH9, ECO:0000269\|PubMed:16087679, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:19837035, ECO:0000269\|PubMed:21123169, ECO:0000269\|PubMed:23345592, ECO:0000269\|PubMed:25965346, ECO:0000269\|PubMed:27467939}.
Q99558	MAP3K14	S820	psp	Mitogen-activated protein kinase kinase kinase 14 (EC 2.7.11.25) (NF-kappa-beta-inducing kinase) (HsNIK) (Serine/threonine-protein kinase NIK)	Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Phosphorylates CHUK/IKKA, thereby promoting proteolytic processing of NFKB2/P100, which leads to NF-kappa-B activation via the non-canonical pathway (PubMed:25406581, PubMed:29230214). Has an essential role in the non-canonical NF-kappa-B signaling that regulates genes encoding molecules involved in B-cell survival, lymphoid organogenesis, and immune response (PubMed:25406581). Could act in a receptor-selective manner. {ECO:0000269\|PubMed:15084608, ECO:0000269\|PubMed:25406581}.
Q9P1Y5	CAMSAP3	S379	ochoa	Calmodulin-regulated spectrin-associated protein 3 (Protein Nezha)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742, PubMed:27802168). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). {ECO:0000250\|UniProtKB:Q80VC9, ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:26715742, ECO:0000269\|PubMed:27693509, ECO:0000269\|PubMed:27802168, ECO:0000269\|PubMed:28089391, ECO:0000269\|PubMed:28386021}.
Q9ULH1	ASAP1	S785	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879). {ECO:0000250, ECO:0000269\|PubMed:20393563, ECO:0000269\|PubMed:25673879}.
Q9Y6Q9	NCOA3	S863	ochoa	Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.
A7KAX9	ARHGAP32	S709	ochoa	Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (GTPase regulator interacting with TrkA) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)	GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12446789, ECO:0000269\|PubMed:12454018, ECO:0000269\|PubMed:12531901, ECO:0000269\|PubMed:12788081, ECO:0000269\|PubMed:12819203, ECO:0000269\|PubMed:12857875, ECO:0000269\|PubMed:17663722}.
P05060	CHGB	S317	ochoa	Secretogranin-1 (Chromogranin-B) (CgB) (Secretogranin I) (SgI) [Cleaved into: PE-11; GAWK peptide; CCB peptide]	Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
P05060	CHGB	S320	ochoa	Secretogranin-1 (Chromogranin-B) (CgB) (Secretogranin I) (SgI) [Cleaved into: PE-11; GAWK peptide; CCB peptide]	Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
P51003	PAPOLA	S532	ochoa	Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha)	Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000269\|PubMed:19224921}.
Q15057	ACAP2	S384	ochoa	Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2)	GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). Doesn't show GAP activity for RAB35 (PubMed:30905672). {ECO:0000269\|PubMed:11062263, ECO:0000269\|PubMed:30905672}.
Q9P2Q2	FRMD4A	S952	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9UJD0	RIMS3	S114	ochoa	Regulating synaptic membrane exocytosis protein 3 (Nim3) (RIM3 gamma) (Rab-3-interacting molecule 3) (RIM 3)	Regulates synaptic membrane exocytosis. {ECO:0000250}.

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reactome_id	name	p	-log10_p
R-HSA-111465	Apoptotic cleavage of cellular proteins	1.640583e-09	8.785
R-HSA-162582	Signal Transduction	8.846895e-09	8.053
R-HSA-75153	Apoptotic execution phase	4.453316e-08	7.351
R-HSA-1640170	Cell Cycle	1.521381e-07	6.818
R-HSA-68877	Mitotic Prometaphase	3.032776e-07	6.518
R-HSA-2500257	Resolution of Sister Chromatid Cohesion	3.690753e-07	6.433
R-HSA-9648025	EML4 and NUDC in mitotic spindle formation	1.387103e-06	5.858
R-HSA-69278	Cell Cycle, Mitotic	1.430974e-06	5.844
R-HSA-68882	Mitotic Anaphase	3.128118e-06	5.505
R-HSA-68886	M Phase	3.593508e-06	5.444
R-HSA-2555396	Mitotic Metaphase and Anaphase	3.522057e-06	5.453
R-HSA-2467813	Separation of Sister Chromatids	6.692701e-06	5.174
R-HSA-1169410	Antiviral mechanism by IFN-stimulated genes	1.856037e-05	4.731
R-HSA-9927432	Developmental Lineage of Mammary Gland Myoepithelial Cells	2.127730e-05	4.672
R-HSA-4839726	Chromatin organization	2.880892e-05	4.540
R-HSA-9675108	Nervous system development	3.048941e-05	4.516
R-HSA-437239	Recycling pathway of L1	3.499587e-05	4.456
R-HSA-2980766	Nuclear Envelope Breakdown	3.630325e-05	4.440
R-HSA-159236	Transport of Mature mRNA derived from an Intron-Containing Transcript	4.070965e-05	4.390
R-HSA-72203	Processing of Capped Intron-Containing Pre-mRNA	4.228551e-05	4.374
R-HSA-422475	Axon guidance	4.330739e-05	4.363
R-HSA-351906	Apoptotic cleavage of cell adhesion proteins	5.352905e-05	4.271
R-HSA-141444	Amplification of signal from unattached kinetochores via a MAD2 inhibitory si...	6.082252e-05	4.216
R-HSA-141424	Amplification of signal from the kinetochores	6.082252e-05	4.216
R-HSA-1169408	ISG15 antiviral mechanism	5.896511e-05	4.229
R-HSA-69618	Mitotic Spindle Checkpoint	6.372115e-05	4.196
R-HSA-199991	Membrane Trafficking	7.974261e-05	4.098
R-HSA-373760	L1CAM interactions	8.195464e-05	4.086
R-HSA-446353	Cell-extracellular matrix interactions	9.579530e-05	4.019
R-HSA-1500931	Cell-Cell communication	1.032643e-04	3.986
R-HSA-5619107	Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC...	1.085514e-04	3.964
R-HSA-9931510	Phosphorylated BMAL1:CLOCK (ARNTL:CLOCK) activates expression of core clock gene...	1.237731e-04	3.907
R-HSA-180746	Nuclear import of Rev protein	1.214480e-04	3.916
R-HSA-1855196	IP3 and IP4 transport between cytosol and nucleus	1.434766e-04	3.843
R-HSA-1855229	IP6 and IP7 transport between cytosol and nucleus	1.434766e-04	3.843
R-HSA-5663202	Diseases of signal transduction by growth factor receptors and second messengers	1.503068e-04	3.823
R-HSA-3247509	Chromatin modifying enzymes	1.506729e-04	3.822
R-HSA-3301854	Nuclear Pore Complex (NPC) Disassembly	1.569504e-04	3.804
R-HSA-177243	Interactions of Rev with host cellular proteins	1.646484e-04	3.783
R-HSA-72202	Transport of Mature Transcript to Cytoplasm	1.942414e-04	3.712
R-HSA-3214841	PKMTs methylate histone lysines	2.075482e-04	3.683
R-HSA-9924644	Developmental Lineages of the Mammary Gland	2.324331e-04	3.634
R-HSA-1855170	IPs transport between nucleus and cytosol	2.432610e-04	3.614
R-HSA-159227	Transport of the SLBP independent Mature mRNA	2.432610e-04	3.614
R-HSA-3769402	Deactivation of the beta-catenin transactivating complex	2.556725e-04	3.592
R-HSA-159230	Transport of the SLBP Dependant Mature mRNA	3.123658e-04	3.505
R-HSA-2028269	Signaling by Hippo	3.054410e-04	3.515
R-HSA-165054	Rev-mediated nuclear export of HIV RNA	3.225248e-04	3.491
R-HSA-170822	Regulation of Glucokinase by Glucokinase Regulatory Protein	3.123658e-04	3.505
R-HSA-168276	NS1 Mediated Effects on Host Pathways	4.038830e-04	3.394
R-HSA-68884	Mitotic Telophase/Cytokinesis	4.286696e-04	3.368
R-HSA-6796648	TP53 Regulates Transcription of DNA Repair Genes	6.017067e-04	3.221
R-HSA-193648	NRAGE signals death through JNK	6.376044e-04	3.195
R-HSA-73887	Death Receptor Signaling	6.433793e-04	3.192
R-HSA-69620	Cell Cycle Checkpoints	6.515066e-04	3.186
R-HSA-8869496	TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif...	7.135159e-04	3.147
R-HSA-6784531	tRNA processing in the nucleus	6.954460e-04	3.158
R-HSA-180910	Vpr-mediated nuclear import of PICs	7.818609e-04	3.107
R-HSA-9931521	The CRY:PER:kinase complex represses transactivation by the BMAL:CLOCK (ARNTL:CL...	9.043460e-04	3.044
R-HSA-9764790	Positive Regulation of CDH1 Gene Transcription	9.138259e-04	3.039
R-HSA-191859	snRNP Assembly	1.059885e-03	2.975
R-HSA-194441	Metabolism of non-coding RNA	1.059885e-03	2.975
R-HSA-446728	Cell junction organization	1.043431e-03	2.982
R-HSA-9734779	Developmental Cell Lineages of the Integumentary System	1.054212e-03	2.977
R-HSA-913531	Interferon Signaling	1.078133e-03	2.967
R-HSA-438064	Post NMDA receptor activation events	1.081687e-03	2.966
R-HSA-6802952	Signaling by BRAF and RAF1 fusions	1.124123e-03	2.949
R-HSA-2470946	Cohesin Loading onto Chromatin	1.219190e-03	2.914
R-HSA-159231	Transport of Mature mRNA Derived from an Intronless Transcript	1.183315e-03	2.927
R-HSA-983189	Kinesins	1.245450e-03	2.905
R-HSA-3134963	DEx/H-box helicases activate type I IFN and inflammatory cytokines production	1.458754e-03	2.836
R-HSA-8876384	Listeria monocytogenes entry into host cells	1.424127e-03	2.846
R-HSA-159234	Transport of Mature mRNAs Derived from Intronless Transcripts	1.441337e-03	2.841
R-HSA-176033	Interactions of Vpr with host cellular proteins	1.441337e-03	2.841
R-HSA-9612973	Autophagy	1.463882e-03	2.834
R-HSA-1445148	Translocation of SLC2A4 (GLUT4) to the plasma membrane	1.563955e-03	2.806
R-HSA-168333	NEP/NS2 Interacts with the Cellular Export Machinery	1.627524e-03	2.788
R-HSA-3928664	Ephrin signaling	1.677249e-03	2.775
R-HSA-9820841	M-decay: degradation of maternal mRNAs by maternally stored factors	1.744679e-03	2.758
R-HSA-168271	Transport of Ribonucleoproteins into the Host Nucleus	1.744679e-03	2.758
R-HSA-2995410	Nuclear Envelope (NE) Reassembly	1.816931e-03	2.741
R-HSA-168274	Export of Viral Ribonucleoproteins from Nucleus	1.941221e-03	2.712
R-HSA-373755	Semaphorin interactions	1.975797e-03	2.704
R-HSA-9764265	Regulation of CDH1 Expression and Function	2.236471e-03	2.650
R-HSA-9764274	Regulation of Expression and Function of Type I Classical Cadherins	2.236471e-03	2.650
R-HSA-9764260	Regulation of Expression and Function of Type II Classical Cadherins	2.350068e-03	2.629
R-HSA-5674400	Constitutive Signaling by AKT1 E17K in Cancer	2.376654e-03	2.624
R-HSA-9764302	Regulation of CDH19 Expression and Function	2.589662e-03	2.587
R-HSA-9759476	Regulation of Homotypic Cell-Cell Adhesion	2.792724e-03	2.554
R-HSA-193704	p75 NTR receptor-mediated signalling	2.835004e-03	2.547
R-HSA-9700645	ALK mutants bind TKIs	3.004109e-03	2.522
R-HSA-264870	Caspase-mediated cleavage of cytoskeletal proteins	3.004109e-03	2.522
R-HSA-6802957	Oncogenic MAPK signaling	3.417033e-03	2.466
R-HSA-204998	Cell death signalling via NRAGE, NRIF and NADE	3.489599e-03	2.457
R-HSA-9839394	TGFBR3 expression	3.783658e-03	2.422
R-HSA-3928662	EPHB-mediated forward signaling	3.536253e-03	2.451
R-HSA-1632852	Macroautophagy	3.750065e-03	2.426
R-HSA-199920	CREB phosphorylation	4.250475e-03	2.372
R-HSA-9772755	Formation of WDR5-containing histone-modifying complexes	4.206822e-03	2.376
R-HSA-6811434	COPI-dependent Golgi-to-ER retrograde traffic	4.074640e-03	2.390
R-HSA-3700989	Transcriptional Regulation by TP53	3.950692e-03	2.403
R-HSA-2468052	Establishment of Sister Chromatid Cohesion	4.412923e-03	2.355
R-HSA-428359	Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RN...	4.412923e-03	2.355
R-HSA-9764561	Regulation of CDH1 Function	4.477398e-03	2.349
R-HSA-190840	Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane	4.580630e-03	2.339
R-HSA-9827857	Specification of primordial germ cells	4.580630e-03	2.339
R-HSA-9856651	MITF-M-dependent gene expression	4.990033e-03	2.302
R-HSA-3371556	Cellular response to heat stress	5.102965e-03	2.292
R-HSA-4420097	VEGFA-VEGFR2 Pathway	5.373555e-03	2.270
R-HSA-380320	Recruitment of NuMA to mitotic centrosomes	5.425034e-03	2.266
R-HSA-9933939	Formation of the polybromo-BAF (pBAF) complex	5.470395e-03	2.262
R-HSA-8952158	RUNX3 regulates BCL2L11 (BIM) transcription	5.504975e-03	2.259
R-HSA-9938206	Developmental Lineage of Mammary Stem Cells	5.975029e-03	2.224
R-HSA-5693532	DNA Double-Strand Break Repair	6.374586e-03	2.196
R-HSA-168164	Toll Like Receptor 3 (TLR3) Cascade	5.927259e-03	2.227
R-HSA-190872	Transport of connexons to the plasma membrane	5.923128e-03	2.227
R-HSA-69275	G2/M Transition	6.217389e-03	2.206
R-HSA-9926550	Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adh...	5.923128e-03	2.227
R-HSA-416482	G alpha (12/13) signalling events	6.443291e-03	2.191
R-HSA-428890	Role of ABL in ROBO-SLIT signaling	6.558277e-03	2.183
R-HSA-9933946	Formation of the embryonic stem cell BAF (esBAF) complex	7.248181e-03	2.140
R-HSA-9619483	Activation of AMPK downstream of NMDARs	7.046988e-03	2.152
R-HSA-3371453	Regulation of HSF1-mediated heat shock response	7.573988e-03	2.121
R-HSA-193639	p75NTR signals via NF-kB	7.248181e-03	2.140
R-HSA-418885	DCC mediated attractive signaling	7.248181e-03	2.140
R-HSA-157858	Gap junction trafficking and regulation	7.635887e-03	2.117
R-HSA-453274	Mitotic G2-G2/M phases	7.180604e-03	2.144
R-HSA-450294	MAP kinase activation	7.683392e-03	2.114
R-HSA-442755	Activation of NMDA receptors and postsynaptic events	7.573988e-03	2.121
R-HSA-109581	Apoptosis	7.548355e-03	2.122
R-HSA-9931509	Expression of BMAL (ARNTL), CLOCK, and NPAS2	8.336065e-03	2.079
R-HSA-8856828	Clathrin-mediated endocytosis	8.504315e-03	2.070
R-HSA-9759475	Regulation of CDH11 Expression and Function	8.517789e-03	2.070
R-HSA-3134973	LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production	9.324654e-03	2.030
R-HSA-9931512	Phosphorylation of CLOCK, acetylation of BMAL1 (ARNTL) at target gene promoters	8.606351e-03	2.065
R-HSA-177929	Signaling by EGFR	8.804330e-03	2.055
R-HSA-169893	Prolonged ERK activation events	9.421091e-03	2.026
R-HSA-373753	Nephrin family interactions	9.481146e-03	2.023
R-HSA-418990	Adherens junctions interactions	8.715357e-03	2.060
R-HSA-166166	MyD88-independent TLR4 cascade	9.531739e-03	2.021
R-HSA-937061	TRIF (TICAM1)-mediated TLR4 signaling	9.531739e-03	2.021
R-HSA-9823730	Formation of definitive endoderm	9.481146e-03	2.023
R-HSA-196025	Formation of annular gap junctions	9.626169e-03	2.017
R-HSA-9663891	Selective autophagy	1.067904e-02	1.971
R-HSA-9932444	ATP-dependent chromatin remodelers	1.108493e-02	1.955
R-HSA-9932451	SWI/SNF chromatin remodelers	1.108493e-02	1.955
R-HSA-3214842	HDMs demethylate histones	1.108493e-02	1.955
R-HSA-201722	Formation of the beta-catenin:TCF transactivating complex	1.136565e-02	1.944
R-HSA-72187	mRNA 3'-end processing	1.150579e-02	1.939
R-HSA-209543	p75NTR recruits signalling complexes	1.152823e-02	1.938
R-HSA-9913351	Formation of the dystrophin-glycoprotein complex (DGC)	1.215409e-02	1.915
R-HSA-166016	Toll Like Receptor 4 (TLR4) Cascade	1.249021e-02	1.903
R-HSA-9705671	SARS-CoV-2 activates/modulates innate and adaptive immune responses	1.337856e-02	1.874
R-HSA-190873	Gap junction degradation	1.355922e-02	1.868
R-HSA-194138	Signaling by VEGF	1.403835e-02	1.853
R-HSA-5674499	Negative feedback regulation of MAPK pathway	1.455004e-02	1.837
R-HSA-5357956	TNFR1-induced NF-kappa-B signaling pathway	1.596537e-02	1.797
R-HSA-6802948	Signaling by high-kinase activity BRAF mutants	1.490503e-02	1.827
R-HSA-9927418	Developmental Lineage of Mammary Gland Luminal Epithelial Cells	1.510953e-02	1.821
R-HSA-168138	Toll Like Receptor 9 (TLR9) Cascade	1.601544e-02	1.795
R-HSA-8935964	RUNX1 regulates expression of components of tight junctions	1.455004e-02	1.837
R-HSA-6811442	Intra-Golgi and retrograde Golgi-to-ER traffic	1.592650e-02	1.798
R-HSA-8986944	Transcriptional Regulation by MECP2	1.434713e-02	1.843
R-HSA-9730414	MITF-M-regulated melanocyte development	1.555720e-02	1.808
R-HSA-73856	RNA Polymerase II Transcription Termination	1.626097e-02	1.789
R-HSA-168325	Viral Messenger RNA Synthesis	1.626097e-02	1.789
R-HSA-8878159	Transcriptional regulation by RUNX3	1.630087e-02	1.788
R-HSA-5693568	Resolution of D-loop Structures through Holliday Junction Intermediates	1.685297e-02	1.773
R-HSA-9930044	Nuclear RNA decay	1.685297e-02	1.773
R-HSA-9022692	Regulation of MECP2 expression and activity	1.685297e-02	1.773
R-HSA-2682334	EPH-Ephrin signaling	1.729960e-02	1.762
R-HSA-2559583	Cellular Senescence	1.746313e-02	1.758
R-HSA-5633007	Regulation of TP53 Activity	1.780969e-02	1.749
R-HSA-8875555	MET activates RAP1 and RAC1	1.845119e-02	1.734
R-HSA-9614657	FOXO-mediated transcription of cell death genes	1.876650e-02	1.727
R-HSA-1839117	Signaling by cytosolic FGFR1 fusion mutants	1.876650e-02	1.727
R-HSA-5607763	CLEC7A (Dectin-1) induces NFAT activation	1.934498e-02	1.713
R-HSA-9764562	Regulation of CDH1 mRNA translation by microRNAs	1.934498e-02	1.713
R-HSA-5693537	Resolution of D-Loop Structures	1.965150e-02	1.707
R-HSA-190828	Gap junction trafficking	1.976305e-02	1.704
R-HSA-6806003	Regulation of TP53 Expression and Degradation	1.988303e-02	1.702
R-HSA-9673013	Diseases of Telomere Maintenance	2.280931e-02	1.642
R-HSA-9670621	Defective Inhibition of DNA Recombination at Telomere	2.280931e-02	1.642
R-HSA-9006821	Alternative Lengthening of Telomeres (ALT)	2.280931e-02	1.642
R-HSA-211728	Regulation of PAK-2p34 activity by PS-GAP/RHG10	2.280931e-02	1.642
R-HSA-9670613	Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations	2.280931e-02	1.642
R-HSA-9699150	Defective DNA double strand break response due to BARD1 loss of function	2.280931e-02	1.642
R-HSA-9663199	Defective DNA double strand break response due to BRCA1 loss of function	2.280931e-02	1.642
R-HSA-9670615	Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations	2.280931e-02	1.642
R-HSA-5368598	Negative regulation of TCF-dependent signaling by DVL-interacting proteins	2.081726e-02	1.682
R-HSA-8875513	MET interacts with TNS proteins	2.081726e-02	1.682
R-HSA-72172	mRNA Splicing	2.149545e-02	1.668
R-HSA-9646399	Aggrephagy	2.278840e-02	1.642
R-HSA-168181	Toll Like Receptor 7/8 (TLR7/8) Cascade	2.181071e-02	1.661
R-HSA-448424	Interleukin-17 signaling	2.156368e-02	1.666
R-HSA-8878171	Transcriptional regulation by RUNX1	2.165178e-02	1.665
R-HSA-983231	Factors involved in megakaryocyte development and platelet production	2.001982e-02	1.699
R-HSA-9725370	Signaling by ALK fusions and activated point mutants	2.335613e-02	1.632
R-HSA-9700206	Signaling by ALK in cancer	2.335613e-02	1.632
R-HSA-2565942	Regulation of PLK1 Activity at G2/M Transition	2.341735e-02	1.630
R-HSA-168188	Toll Like Receptor TLR6:TLR2 Cascade	2.373812e-02	1.625
R-HSA-166058	MyD88:MAL(TIRAP) cascade initiated on plasma membrane	2.373812e-02	1.625
R-HSA-8875360	InlB-mediated entry of Listeria monocytogenes into host cell	2.435444e-02	1.613
R-HSA-399954	Sema3A PAK dependent Axon repulsion	2.435444e-02	1.613
R-HSA-8856688	Golgi-to-ER retrograde transport	2.557603e-02	1.592
R-HSA-68875	Mitotic Prophase	2.558022e-02	1.592
R-HSA-8951430	RUNX3 regulates WNT signaling	2.975534e-02	1.526
R-HSA-4411364	Binding of TCF/LEF:CTNNB1 to target gene promoters	2.975534e-02	1.526
R-HSA-389977	Post-chaperonin tubulin folding pathway	2.777398e-02	1.556
R-HSA-9934037	Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF)	2.777398e-02	1.556
R-HSA-5674135	MAP2K and MAPK activation	2.951001e-02	1.530
R-HSA-8854518	AURKA Activation by TPX2	2.782260e-02	1.556
R-HSA-5578749	Transcriptional regulation by small RNAs	2.632552e-02	1.580
R-HSA-72163	mRNA Splicing - Major Pathway	2.639107e-02	1.579
R-HSA-400685	Sema4D in semaphorin signaling	2.952012e-02	1.530
R-HSA-6806834	Signaling by MET	2.989512e-02	1.524
R-HSA-975155	MyD88 dependent cascade initiated on endosome	2.734101e-02	1.563
R-HSA-181438	Toll Like Receptor 2 (TLR2) Cascade	2.959176e-02	1.529
R-HSA-168179	Toll Like Receptor TLR1:TLR2 Cascade	2.959176e-02	1.529
R-HSA-5653656	Vesicle-mediated transport	2.568796e-02	1.590
R-HSA-187037	Signaling by NTRK1 (TRKA)	2.951267e-02	1.530
R-HSA-9022707	MECP2 regulates transcription factors	2.975534e-02	1.526
R-HSA-8853884	Transcriptional Regulation by VENTX	2.599237e-02	1.585
R-HSA-8853659	RET signaling	3.007462e-02	1.522
R-HSA-209560	NF-kB is activated and signals survival	3.141628e-02	1.503
R-HSA-975871	MyD88 cascade initiated on plasma membrane	3.147971e-02	1.502
R-HSA-168142	Toll Like Receptor 10 (TLR10) Cascade	3.147971e-02	1.502
R-HSA-168176	Toll Like Receptor 5 (TLR5) Cascade	3.147971e-02	1.502
R-HSA-5693571	Nonhomologous End-Joining (NHEJ)	3.214940e-02	1.493
R-HSA-1280215	Cytokine Signaling in Immune system	3.285574e-02	1.483
R-HSA-191650	Regulation of gap junction activity	3.309218e-02	1.480
R-HSA-165159	MTOR signalling	3.335562e-02	1.477
R-HSA-162909	Host Interactions of HIV factors	3.406407e-02	1.468
R-HSA-1483249	Inositol phosphate metabolism	3.426091e-02	1.465
R-HSA-525793	Myogenesis	3.454504e-02	1.462
R-HSA-1474165	Reproduction	3.619447e-02	1.441
R-HSA-421270	Cell-cell junction organization	3.656839e-02	1.437
R-HSA-5693538	Homology Directed Repair	3.669985e-02	1.435
R-HSA-75893	TNF signaling	3.800319e-02	1.420
R-HSA-446107	Type I hemidesmosome assembly	3.989691e-02	1.399
R-HSA-444257	RSK activation	3.989691e-02	1.399
R-HSA-8875656	MET receptor recycling	3.989691e-02	1.399
R-HSA-9768778	Regulation of NPAS4 mRNA translation	3.989691e-02	1.399
R-HSA-9617629	Regulation of FOXO transcriptional activity by acetylation	3.960185e-02	1.402
R-HSA-4641265	Repression of WNT target genes	3.960185e-02	1.402
R-HSA-8941856	RUNX3 regulates NOTCH signaling	3.960185e-02	1.402
R-HSA-372708	p130Cas linkage to MAPK signaling for integrins	4.433034e-02	1.353
R-HSA-176187	Activation of ATR in response to replication stress	3.983304e-02	1.400
R-HSA-380284	Loss of proteins required for interphase microtubule organization from the centr...	3.957490e-02	1.403
R-HSA-380259	Loss of Nlp from mitotic centrosomes	3.957490e-02	1.403
R-HSA-9764560	Regulation of CDH1 Gene Transcription	4.075638e-02	1.390
R-HSA-8864260	Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors	4.208344e-02	1.376
R-HSA-1500620	Meiosis	4.577465e-02	1.339
R-HSA-975138	TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation	4.263661e-02	1.370
R-HSA-6807878	COPI-mediated anterograde transport	4.607527e-02	1.337
R-HSA-8953854	Metabolism of RNA	4.330845e-02	1.363
R-HSA-9768759	Regulation of NPAS4 gene expression	4.433034e-02	1.353
R-HSA-373752	Netrin-1 signaling	4.208344e-02	1.376
R-HSA-1834949	Cytosolic sensors of pathogen-associated DNA	4.075638e-02	1.390
R-HSA-2995383	Initiation of Nuclear Envelope (NE) Reformation	3.933642e-02	1.405
R-HSA-9825895	Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ...	3.989691e-02	1.399
R-HSA-69273	Cyclin A/B1/B2 associated events during G2/M transition	3.983304e-02	1.400
R-HSA-6804115	TP53 regulates transcription of additional cell cycle genes whose exact role in ...	4.614368e-02	1.336
R-HSA-176034	Interactions of Tat with host cellular proteins	4.761798e-02	1.322
R-HSA-352238	Breakdown of the nuclear lamina	4.761798e-02	1.322
R-HSA-1257604	PIP3 activates AKT signaling	4.806253e-02	1.318
R-HSA-110381	Resolution of AP sites via the single-nucleotide replacement pathway	4.836853e-02	1.315
R-HSA-8941284	RUNX2 regulates chondrocyte maturation	4.836853e-02	1.315
R-HSA-426496	Post-transcriptional silencing by small RNAs	4.836853e-02	1.315
R-HSA-5685939	HDR through MMEJ (alt-NHEJ)	4.896984e-02	1.310
R-HSA-9796292	Formation of axial mesoderm	4.896984e-02	1.310
R-HSA-170968	Frs2-mediated activation	4.896984e-02	1.310
R-HSA-9634815	Transcriptional Regulation by NPAS4	4.929597e-02	1.307
R-HSA-9006925	Intracellular signaling by second messengers	4.976165e-02	1.303
R-HSA-168898	Toll-like Receptor Cascades	5.000274e-02	1.301
R-HSA-5357801	Programmed Cell Death	5.013726e-02	1.300
R-HSA-166520	Signaling by NTRKs	5.098648e-02	1.293
R-HSA-428543	Inactivation of CDC42 and RAC1	5.177068e-02	1.286
R-HSA-430116	GP1b-IX-V activation signalling	5.177068e-02	1.286
R-HSA-176974	Unwinding of DNA	5.177068e-02	1.286
R-HSA-2025928	Calcineurin activates NFAT	5.177068e-02	1.286
R-HSA-198693	AKT phosphorylates targets in the nucleus	5.177068e-02	1.286
R-HSA-6802946	Signaling by moderate kinase activity BRAF mutants	5.227075e-02	1.282
R-HSA-6802955	Paradoxical activation of RAF signaling by kinase inactive BRAF	5.227075e-02	1.282
R-HSA-9649948	Signaling downstream of RAS mutants	5.227075e-02	1.282
R-HSA-6802949	Signaling by RAS mutants	5.227075e-02	1.282
R-HSA-1606322	ZBP1(DAI) mediated induction of type I IFNs	5.274181e-02	1.278
R-HSA-4419969	Depolymerization of the Nuclear Lamina	5.274181e-02	1.278
R-HSA-74160	Gene expression (Transcription)	5.283841e-02	1.277
R-HSA-9833482	PKR-mediated signaling	5.337848e-02	1.273
R-HSA-1221632	Meiotic synapsis	5.440441e-02	1.264
R-HSA-162599	Late Phase of HIV Life Cycle	5.505499e-02	1.259
R-HSA-1266738	Developmental Biology	5.553340e-02	1.255
R-HSA-162587	HIV Life Cycle	5.593126e-02	1.252
R-HSA-5685942	HDR through Homologous Recombination (HRR)	5.690136e-02	1.245
R-HSA-9833576	CDH11 homotypic and heterotypic interactions	6.649345e-02	1.177
R-HSA-5603029	IkBA variant leads to EDA-ID	6.649345e-02	1.177
R-HSA-2032785	YAP1- and WWTR1 (TAZ)-stimulated gene expression	5.953455e-02	1.225
R-HSA-3270619	IRF3-mediated induction of type I IFN	7.129415e-02	1.147
R-HSA-9709603	Impaired BRCA2 binding to PALB2	6.205959e-02	1.207
R-HSA-1362277	Transcription of E2F targets under negative control by DREAM complex	7.228826e-02	1.141
R-HSA-6807004	Negative regulation of MET activity	7.228826e-02	1.141
R-HSA-9701193	Defective homologous recombination repair (HRR) due to PALB2 loss of function	7.228826e-02	1.141
R-HSA-9701192	Defective homologous recombination repair (HRR) due to BRCA1 loss of function	7.228826e-02	1.141
R-HSA-9704646	Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of...	7.228826e-02	1.141
R-HSA-9704331	Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of...	7.228826e-02	1.141
R-HSA-429947	Deadenylation of mRNA	6.190191e-02	1.208
R-HSA-389960	Formation of tubulin folding intermediates by CCT/TriC	6.190191e-02	1.208
R-HSA-380972	Energy dependent regulation of mTOR by LKB1-AMPK	6.031226e-02	1.220
R-HSA-182971	EGFR downregulation	6.824108e-02	1.166
R-HSA-389958	Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding	6.824108e-02	1.166
R-HSA-8941326	RUNX2 regulates bone development	6.500671e-02	1.187
R-HSA-9656223	Signaling by RAF1 mutants	6.150762e-02	1.211
R-HSA-186763	Downstream signal transduction	6.824108e-02	1.166
R-HSA-5693567	HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA)	6.381725e-02	1.195
R-HSA-6804757	Regulation of TP53 Degradation	6.500671e-02	1.187
R-HSA-9909396	Circadian clock	6.428223e-02	1.192
R-HSA-416572	Sema4D induced cell migration and growth-cone collapse	7.228826e-02	1.141
R-HSA-201681	TCF dependent signaling in response to WNT	7.084823e-02	1.150
R-HSA-9762292	Regulation of CDH11 function	6.536008e-02	1.185
R-HSA-6811440	Retrograde transport at the Trans-Golgi-Network	5.793622e-02	1.237
R-HSA-1810476	RIP-mediated NFkB activation via ZBP1	7.129415e-02	1.147
R-HSA-392517	Rap1 signalling	6.205959e-02	1.207
R-HSA-5655302	Signaling by FGFR1 in disease	6.150762e-02	1.211
R-HSA-446388	Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen...	6.649345e-02	1.177
R-HSA-8863678	Neurodegenerative Diseases	6.190191e-02	1.208
R-HSA-8862803	Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis...	6.190191e-02	1.208
R-HSA-9707616	Heme signaling	6.670264e-02	1.176
R-HSA-9705683	SARS-CoV-2-host interactions	7.208577e-02	1.142
R-HSA-2219528	PI3K/AKT Signaling in Cancer	5.900443e-02	1.229
R-HSA-9609736	Assembly and cell surface presentation of NMDA receptors	6.150762e-02	1.211
R-HSA-3000171	Non-integrin membrane-ECM interactions	6.232246e-02	1.205
R-HSA-73894	DNA Repair	7.241297e-02	1.140
R-HSA-8854214	TBC/RABGAPs	7.547200e-02	1.122
R-HSA-1538133	G0 and Early G1	7.678022e-02	1.115
R-HSA-4791275	Signaling by WNT in cancer	7.678022e-02	1.115
R-HSA-6794362	Protein-protein interactions at synapses	7.778131e-02	1.109
R-HSA-446343	Localization of the PINCH-ILK-PARVIN complex to focal adhesions	7.860630e-02	1.105
R-HSA-8985801	Regulation of cortical dendrite branching	7.860630e-02	1.105
R-HSA-6804754	Regulation of TP53 Expression	7.860630e-02	1.105
R-HSA-8856825	Cargo recognition for clathrin-mediated endocytosis	7.970195e-02	1.099
R-HSA-9615933	Postmitotic nuclear pore complex (NPC) reformation	8.057726e-02	1.094
R-HSA-210990	PECAM1 interactions	8.061670e-02	1.094
R-HSA-9614399	Regulation of localization of FOXO transcription factors	8.061670e-02	1.094
R-HSA-8876493	InlA-mediated entry of Listeria monocytogenes into host cells	8.061670e-02	1.094
R-HSA-9759811	Regulation of CDH11 mRNA translation by microRNAs	8.061670e-02	1.094
R-HSA-8875878	MET promotes cell motility	8.067342e-02	1.093
R-HSA-5357786	TNFR1-induced proapoptotic signaling	8.342363e-02	1.079
R-HSA-450321	JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ...	8.342363e-02	1.079
R-HSA-399955	SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion	8.423154e-02	1.075
R-HSA-388844	Receptor-type tyrosine-protein phosphatases	8.423154e-02	1.075
R-HSA-5688426	Deubiquitination	8.460938e-02	1.073
R-HSA-442742	CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling	8.593092e-02	1.066
R-HSA-354192	Integrin signaling	8.593092e-02	1.066
R-HSA-8939243	RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno...	8.593092e-02	1.066
R-HSA-9674415	Drug resistance of PDGFR mutants	1.088670e-01	0.963
R-HSA-9674428	PDGFR mutants bind TKIs	1.088670e-01	0.963
R-HSA-9674403	Regorafenib-resistant PDGFR mutants	1.088670e-01	0.963
R-HSA-5467333	APC truncation mutants are not K63 polyubiquitinated	1.088670e-01	0.963
R-HSA-9674396	Imatinib-resistant PDGFR mutants	1.088670e-01	0.963
R-HSA-5467343	Deletions in the AMER1 gene destabilize the destruction complex	1.088670e-01	0.963
R-HSA-9674401	Sunitinib-resistant PDGFR mutants	1.088670e-01	0.963
R-HSA-9674404	Sorafenib-resistant PDGFR mutants	1.088670e-01	0.963
R-HSA-8865999	MET activates PTPN11	1.141361e-01	0.943
R-HSA-8951671	RUNX3 regulates YAP1-mediated transcription	8.724162e-02	1.059
R-HSA-110357	Displacement of DNA glycosylase by APEX1	1.103404e-01	0.957
R-HSA-8949275	RUNX3 Regulates Immune Response and Cell Migration	1.103404e-01	0.957
R-HSA-9013973	TICAM1-dependent activation of IRF3/IRF7	9.746491e-02	1.011
R-HSA-381183	ATF6 (ATF6-alpha) activates chaperone genes	9.746491e-02	1.011
R-HSA-428540	Activation of RAC1	9.746491e-02	1.011
R-HSA-4839748	Signaling by AMER1 mutants	9.746491e-02	1.011
R-HSA-5339716	Signaling by GSK3beta mutants	9.746491e-02	1.011
R-HSA-174437	Removal of the Flap Intermediate from the C-strand	1.135025e-01	0.945
R-HSA-350054	Notch-HLH transcription pathway	1.083563e-01	0.965
R-HSA-8940973	RUNX2 regulates osteoblast differentiation	1.021636e-01	0.991
R-HSA-5696394	DNA Damage Recognition in GG-NER	9.569073e-02	1.019
R-HSA-9615710	Late endosomal microautophagy	1.140232e-01	0.943
R-HSA-9709570	Impaired BRCA2 binding to RAD51	1.140232e-01	0.943
R-HSA-112382	Formation of RNA Pol II elongation complex	9.223631e-02	1.035
R-HSA-75955	RNA Polymerase II Transcription Elongation	1.003119e-01	0.999
R-HSA-380270	Recruitment of mitotic centrosome proteins and complexes	9.150887e-02	1.039
R-HSA-380287	Centrosome maturation	1.054515e-01	0.977
R-HSA-5620912	Anchoring of the basal body to the plasma membrane	1.154644e-01	0.938
R-HSA-5693565	Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at...	9.248462e-02	1.034
R-HSA-9609690	HCMV Early Events	9.079062e-02	1.042
R-HSA-4641262	Disassembly of the destruction complex and recruitment of AXIN to the membrane	9.101031e-02	1.041
R-HSA-69481	G2/M Checkpoints	1.047716e-01	0.980
R-HSA-166208	mTORC1-mediated signalling	1.083563e-01	0.965
R-HSA-168638	NOD1/2 Signaling Pathway	1.060535e-01	0.974
R-HSA-3214847	HATs acetylate histones	9.199716e-02	1.036
R-HSA-199977	ER to Golgi Anterograde Transport	1.063848e-01	0.973
R-HSA-190861	Gap junction assembly	1.060535e-01	0.974
R-HSA-9006934	Signaling by Receptor Tyrosine Kinases	8.856427e-02	1.053
R-HSA-8953750	Transcriptional Regulation by E2F6	8.929254e-02	1.049
R-HSA-9854907	Regulation of MITF-M dependent genes involved in metabolism	1.141361e-01	0.943
R-HSA-5357905	Regulation of TNFR1 signaling	9.984418e-02	1.001
R-HSA-9734009	Defective Intrinsic Pathway for Apoptosis	9.101031e-02	1.041
R-HSA-211000	Gene Silencing by RNA	1.014278e-01	0.994
R-HSA-450282	MAPK targets/ Nuclear events mediated by MAP kinases	1.140232e-01	0.943
R-HSA-9824585	Regulation of MITF-M-dependent genes involved in pigmentation	9.126232e-02	1.040
R-HSA-9839373	Signaling by TGFBR3	9.984418e-02	1.001
R-HSA-70171	Glycolysis	9.780270e-02	1.010
R-HSA-4839743	Signaling by CTNNB1 phospho-site mutants	1.158067e-01	0.936
R-HSA-5358749	CTNNB1 S37 mutants aren't phosphorylated	1.158067e-01	0.936
R-HSA-5358752	CTNNB1 T41 mutants aren't phosphorylated	1.158067e-01	0.936
R-HSA-5358751	CTNNB1 S45 mutants aren't phosphorylated	1.158067e-01	0.936
R-HSA-5358747	CTNNB1 S33 mutants aren't phosphorylated	1.158067e-01	0.936
R-HSA-198323	AKT phosphorylates targets in the cytosol	1.158067e-01	0.936
R-HSA-5693616	Presynaptic phase of homologous DNA pairing and strand exchange	1.170096e-01	0.932
R-HSA-187687	Signalling to ERKs	1.170096e-01	0.932
R-HSA-5696399	Global Genome Nucleotide Excision Repair (GG-NER)	1.180821e-01	0.928
R-HSA-9816359	Maternal to zygotic transition (MZT)	1.194639e-01	0.923
R-HSA-5607764	CLEC7A (Dectin-1) signaling	1.196116e-01	0.922
R-HSA-389957	Prefoldin mediated transfer of substrate to CCT/TriC	1.221052e-01	0.913
R-HSA-9634638	Estrogen-dependent nuclear events downstream of ESR-membrane signaling	1.221052e-01	0.913
R-HSA-9018519	Estrogen-dependent gene expression	1.242203e-01	0.906
R-HSA-195721	Signaling by WNT	1.279671e-01	0.893
R-HSA-9766229	Degradation of CDH1	1.282977e-01	0.892
R-HSA-162906	HIV Infection	1.287558e-01	0.890
R-HSA-180292	GAB1 signalosome	1.297375e-01	0.887
R-HSA-156711	Polo-like kinase mediated events	1.297375e-01	0.887
R-HSA-9613829	Chaperone Mediated Autophagy	1.297375e-01	0.887
R-HSA-9856649	Transcriptional and post-translational regulation of MITF-M expression and activ...	1.314926e-01	0.881
R-HSA-5620920	Cargo trafficking to the periciliary membrane	1.314926e-01	0.881
R-HSA-73857	RNA Polymerase II Transcription	1.326604e-01	0.877
R-HSA-9006936	Signaling by TGFB family members	1.354145e-01	0.868
R-HSA-8939246	RUNX1 regulates transcription of genes involved in differentiation of myeloid ce...	1.354897e-01	0.868
R-HSA-390696	Adrenoceptors	1.354897e-01	0.868
R-HSA-381033	ATF6 (ATF6-alpha) activates chaperones	1.355262e-01	0.868
R-HSA-2559584	Formation of Senescence-Associated Heterochromatin Foci (SAHF)	1.355262e-01	0.868
R-HSA-9933947	Formation of the non-canonical BAF (ncBAF) complex	1.355262e-01	0.868
R-HSA-110314	Recognition of DNA damage by PCNA-containing replication complex	1.366654e-01	0.864
R-HSA-6804756	Regulation of TP53 Activity through Phosphorylation	1.416602e-01	0.849
R-HSA-912631	Regulation of signaling by CBL	1.469560e-01	0.833
R-HSA-881907	Gastrin-CREB signalling pathway via PKC and MAPK	1.469560e-01	0.833
R-HSA-1834941	STING mediated induction of host immune responses	1.469560e-01	0.833
R-HSA-4086398	Ca2+ pathway	1.494740e-01	0.825
R-HSA-5693554	Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD...	1.519962e-01	0.818
R-HSA-8941333	RUNX2 regulates genes involved in differentiation of myeloid cells	1.528525e-01	0.816
R-HSA-1251932	PLCG1 events in ERBB2 signaling	1.528525e-01	0.816
R-HSA-165181	Inhibition of TSC complex formation by PKB	1.528525e-01	0.816
R-HSA-9652169	Signaling by MAP2K mutants	1.528525e-01	0.816
R-HSA-9705677	SARS-CoV-2 targets PDZ proteins in cell-cell junction	1.528525e-01	0.816
R-HSA-5693579	Homologous DNA Pairing and Strand Exchange	1.532909e-01	0.814
R-HSA-9909649	Regulation of PD-L1(CD274) transcription	1.533403e-01	0.814
R-HSA-69190	DNA strand elongation	1.536300e-01	0.814
R-HSA-5684264	MAP3K8 (TPL2)-dependent MAPK1/3 activation	1.564942e-01	0.806
R-HSA-399956	CRMPs in Sema3A signaling	1.564942e-01	0.806
R-HSA-9933937	Formation of the canonical BAF (cBAF) complex	1.564942e-01	0.806
R-HSA-1433559	Regulation of KIT signaling	1.564942e-01	0.806
R-HSA-9734091	Drug-mediated inhibition of MET activation	2.058877e-01	0.686
R-HSA-5602566	TICAM1 deficiency - HSE	2.058877e-01	0.686
R-HSA-9763198	Impaired BRCA2 binding to SEM1 (DSS1)	2.058877e-01	0.686
R-HSA-5632968	Defective Mismatch Repair Associated With MSH6	2.058877e-01	0.686
R-HSA-9709275	Impaired BRCA2 translocation to the nucleus	2.058877e-01	0.686
R-HSA-74713	IRS activation	1.936414e-01	0.713
R-HSA-9818032	NFE2L2 regulating MDR associated enzymes	1.623770e-01	0.789
R-HSA-170984	ARMS-mediated activation	1.623770e-01	0.789
R-HSA-9613354	Lipophagy	1.623770e-01	0.789
R-HSA-8941855	RUNX3 regulates CDKN1A transcription	2.355932e-01	0.628
R-HSA-5635851	GLI proteins bind promoters of Hh responsive genes to promote transcription	2.355932e-01	0.628
R-HSA-68689	CDC6 association with the ORC:origin complex	2.355932e-01	0.628
R-HSA-8985586	SLIT2:ROBO1 increases RHOA activity	2.355932e-01	0.628
R-HSA-5340588	Signaling by RNF43 mutants	2.355932e-01	0.628
R-HSA-9014325	TICAM1,TRAF6-dependent induction of TAK1 complex	1.906893e-01	0.720
R-HSA-4839744	Signaling by APC mutants	2.201216e-01	0.657
R-HSA-5467348	Truncations of AMER1 destabilize the destruction complex	2.201216e-01	0.657
R-HSA-5467337	APC truncation mutants have impaired AXIN binding	2.201216e-01	0.657
R-HSA-5467340	AXIN missense mutants destabilize the destruction complex	2.201216e-01	0.657
R-HSA-8948700	Competing endogenous RNAs (ceRNAs) regulate PTEN translation	1.785719e-01	0.748
R-HSA-196299	Beta-catenin phosphorylation cascade	1.785719e-01	0.748
R-HSA-168927	TICAM1, RIP1-mediated IKK complex recruitment	1.785719e-01	0.748
R-HSA-354194	GRB2:SOS provides linkage to MAPK signaling for Integrins	2.016150e-01	0.695
R-HSA-9687136	Aberrant regulation of mitotic exit in cancer due to RB1 defects	2.016150e-01	0.695
R-HSA-936964	Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE)	2.254761e-01	0.647
R-HSA-918233	TRAF3-dependent IRF activation pathway	2.254761e-01	0.647
R-HSA-141430	Inactivation of APC/C via direct inhibition of the APC/C complex	2.254761e-01	0.647
R-HSA-5696397	Gap-filling DNA repair synthesis and ligation in GG-NER	2.037588e-01	0.691
R-HSA-174414	Processive synthesis on the C-strand of the telomere	1.847816e-01	0.733
R-HSA-445095	Interaction between L1 and Ankyrins	1.847816e-01	0.733
R-HSA-390522	Striated Muscle Contraction	1.831088e-01	0.737
R-HSA-5673000	RAF activation	1.986672e-01	0.702
R-HSA-9675136	Diseases of DNA Double-Strand Break Repair	1.986672e-01	0.702
R-HSA-9701190	Defective homologous recombination repair (HRR) due to BRCA2 loss of function	1.986672e-01	0.702
R-HSA-9764725	Negative Regulation of CDH1 Gene Transcription	1.678871e-01	0.775
R-HSA-5693606	DNA Double Strand Break Response	1.634206e-01	0.787
R-HSA-195253	Degradation of beta-catenin by the destruction complex	1.955617e-01	0.709
R-HSA-8866910	TFAP2 (AP-2) family regulates transcription of growth factors and their receptor...	2.254761e-01	0.647
R-HSA-5693607	Processing of DNA double-strand break ends	2.330211e-01	0.633
R-HSA-9617828	FOXO-mediated transcription of cell cycle genes	2.037588e-01	0.691
R-HSA-5620916	VxPx cargo-targeting to cilium	1.650857e-01	0.782
R-HSA-3928665	EPH-ephrin mediated repulsion of cells	1.893612e-01	0.723
R-HSA-8866654	E3 ubiquitin ligases ubiquitinate target proteins	1.606528e-01	0.794
R-HSA-5685938	HDR through Single Strand Annealing (SSA)	1.680839e-01	0.774
R-HSA-77595	Processing of Intronless Pre-mRNAs	2.254761e-01	0.647
R-HSA-2559585	Oncogene Induced Senescence	2.147193e-01	0.668
R-HSA-450531	Regulation of mRNA stability by proteins that bind AU-rich elements	2.184570e-01	0.661
R-HSA-674695	RNA Polymerase II Pre-transcription Events	1.589299e-01	0.799
R-HSA-5610787	Hedgehog 'off' state	2.177795e-01	0.662
R-HSA-8934593	Regulation of RUNX1 Expression and Activity	1.680517e-01	0.775
R-HSA-445144	Signal transduction by L1	1.650857e-01	0.782
R-HSA-2122947	NOTCH1 Intracellular Domain Regulates Transcription	2.164686e-01	0.665
R-HSA-1980143	Signaling by NOTCH1	1.787356e-01	0.748
R-HSA-5260271	Diseases of Immune System	1.801223e-01	0.744
R-HSA-5602358	Diseases associated with the TLR signaling cascade	1.801223e-01	0.744
R-HSA-73933	Resolution of Abasic Sites (AP sites)	1.942571e-01	0.712
R-HSA-9860276	SLC15A4:TASL-dependent IRF5 activation	2.355932e-01	0.628
R-HSA-141405	Inhibition of the proteolytic activity of APC/C required for the onset of anapha...	2.254761e-01	0.647
R-HSA-5689603	UCH proteinases	1.787356e-01	0.748
R-HSA-9609646	HCMV Infection	2.109385e-01	0.676
R-HSA-9860927	Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ...	2.147193e-01	0.668
R-HSA-6811436	COPI-independent Golgi-to-ER retrograde traffic	1.965826e-01	0.706
R-HSA-1839124	FGFR1 mutant receptor activation	1.680839e-01	0.774
R-HSA-9007101	Rab regulation of trafficking	1.867190e-01	0.729
R-HSA-9855142	Cellular responses to mechanical stimuli	2.112859e-01	0.675
R-HSA-9758941	Gastrulation	1.640538e-01	0.785
R-HSA-9733709	Cardiogenesis	1.680839e-01	0.774
R-HSA-5683057	MAPK family signaling cascades	2.067533e-01	0.685
R-HSA-77042	Formation of editosomes by ADAR proteins	2.058877e-01	0.686
R-HSA-169131	Inhibition of PKR	2.058877e-01	0.686
R-HSA-425381	Bicarbonate transporters	2.201216e-01	0.657
R-HSA-9706369	Negative regulation of FLT3	2.016150e-01	0.695
R-HSA-6804758	Regulation of TP53 Activity through Acetylation	1.680839e-01	0.774
R-HSA-198725	Nuclear Events (kinase and transcription factor activation)	2.184570e-01	0.661
R-HSA-69242	S Phase	1.573563e-01	0.803
R-HSA-198753	ERK/MAPK targets	1.840479e-01	0.735
R-HSA-2173788	Downregulation of TGF-beta receptor signaling	2.241317e-01	0.649
R-HSA-389356	Co-stimulation by CD28	2.027268e-01	0.693
R-HSA-9607240	FLT3 Signaling	1.942571e-01	0.712
R-HSA-8939247	RUNX1 regulates transcription of genes involved in interleukin signaling	1.936414e-01	0.713
R-HSA-9758919	Epithelial-Mesenchymal Transition (EMT) during gastrulation	2.355932e-01	0.628
R-HSA-8943724	Regulation of PTEN gene transcription	1.678871e-01	0.775
R-HSA-512988	Interleukin-3, Interleukin-5 and GM-CSF signaling	2.238191e-01	0.650
R-HSA-168643	Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali...	2.144089e-01	0.669
R-HSA-210745	Regulation of gene expression in beta cells	2.200450e-01	0.657
R-HSA-447038	NrCAM interactions	1.936414e-01	0.713
R-HSA-9825892	Regulation of MITF-M-dependent genes involved in cell cycle and proliferation	2.037588e-01	0.691
R-HSA-163765	ChREBP activates metabolic gene expression	2.201216e-01	0.657
R-HSA-9668328	Sealing of the nuclear envelope (NE) by ESCRT-III	1.680839e-01	0.774
R-HSA-9029569	NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu...	2.356346e-01	0.628
R-HSA-5617833	Cilium Assembly	2.367414e-01	0.626
R-HSA-68962	Activation of the pre-replicative complex	2.384620e-01	0.623
R-HSA-877300	Interferon gamma signaling	2.390652e-01	0.621
R-HSA-69473	G2/M DNA damage checkpoint	2.424021e-01	0.615
R-HSA-429914	Deadenylation-dependent mRNA decay	2.492530e-01	0.603
R-HSA-176407	Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase	2.500083e-01	0.602
R-HSA-5637812	Signaling by EGFRvIII in Cancer	2.500083e-01	0.602
R-HSA-5637810	Constitutive Signaling by EGFRvIII	2.500083e-01	0.602
R-HSA-5358565	Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)	2.500083e-01	0.602
R-HSA-5210891	Uptake and function of anthrax toxins	2.500083e-01	0.602
R-HSA-9818028	NFE2L2 regulates pentose phosphate pathway genes	2.503831e-01	0.601
R-HSA-4839735	Signaling by AXIN mutants	2.503831e-01	0.601
R-HSA-8852135	Protein ubiquitination	2.547312e-01	0.594
R-HSA-205017	NFG and proNGF binds to p75NTR	2.923504e-01	0.534
R-HSA-73930	Abasic sugar-phosphate removal via the single-nucleotide replacement pathway	2.923504e-01	0.534
R-HSA-5339700	Signaling by TCF7L2 mutants	2.923504e-01	0.534
R-HSA-5602571	TRAF3 deficiency - HSE	2.923504e-01	0.534
R-HSA-5609974	Defective PGM1 causes PGM1-CDG	2.923504e-01	0.534
R-HSA-5619111	Defective SLC20A2 causes idiopathic basal ganglia calcification 1 (IBGC1)	2.923504e-01	0.534
R-HSA-5603027	IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (E...	2.923504e-01	0.534
R-HSA-3560792	Defective SLC26A2 causes chondrodysplasias	2.923504e-01	0.534
R-HSA-5602636	IKBKB deficiency causes SCID	2.923504e-01	0.534
R-HSA-5619109	Defective SLC6A2 causes orthostatic intolerance (OI)	2.923504e-01	0.534
R-HSA-5619050	Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tu...	2.923504e-01	0.534
R-HSA-9665230	Drug resistance in ERBB2 KD mutants	3.694037e-01	0.432
R-HSA-211736	Stimulation of the cell death response by PAK-2p34	3.694037e-01	0.432
R-HSA-9652282	Drug-mediated inhibition of ERBB2 signaling	3.694037e-01	0.432
R-HSA-8854521	Interaction between PHLDA1 and AURKA	3.694037e-01	0.432
R-HSA-8951911	RUNX3 regulates RUNX1-mediated transcription	3.694037e-01	0.432
R-HSA-9665249	Resistance of ERBB2 KD mutants to afatinib	3.694037e-01	0.432
R-HSA-9665245	Resistance of ERBB2 KD mutants to tesevatinib	3.694037e-01	0.432
R-HSA-9665251	Resistance of ERBB2 KD mutants to lapatinib	3.694037e-01	0.432
R-HSA-9665246	Resistance of ERBB2 KD mutants to neratinib	3.694037e-01	0.432
R-HSA-9665737	Drug resistance in ERBB2 TMD/JMD mutants	3.694037e-01	0.432
R-HSA-3828062	Glycogen storage disease type 0 (muscle GYS1)	3.694037e-01	0.432
R-HSA-3814836	Glycogen storage disease type XV (GYG1)	3.694037e-01	0.432
R-HSA-9665244	Resistance of ERBB2 KD mutants to sapitinib	3.694037e-01	0.432
R-HSA-5619089	Defective SLC6A5 causes hyperekplexia 3 (HKPX3)	3.694037e-01	0.432
R-HSA-9665247	Resistance of ERBB2 KD mutants to osimertinib	3.694037e-01	0.432
R-HSA-9665233	Resistance of ERBB2 KD mutants to trastuzumab	3.694037e-01	0.432
R-HSA-9665250	Resistance of ERBB2 KD mutants to AEE788	3.694037e-01	0.432
R-HSA-113507	E2F-enabled inhibition of pre-replication complex formation	2.779719e-01	0.556
R-HSA-6802953	RAS signaling downstream of NF1 loss-of-function variants	2.779719e-01	0.556
R-HSA-9912481	Branched-chain ketoacid dehydrogenase kinase deficiency	2.779719e-01	0.556
R-HSA-8851907	MET activates PI3K/AKT signaling	3.201876e-01	0.495
R-HSA-112412	SOS-mediated signalling	3.201876e-01	0.495
R-HSA-9726840	SHOC2 M1731 mutant abolishes MRAS complex function	3.201876e-01	0.495
R-HSA-167021	PLC-gamma1 signalling	4.380709e-01	0.358
R-HSA-9034793	Activated NTRK3 signals through PLCG1	4.380709e-01	0.358
R-HSA-111446	Activation of BIM and translocation to mitochondria	4.380709e-01	0.358
R-HSA-8866906	TFAP2 (AP-2) family regulates transcription of other transcription factors	4.380709e-01	0.358
R-HSA-209563	Axonal growth stimulation	4.380709e-01	0.358
R-HSA-9673766	Signaling by cytosolic PDGFRA and PDGFRB fusion proteins	4.380709e-01	0.358
R-HSA-9944971	Loss of Function of KMT2D in Kabuki Syndrome	4.380709e-01	0.358
R-HSA-8941237	Invadopodia formation	4.380709e-01	0.358
R-HSA-9944997	Loss of Function of KMT2D in MLL4 Complex Formation in Kabuki Syndrome	4.380709e-01	0.358
R-HSA-5603037	IRAK4 deficiency (TLR5)	4.380709e-01	0.358
R-HSA-5660862	Defective SLC7A7 causes lysinuric protein intolerance (LPI)	4.380709e-01	0.358
R-HSA-8851805	MET activates RAS signaling	2.812016e-01	0.551
R-HSA-9027276	Erythropoietin activates Phosphoinositide-3-kinase (PI3K)	2.812016e-01	0.551
R-HSA-975144	IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation	2.812016e-01	0.551
R-HSA-9931530	Phosphorylation and nuclear translocation of the CRY:PER:kinase complex	2.812016e-01	0.551
R-HSA-937039	IRAK1 recruits IKK complex	2.812016e-01	0.551
R-HSA-9820865	Z-decay: degradation of maternal mRNAs by zygotically expressed factors	2.812016e-01	0.551
R-HSA-164940	Nef mediated downregulation of MHC class I complex cell surface expression	3.617737e-01	0.442
R-HSA-9828211	Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation	3.617737e-01	0.442
R-HSA-212718	EGFR interacts with phospholipase C-gamma	3.617737e-01	0.442
R-HSA-9660537	Signaling by MRAS-complex mutants	3.617737e-01	0.442
R-HSA-9726842	Gain-of-function MRAS complexes activate RAF signaling	3.617737e-01	0.442
R-HSA-9665348	Signaling by ERBB2 ECD mutants	2.750670e-01	0.561
R-HSA-5651801	PCNA-Dependent Long Patch Base Excision Repair	2.750670e-01	0.561
R-HSA-937041	IKK complex recruitment mediated by RIP1	3.005119e-01	0.522
R-HSA-69166	Removal of the Flap Intermediate	3.435297e-01	0.464
R-HSA-193692	Regulated proteolysis of p75NTR	4.023671e-01	0.395
R-HSA-201688	WNT mediated activation of DVL	4.023671e-01	0.395
R-HSA-9026527	Activated NTRK2 signals through PLCG1	4.992644e-01	0.302
R-HSA-205025	NADE modulates death signalling	4.992644e-01	0.302
R-HSA-9013957	TLR3-mediated TICAM1-dependent programmed cell death	4.992644e-01	0.302
R-HSA-211163	AKT-mediated inactivation of FOXO1A	4.992644e-01	0.302
R-HSA-9818035	NFE2L2 regulating ER-stress associated genes	4.992644e-01	0.302
R-HSA-174411	Polymerase switching on the C-strand of the telomere	2.883277e-01	0.540
R-HSA-9909620	Regulation of PD-L1(CD274) translation	3.262086e-01	0.487
R-HSA-937072	TRAF6-mediated induction of TAK1 complex within TLR4 complex	3.746075e-01	0.426
R-HSA-450385	Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA	3.746075e-01	0.426
R-HSA-450513	Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA	3.746075e-01	0.426
R-HSA-210991	Basigin interactions	3.520301e-01	0.453
R-HSA-179409	APC-Cdc20 mediated degradation of Nek2A	3.520301e-01	0.453
R-HSA-9027277	Erythropoietin activates Phospholipase C gamma (PLCG)	4.416910e-01	0.355
R-HSA-451308	Activation of Ca-permeable Kainate Receptor	4.416910e-01	0.355
R-HSA-5140745	WNT5A-dependent internalization of FZD2, FZD5 and ROR2	4.416910e-01	0.355
R-HSA-1362300	Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL...	4.053794e-01	0.392
R-HSA-176412	Phosphorylation of the APC/C	4.053794e-01	0.392
R-HSA-5603041	IRAK4 deficiency (TLR2/4)	3.778572e-01	0.423
R-HSA-167287	HIV elongation arrest and recovery	3.552816e-01	0.449
R-HSA-167290	Pausing and recovery of HIV elongation	3.552816e-01	0.449
R-HSA-9927426	Developmental Lineage of Mammary Gland Alveolar Cells	3.359504e-01	0.474
R-HSA-9006335	Signaling by Erythropoietin	3.778184e-01	0.423
R-HSA-975110	TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling	4.356882e-01	0.361
R-HSA-8941332	RUNX2 regulates genes involved in cell migration	4.795408e-01	0.319
R-HSA-933543	NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10	4.795408e-01	0.319
R-HSA-5658442	Regulation of RAS by GAPs	3.543741e-01	0.451
R-HSA-8943723	Regulation of PTEN mRNA translation	4.290958e-01	0.367
R-HSA-6807505	RNA polymerase II transcribes snRNA genes	3.054521e-01	0.515
R-HSA-4641263	Regulation of FZD by ubiquitination	4.653985e-01	0.332
R-HSA-933542	TRAF6 mediated NF-kB activation	4.543141e-01	0.343
R-HSA-3371497	HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig...	3.808783e-01	0.419
R-HSA-9937080	Developmental Lineage of Multipotent Pancreatic Progenitor Cells	4.450267e-01	0.352
R-HSA-8955332	Carboxyterminal post-translational modifications of tubulin	4.481026e-01	0.349
R-HSA-9768727	Regulation of CDH1 posttranslational processing and trafficking to plasma membra...	4.888423e-01	0.311
R-HSA-8874081	MET activates PTK2 signaling	5.035362e-01	0.298
R-HSA-1368108	BMAL1:CLOCK,NPAS2 activates circadian expression	5.102827e-01	0.292
R-HSA-5696400	Dual Incision in GG-NER	5.102827e-01	0.292
R-HSA-1643713	Signaling by EGFR in Cancer	5.035362e-01	0.298
R-HSA-1236382	Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants	3.520301e-01	0.453
R-HSA-5637815	Signaling by Ligand-Responsive EGFR Variants in Cancer	3.520301e-01	0.453
R-HSA-174417	Telomere C-strand (Lagging Strand) Synthesis	3.372155e-01	0.472
R-HSA-202433	Generation of second messenger molecules	3.008622e-01	0.522
R-HSA-73886	Chromosome Maintenance	4.893009e-01	0.310
R-HSA-180024	DARPP-32 events	3.778184e-01	0.423
R-HSA-180786	Extension of Telomeres	5.078671e-01	0.294
R-HSA-9013695	NOTCH4 Intracellular Domain Regulates Transcription	3.520301e-01	0.453
R-HSA-73893	DNA Damage Bypass	4.845816e-01	0.315
R-HSA-9834899	Specification of the neural plate border	3.005119e-01	0.522
R-HSA-5696398	Nucleotide Excision Repair	3.749759e-01	0.426
R-HSA-9734767	Developmental Cell Lineages	3.603142e-01	0.443
R-HSA-69183	Processive synthesis on the lagging strand	3.746075e-01	0.426
R-HSA-9020702	Interleukin-1 signaling	3.152149e-01	0.501
R-HSA-445989	TAK1-dependent IKK and NF-kappa-B activation	3.037250e-01	0.518
R-HSA-9754189	Germ layer formation at gastrulation	3.005119e-01	0.522
R-HSA-2426168	Activation of gene expression by SREBF (SREBP)	3.061371e-01	0.514
R-HSA-9603381	Activated NTRK3 signals through PI3K	3.201876e-01	0.495
R-HSA-75067	Processing of Capped Intronless Pre-mRNA	2.665058e-01	0.574
R-HSA-198203	PI3K/AKT activation	4.416910e-01	0.355
R-HSA-5696395	Formation of Incision Complex in GG-NER	3.008622e-01	0.522
R-HSA-164938	Nef-mediates down modulation of cell surface receptors by recruiting them to cla...	4.653985e-01	0.332
R-HSA-3858494	Beta-catenin independent WNT signaling	3.164755e-01	0.500
R-HSA-76009	Platelet Aggregation (Plug Formation)	2.709069e-01	0.567
R-HSA-749476	RNA Polymerase III Abortive And Retractive Initiation	3.763256e-01	0.424
R-HSA-74158	RNA Polymerase III Transcription	3.763256e-01	0.424
R-HSA-186797	Signaling by PDGF	4.169728e-01	0.380
R-HSA-9020558	Interleukin-2 signaling	4.795408e-01	0.319
R-HSA-1168372	Downstream signaling events of B Cell Receptor (BCR)	2.925505e-01	0.534
R-HSA-6803211	TP53 Regulates Transcription of Death Receptors and Ligands	3.435297e-01	0.464
R-HSA-2122948	Activated NOTCH1 Transmits Signal to the Nucleus	5.035362e-01	0.298
R-HSA-9619665	EGR2 and SOX10-mediated initiation of Schwann cell myelination	3.159381e-01	0.500
R-HSA-1655829	Regulation of cholesterol biosynthesis by SREBP (SREBF)	4.204033e-01	0.376
R-HSA-112040	G-protein mediated events	4.968578e-01	0.304
R-HSA-164939	Nef mediated downregulation of CD28 cell surface expression	2.923504e-01	0.534
R-HSA-5655291	Signaling by FGFR4 in disease	3.435297e-01	0.464
R-HSA-1433617	Regulation of signaling by NODAL	4.023671e-01	0.395
R-HSA-430039	mRNA decay by 5' to 3' exoribonuclease	4.356882e-01	0.361
R-HSA-9832991	Formation of the posterior neural plate	4.795408e-01	0.319
R-HSA-6783310	Fanconi Anemia Pathway	4.111760e-01	0.386
R-HSA-202403	TCR signaling	3.363792e-01	0.473
R-HSA-164952	The role of Nef in HIV-1 replication and disease pathogenesis	4.290958e-01	0.367
R-HSA-6807070	PTEN Regulation	3.468924e-01	0.460
R-HSA-6794361	Neurexins and neuroligins	2.596968e-01	0.586
R-HSA-9703465	Signaling by FLT3 fusion proteins	3.104546e-01	0.508
R-HSA-442729	CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde	3.617737e-01	0.442
R-HSA-1253288	Downregulation of ERBB4 signaling	3.617737e-01	0.442
R-HSA-75035	Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex	3.123264e-01	0.505
R-HSA-975163	IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation	3.435297e-01	0.464
R-HSA-428542	Regulation of commissural axon pathfinding by SLIT and ROBO	4.023671e-01	0.395
R-HSA-9013700	NOTCH4 Activation and Transmission of Signal to the Nucleus	4.023671e-01	0.395
R-HSA-9675126	Diseases of mitotic cell cycle	2.765623e-01	0.558
R-HSA-419408	Lysosphingolipid and LPA receptors	3.746075e-01	0.426
R-HSA-112043	PLC beta mediated events	4.008506e-01	0.397
R-HSA-1266695	Interleukin-7 signaling	2.883277e-01	0.540
R-HSA-9818749	Regulation of NFE2L2 gene expression	2.779719e-01	0.556
R-HSA-212436	Generic Transcription Pathway	3.678213e-01	0.434
R-HSA-5684996	MAPK1/MAPK3 signaling	4.182532e-01	0.379
R-HSA-5649702	APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement P...	4.023671e-01	0.395
R-HSA-9933387	RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression	4.003351e-01	0.398
R-HSA-1226099	Signaling by FGFR in disease	3.484744e-01	0.458
R-HSA-432142	Platelet sensitization by LDL	4.943962e-01	0.306
R-HSA-69239	Synthesis of DNA	5.054262e-01	0.296
R-HSA-8939211	ESR-mediated signaling	3.541553e-01	0.451
R-HSA-1295596	Spry regulation of FGF signaling	3.746075e-01	0.426
R-HSA-5621575	CD209 (DC-SIGN) signaling	4.543141e-01	0.343
R-HSA-111932	CaMK IV-mediated phosphorylation of CREB	4.416910e-01	0.355
R-HSA-1433557	Signaling by SCF-KIT	3.741038e-01	0.427
R-HSA-5358508	Mismatch Repair	2.750670e-01	0.561
R-HSA-9860931	Response of endothelial cells to shear stress	2.587755e-01	0.587
R-HSA-110373	Resolution of AP sites via the multiple-nucleotide patch replacement pathway	5.035362e-01	0.298
R-HSA-5673001	RAF/MAP kinase cascade	3.657084e-01	0.437
R-HSA-8848021	Signaling by PTK6	4.330802e-01	0.363
R-HSA-9006927	Signaling by Non-Receptor Tyrosine Kinases	4.330802e-01	0.363
R-HSA-2262752	Cellular responses to stress	3.927026e-01	0.406
R-HSA-5632928	Defective Mismatch Repair Associated With MSH2	2.923504e-01	0.534
R-HSA-190827	Transport of connexins along the secretory pathway	2.923504e-01	0.534
R-HSA-75064	mRNA Editing: A to I Conversion	3.694037e-01	0.432
R-HSA-75102	C6 deamination of adenosine	3.694037e-01	0.432
R-HSA-198765	Signalling to ERK5	3.694037e-01	0.432
R-HSA-9657688	Defective factor XII causes hereditary angioedema	3.694037e-01	0.432
R-HSA-8948747	Regulation of PTEN localization	3.201876e-01	0.495
R-HSA-8875791	MET activates STAT3	4.380709e-01	0.358
R-HSA-8849469	PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1	3.617737e-01	0.442
R-HSA-8866904	Negative regulation of activity of TFAP2 (AP-2) family transcription factors	3.617737e-01	0.442
R-HSA-174490	Membrane binding and targetting of GAG proteins	3.123264e-01	0.505
R-HSA-8866907	Activation of the TFAP2 (AP-2) family of transcription factors	4.023671e-01	0.395
R-HSA-8866911	TFAP2 (AP-2) family regulates transcription of cell cycle factors	4.992644e-01	0.302
R-HSA-9617324	Negative regulation of NMDA receptor-mediated neuronal transmission	3.778572e-01	0.423
R-HSA-8852276	The role of GTSE1 in G2/M progression after G2 checkpoint	2.916013e-01	0.535
R-HSA-9675151	Disorders of Developmental Biology	4.356882e-01	0.361
R-HSA-451306	Ionotropic activity of kainate receptors	4.795408e-01	0.319
R-HSA-69052	Switching of origins to a post-replicative state	3.342970e-01	0.476
R-HSA-399719	Trafficking of AMPA receptors	4.227601e-01	0.374
R-HSA-1489509	DAG and IP3 signaling	4.111760e-01	0.386
R-HSA-5218921	VEGFR2 mediated cell proliferation	4.791520e-01	0.320
R-HSA-5620924	Intraflagellar transport	4.664158e-01	0.331
R-HSA-8953897	Cellular responses to stimuli	3.858282e-01	0.414
R-HSA-5205647	Mitophagy	5.102827e-01	0.292
R-HSA-5675221	Negative regulation of MAPK pathway	3.372155e-01	0.472
R-HSA-1852241	Organelle biogenesis and maintenance	4.065471e-01	0.391
R-HSA-9664873	Pexophagy	4.416910e-01	0.355
R-HSA-1660516	Synthesis of PIPs at the early endosome membrane	4.791520e-01	0.320
R-HSA-112314	Neurotransmitter receptors and postsynaptic signal transmission	2.877294e-01	0.541
R-HSA-9768777	Regulation of NPAS4 gene transcription	4.023671e-01	0.395
R-HSA-389357	CD28 dependent PI3K/Akt signaling	3.328003e-01	0.478
R-HSA-9616222	Transcriptional regulation of granulopoiesis	4.169728e-01	0.380
R-HSA-9725371	Nuclear events stimulated by ALK signaling in cancer	4.664158e-01	0.331
R-HSA-74749	Signal attenuation	4.416910e-01	0.355
R-HSA-8934903	Receptor Mediated Mitophagy	4.416910e-01	0.355
R-HSA-380994	ATF4 activates genes in response to endoplasmic reticulum stress	3.552816e-01	0.449
R-HSA-9620244	Long-term potentiation	4.791520e-01	0.320
R-HSA-6811558	PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling	4.131566e-01	0.384
R-HSA-5687128	MAPK6/MAPK4 signaling	3.871309e-01	0.412
R-HSA-390466	Chaperonin-mediated protein folding	4.284877e-01	0.368
R-HSA-5676594	TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway	3.123264e-01	0.505
R-HSA-170834	Signaling by TGF-beta Receptor Complex	2.694115e-01	0.570
R-HSA-9031628	NGF-stimulated transcription	4.664158e-01	0.331
R-HSA-9682385	FLT3 signaling in disease	3.763256e-01	0.424
R-HSA-447041	CHL1 interactions	3.201876e-01	0.495
R-HSA-111453	BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members	3.617737e-01	0.442
R-HSA-174495	Synthesis And Processing Of GAG, GAGPOL Polyproteins	3.435297e-01	0.464
R-HSA-937042	IRAK2 mediated activation of TAK1 complex	4.023671e-01	0.395
R-HSA-200425	Carnitine shuttle	4.290958e-01	0.367
R-HSA-1660499	Synthesis of PIPs at the plasma membrane	4.169728e-01	0.380
R-HSA-5628897	TP53 Regulates Metabolic Genes	5.091667e-01	0.293
R-HSA-8849932	Synaptic adhesion-like molecules	2.750670e-01	0.561
R-HSA-445355	Smooth Muscle Contraction	4.058749e-01	0.392
R-HSA-2173793	Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer	4.573144e-01	0.340
R-HSA-2173789	TGF-beta receptor signaling activates SMADs	3.741038e-01	0.427
R-HSA-190704	Oligomerization of connexins into connexons	2.923504e-01	0.534
R-HSA-9657689	Defective SERPING1 causes hereditary angioedema	2.923504e-01	0.534
R-HSA-9635644	Inhibition of membrane repair	2.923504e-01	0.534
R-HSA-5423599	Diseases of Mismatch Repair (MMR)	4.380709e-01	0.358
R-HSA-9619229	Activation of RAC1 downstream of NMDARs	4.023671e-01	0.395
R-HSA-5626978	TNFR1-mediated ceramide production	4.992644e-01	0.302
R-HSA-193670	p75NTR negatively regulates cell cycle via SC1	4.992644e-01	0.302
R-HSA-9729555	Sensory perception of sour taste	4.992644e-01	0.302
R-HSA-416700	Other semaphorin interactions	3.746075e-01	0.426
R-HSA-5218920	VEGFR2 mediated vascular permeability	3.189494e-01	0.496
R-HSA-9706019	RHOBTB3 ATPase cycle	4.795408e-01	0.319
R-HSA-9675135	Diseases of DNA repair	2.871971e-01	0.542
R-HSA-201556	Signaling by ALK	2.829998e-01	0.548
R-HSA-8877330	RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)	3.123264e-01	0.505
R-HSA-199418	Negative regulation of the PI3K/AKT network	5.046725e-01	0.297
R-HSA-2151201	Transcriptional activation of mitochondrial biogenesis	4.492878e-01	0.347
R-HSA-9823739	Formation of the anterior neural plate	3.746075e-01	0.426
R-HSA-9708296	tRNA-derived small RNA (tsRNA or tRNA-related fragment, tRF) biogenesis	3.694037e-01	0.432
R-HSA-9725554	Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin	2.829998e-01	0.548
R-HSA-9958790	SLC-mediated transport of inorganic anions	4.167918e-01	0.380
R-HSA-9819196	Zygotic genome activation (ZGA)	3.520301e-01	0.453
R-HSA-5358606	Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)	4.653985e-01	0.332
R-HSA-399721	Glutamate binding, activation of AMPA receptors and synaptic plasticity	4.670731e-01	0.331
R-HSA-9830369	Kidney development	4.968578e-01	0.304
R-HSA-9762293	Regulation of CDH11 gene transcription	4.023671e-01	0.395
R-HSA-5336415	Uptake and function of diphtheria toxin	3.201876e-01	0.495
R-HSA-391160	Signal regulatory protein family interactions	3.435297e-01	0.464
R-HSA-448706	Interleukin-1 processing	4.023671e-01	0.395
R-HSA-9824594	Regulation of MITF-M-dependent genes involved in apoptosis	3.520301e-01	0.453
R-HSA-450302	activated TAK1 mediates p38 MAPK activation	3.778572e-01	0.423
R-HSA-9645460	Alpha-protein kinase 1 signaling pathway	4.795408e-01	0.319
R-HSA-3000170	Syndecan interactions	4.290958e-01	0.367
R-HSA-186712	Regulation of beta-cell development	5.078671e-01	0.294
R-HSA-9831926	Nephron development	2.750670e-01	0.561
R-HSA-70326	Glucose metabolism	2.588995e-01	0.587
R-HSA-9768919	NPAS4 regulates expression of target genes	3.359504e-01	0.474
R-HSA-5689877	Josephin domain DUBs	4.416910e-01	0.355
R-HSA-6791312	TP53 Regulates Transcription of Cell Cycle Genes	3.367618e-01	0.473
R-HSA-2586552	Signaling by Leptin	4.416910e-01	0.355
R-HSA-391251	Protein folding	5.105499e-01	0.292
R-HSA-8936459	RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun...	5.125215e-01	0.290
R-HSA-2132295	MHC class II antigen presentation	5.126654e-01	0.290
R-HSA-9917777	Epigenetic regulation by WDR5-containing histone modifying complexes	5.144733e-01	0.289
R-HSA-416550	Sema4D mediated inhibition of cell attachment and migration	5.157712e-01	0.288
R-HSA-9623433	NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis	5.157712e-01	0.288
R-HSA-9824878	Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7	5.157712e-01	0.288
R-HSA-5693548	Sensing of DNA Double Strand Breaks	5.157712e-01	0.288
R-HSA-1236977	Endosomal/Vacuolar pathway	5.157712e-01	0.288
R-HSA-9024446	NR1H2 and NR1H3-mediated signaling	5.166897e-01	0.287
R-HSA-5621481	C-type lectin receptors (CLRs)	5.202374e-01	0.284
R-HSA-3371571	HSF1-dependent transactivation	5.203426e-01	0.284
R-HSA-1169091	Activation of NF-kappaB in B cells	5.203426e-01	0.284
R-HSA-174048	APC/C:Cdc20 mediated degradation of Cyclin B	5.225863e-01	0.282
R-HSA-9856532	Mechanical load activates signaling by PIEZO1 and integrins in osteocytes	5.225863e-01	0.282
R-HSA-844456	The NLRP3 inflammasome	5.225863e-01	0.282
R-HSA-2644606	Constitutive Signaling by NOTCH1 PEST Domain Mutants	5.243943e-01	0.280
R-HSA-2644602	Signaling by NOTCH1 PEST Domain Mutants in Cancer	5.243943e-01	0.280
R-HSA-2894862	Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants	5.243943e-01	0.280
R-HSA-2894858	Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer	5.243943e-01	0.280
R-HSA-2644603	Signaling by NOTCH1 in Cancer	5.243943e-01	0.280
R-HSA-3928663	EPHA-mediated growth cone collapse	5.274025e-01	0.278
R-HSA-167243	Tat-mediated HIV elongation arrest and recovery	5.274025e-01	0.278
R-HSA-167238	Pausing and recovery of Tat-mediated HIV elongation	5.274025e-01	0.278
R-HSA-9841251	Mitochondrial unfolded protein response (UPRmt)	5.274025e-01	0.278
R-HSA-9006115	Signaling by NTRK2 (TRKB)	5.274025e-01	0.278
R-HSA-6803204	TP53 Regulates Transcription of Genes Involved in Cytochrome C Release	5.274025e-01	0.278
R-HSA-381119	Unfolded Protein Response (UPR)	5.299504e-01	0.276
R-HSA-381042	PERK regulates gene expression	5.313477e-01	0.275
R-HSA-381038	XBP1(S) activates chaperone genes	5.344075e-01	0.272
R-HSA-5654743	Signaling by FGFR4	5.347849e-01	0.272
R-HSA-2219530	Constitutive Signaling by Aberrant PI3K in Cancer	5.372624e-01	0.270
R-HSA-68949	Orc1 removal from chromatin	5.378786e-01	0.269
R-HSA-2559580	Oxidative Stress Induced Senescence	5.399445e-01	0.268
R-HSA-1483255	PI Metabolism	5.399445e-01	0.268
R-HSA-389513	Co-inhibition by CTLA4	5.498920e-01	0.260
R-HSA-1181150	Signaling by NODAL	5.498920e-01	0.260
R-HSA-2197563	NOTCH2 intracellular domain regulates transcription	5.502862e-01	0.259
R-HSA-8951936	RUNX3 regulates p14-ARF	5.502862e-01	0.259
R-HSA-8983432	Interleukin-15 signaling	5.502862e-01	0.259
R-HSA-2691230	Signaling by NOTCH1 HD Domain Mutants in Cancer	5.502862e-01	0.259
R-HSA-2691232	Constitutive Signaling by NOTCH1 HD Domain Mutants	5.502862e-01	0.259
R-HSA-9005895	Pervasive developmental disorders	5.502862e-01	0.259
R-HSA-9697154	Disorders of Nervous System Development	5.502862e-01	0.259
R-HSA-9005891	Loss of function of MECP2 in Rett syndrome	5.502862e-01	0.259
R-HSA-69091	Polymerase switching	5.502862e-01	0.259
R-HSA-69109	Leading Strand Synthesis	5.502862e-01	0.259
R-HSA-8983711	OAS antiviral response	5.502862e-01	0.259
R-HSA-5654732	Negative regulation of FGFR3 signaling	5.506954e-01	0.259
R-HSA-450408	AUF1 (hnRNP D0) binds and destabilizes mRNA	5.519956e-01	0.258
R-HSA-6785807	Interleukin-4 and Interleukin-13 signaling	5.535809e-01	0.257
R-HSA-9818026	NFE2L2 regulating inflammation associated genes	5.537971e-01	0.257
R-HSA-9673768	Signaling by membrane-tethered fusions of PDGFRA or PDGFRB	5.537971e-01	0.257
R-HSA-9673221	Defective F9 activation	5.537971e-01	0.257
R-HSA-9706377	FLT3 signaling by CBL mutants	5.537971e-01	0.257
R-HSA-9022535	Loss of phosphorylation of MECP2 at T308	5.537971e-01	0.257
R-HSA-8939245	RUNX1 regulates transcription of genes involved in BCR signaling	5.537971e-01	0.257
R-HSA-9931529	Phosphorylation and nuclear translocation of BMAL1 (ARNTL) and CLOCK	5.537971e-01	0.257
R-HSA-1606341	IRF3 mediated activation of type 1 IFN	5.537971e-01	0.257
R-HSA-8866376	Reelin signalling pathway	5.537971e-01	0.257
R-HSA-8849468	PTK6 Regulates Proteins Involved in RNA Processing	5.537971e-01	0.257
R-HSA-390648	Muscarinic acetylcholine receptors	5.537971e-01	0.257
R-HSA-435368	Zinc efflux and compartmentalization by the SLC30 family	5.537971e-01	0.257
R-HSA-9694516	SARS-CoV-2 Infection	5.539322e-01	0.257
R-HSA-174178	APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ...	5.551493e-01	0.256
R-HSA-432722	Golgi Associated Vesicle Biogenesis	5.551493e-01	0.256
R-HSA-212165	Epigenetic regulation of gene expression	5.560714e-01	0.255
R-HSA-2559586	DNA Damage/Telomere Stress Induced Senescence	5.568206e-01	0.254
R-HSA-5619102	SLC transporter disorders	5.574268e-01	0.254
R-HSA-948021	Transport to the Golgi and subsequent modification	5.645255e-01	0.248
R-HSA-111885	Opioid Signalling	5.650845e-01	0.248
R-HSA-774815	Nucleosome assembly	5.719024e-01	0.243
R-HSA-606279	Deposition of new CENPA-containing nucleosomes at the centromere	5.719024e-01	0.243
R-HSA-5654741	Signaling by FGFR3	5.719024e-01	0.243
R-HSA-72649	Translation initiation complex formation	5.721307e-01	0.243
R-HSA-5689896	Ovarian tumor domain proteases	5.721898e-01	0.242
R-HSA-2173796	SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription	5.721898e-01	0.242
R-HSA-5656169	Termination of translesion DNA synthesis	5.733679e-01	0.242
R-HSA-9664565	Signaling by ERBB2 KD Mutants	5.733679e-01	0.242
R-HSA-5654733	Negative regulation of FGFR4 signaling	5.733679e-01	0.242
R-HSA-917729	Endosomal Sorting Complex Required For Transport (ESCRT)	5.733679e-01	0.242
R-HSA-376176	Signaling by ROBO receptors	5.735114e-01	0.241
R-HSA-5602498	MyD88 deficiency (TLR2/4)	5.762527e-01	0.239
R-HSA-111931	PKA-mediated phosphorylation of CREB	5.762527e-01	0.239
R-HSA-69186	Lagging Strand Synthesis	5.762527e-01	0.239
R-HSA-983168	Antigen processing: Ubiquitination & Proteasome degradation	5.782681e-01	0.238
R-HSA-9818030	NFE2L2 regulating tumorigenic genes	5.830296e-01	0.234
R-HSA-442720	CREB1 phosphorylation through the activation of Adenylate Cyclase	5.830296e-01	0.234
R-HSA-2559582	Senescence-Associated Secretory Phenotype (SASP)	5.882718e-01	0.230
R-HSA-9012852	Signaling by NOTCH3	5.888011e-01	0.230
R-HSA-72165	mRNA Splicing - Minor Pathway	5.899036e-01	0.229
R-HSA-174084	Autodegradation of Cdh1 by Cdh1:APC/C	5.899036e-01	0.229
R-HSA-76046	RNA Polymerase III Transcription Initiation	5.953806e-01	0.225
R-HSA-9013508	NOTCH3 Intracellular Domain Regulates Transcription	5.953806e-01	0.225
R-HSA-1227990	Signaling by ERBB2 in Cancer	5.953806e-01	0.225
R-HSA-114452	Activation of BH3-only proteins	5.953806e-01	0.225
R-HSA-9687139	Aberrant regulation of mitotic cell cycle due to RB1 defects	5.953806e-01	0.225
R-HSA-9671555	Signaling by PDGFR in disease	6.016228e-01	0.221
R-HSA-438066	Unblocking of NMDA receptors, glutamate binding and activation	6.016228e-01	0.221
R-HSA-76066	RNA Polymerase III Transcription Initiation From Type 2 Promoter	6.016228e-01	0.221
R-HSA-442982	Ras activation upon Ca2+ influx through NMDA receptor	6.016228e-01	0.221
R-HSA-9034015	Signaling by NTRK3 (TRKC)	6.016228e-01	0.221
R-HSA-175474	Assembly Of The HIV Virion	6.016228e-01	0.221
R-HSA-182218	Nef Mediated CD8 Down-regulation	6.023938e-01	0.220
R-HSA-5638303	Inhibition of Signaling by Overexpressed EGFR	6.023938e-01	0.220
R-HSA-5638302	Signaling by Overexpressed Wild-Type EGFR in Cancer	6.023938e-01	0.220
R-HSA-176417	Phosphorylation of Emi1	6.023938e-01	0.220
R-HSA-9907570	Loss-of-function mutations in DLD cause MSUD3/DLDD	6.023938e-01	0.220
R-HSA-9022537	Loss of MECP2 binding ability to the NCoR/SMRT complex	6.023938e-01	0.220
R-HSA-9865113	Loss-of-function mutations in DBT cause MSUD2	6.023938e-01	0.220
R-HSA-8937144	Aryl hydrocarbon receptor signalling	6.023938e-01	0.220
R-HSA-193681	Ceramide signalling	6.023938e-01	0.220
R-HSA-187706	Signalling to p38 via RIT and RIN	6.023938e-01	0.220
R-HSA-5660668	CLEC7A/inflammasome pathway	6.023938e-01	0.220
R-HSA-427652	Sodium-coupled phosphate cotransporters	6.023938e-01	0.220
R-HSA-2660826	Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant	6.023938e-01	0.220
R-HSA-2660825	Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant	6.023938e-01	0.220
R-HSA-8950505	Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati...	6.035898e-01	0.219
R-HSA-72702	Ribosomal scanning and start codon recognition	6.051409e-01	0.218
R-HSA-9662361	Sensory processing of sound by outer hair cells of the cochlea	6.051409e-01	0.218
R-HSA-5358351	Signaling by Hedgehog	6.137372e-01	0.212
R-HSA-205043	NRIF signals cell death from the nucleus	6.139779e-01	0.212
R-HSA-5578768	Physiological factors	6.139779e-01	0.212
R-HSA-453279	Mitotic G1 phase and G1/S transition	6.140133e-01	0.212
R-HSA-381070	IRE1alpha activates chaperones	6.146238e-01	0.211
R-HSA-9909648	Regulation of PD-L1(CD274) expression	6.152179e-01	0.211
R-HSA-936440	Negative regulators of DDX58/IFIH1 signaling	6.167019e-01	0.210
R-HSA-9833109	Evasion by RSV of host interferon responses	6.167019e-01	0.210
R-HSA-162588	Budding and maturation of HIV virion	6.167019e-01	0.210
R-HSA-5689880	Ub-specific processing proteases	6.245281e-01	0.204
R-HSA-909733	Interferon alpha/beta signaling	6.248116e-01	0.204
R-HSA-76061	RNA Polymerase III Transcription Initiation From Type 1 Promoter	6.259697e-01	0.203
R-HSA-9013507	NOTCH3 Activation and Transmission of Signal to the Nucleus	6.259697e-01	0.203
R-HSA-6803205	TP53 regulates transcription of several additional cell death genes whose specif...	6.259697e-01	0.203
R-HSA-8941858	Regulation of RUNX3 expression and activity	6.297538e-01	0.201
R-HSA-3371568	Attenuation phase	6.297538e-01	0.201
R-HSA-167152	Formation of HIV elongation complex in the absence of HIV Tat	6.297538e-01	0.201
R-HSA-9844594	Transcriptional regulation of brown and beige adipocyte differentiation by EBF2	6.297538e-01	0.201
R-HSA-9843743	Transcriptional regulation of brown and beige adipocyte differentiation	6.297538e-01	0.201
R-HSA-449147	Signaling by Interleukins	6.306962e-01	0.200
R-HSA-2029480	Fcgamma receptor (FCGR) dependent phagocytosis	6.337351e-01	0.198
R-HSA-9610379	HCMV Late Events	6.337978e-01	0.198
R-HSA-72662	Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub...	6.367613e-01	0.196
R-HSA-2173795	Downregulation of SMAD2/3:SMAD4 transcriptional activity	6.373068e-01	0.196
R-HSA-68867	Assembly of the pre-replicative complex	6.398077e-01	0.194
R-HSA-8876198	RAB GEFs exchange GTP for GDP on RABs	6.418345e-01	0.193
R-HSA-9027284	Erythropoietin activates RAS	6.431338e-01	0.192
R-HSA-111447	Activation of BAD and translocation to mitochondria	6.431338e-01	0.192
R-HSA-174430	Telomere C-strand synthesis initiation	6.431338e-01	0.192
R-HSA-9735871	SARS-CoV-1 targets host intracellular signalling and regulatory pathways	6.431338e-01	0.192
R-HSA-196780	Biotin transport and metabolism	6.431338e-01	0.192
R-HSA-9701898	STAT3 nuclear events downstream of ALK signaling	6.431338e-01	0.192
R-HSA-8857538	PTK6 promotes HIF1A stabilization	6.457003e-01	0.190
R-HSA-426486	Small interfering RNA (siRNA) biogenesis	6.457003e-01	0.190
R-HSA-9842640	Signaling by LTK in cancer	6.457003e-01	0.190
R-HSA-2980767	Activation of NIMA Kinases NEK9, NEK6, NEK7	6.457003e-01	0.190
R-HSA-9027283	Erythropoietin activates STAT5	6.457003e-01	0.190
R-HSA-9645135	STAT5 Activation	6.457003e-01	0.190
R-HSA-5263617	Metabolism of ingested MeSeO2H into MeSeH	6.457003e-01	0.190
R-HSA-9865125	Loss-of-function mutations in BCKDHA or BCKDHB cause MSUD	6.457003e-01	0.190
R-HSA-5619070	Defective SLC16A1 causes symptomatic deficiency in lactate transport (SDLT)	6.457003e-01	0.190
R-HSA-9912529	H139Hfs13* PPM1K causes a mild variant of MSUD	6.457003e-01	0.190
R-HSA-6806942	MET Receptor Activation	6.457003e-01	0.190
R-HSA-69478	G2/M DNA replication checkpoint	6.457003e-01	0.190
R-HSA-2161517	Abacavir transmembrane transport	6.457003e-01	0.190
R-HSA-389542	NADPH regeneration	6.457003e-01	0.190
R-HSA-164944	Nef and signal transduction	6.457003e-01	0.190
R-HSA-391906	Leukotriene receptors	6.457003e-01	0.190
R-HSA-447043	Neurofascin interactions	6.457003e-01	0.190
R-HSA-1855167	Synthesis of pyrophosphates in the cytosol	6.492728e-01	0.188
R-HSA-9830674	Formation of the ureteric bud	6.492728e-01	0.188
R-HSA-9842860	Regulation of endogenous retroelements	6.500031e-01	0.187
R-HSA-388841	Regulation of T cell activation by CD28 family	6.514114e-01	0.186
R-HSA-397795	G-protein beta:gamma signalling	6.571768e-01	0.182
R-HSA-5654726	Negative regulation of FGFR1 signaling	6.571768e-01	0.182
R-HSA-1855204	Synthesis of IP3 and IP4 in the cytosol	6.571768e-01	0.182
R-HSA-216083	Integrin cell surface interactions	6.577935e-01	0.182
R-HSA-1280218	Adaptive Immune System	6.579559e-01	0.182
R-HSA-5610780	Degradation of GLI1 by the proteasome	6.653953e-01	0.177
R-HSA-9932298	Degradation of CRY and PER proteins	6.653953e-01	0.177
R-HSA-6811438	Intra-Golgi traffic	6.653953e-01	0.177
R-HSA-9845323	Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs)	6.668780e-01	0.176
R-HSA-1660661	Sphingolipid de novo biosynthesis	6.668780e-01	0.176
R-HSA-8878166	Transcriptional regulation by RUNX2	6.684362e-01	0.175
R-HSA-450604	KSRP (KHSRP) binds and destabilizes mRNA	6.705205e-01	0.174
R-HSA-5083625	Defective GALNT3 causes HFTC	6.705205e-01	0.174
R-HSA-5083636	Defective GALNT12 causes CRCS1	6.705205e-01	0.174
R-HSA-5099900	WNT5A-dependent internalization of FZD4	6.705205e-01	0.174
R-HSA-9758274	Regulation of NF-kappa B signaling	6.705205e-01	0.174
R-HSA-9673324	WNT5:FZD7-mediated leishmania damping	6.705205e-01	0.174
R-HSA-9664420	Killing mechanisms	6.705205e-01	0.174
R-HSA-434316	Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion	6.705205e-01	0.174
R-HSA-9634600	Regulation of glycolysis by fructose 2,6-bisphosphate metabolism	6.705205e-01	0.174
R-HSA-9945266	Differentiation of T cells	6.705205e-01	0.174
R-HSA-9942503	Differentiation of naive CD+ T cells to T helper 1 cells (Th1 cells)	6.705205e-01	0.174
R-HSA-210744	Regulation of gene expression in late stage (branching morphogenesis) pancreatic...	6.705205e-01	0.174
R-HSA-9665686	Signaling by ERBB2 TMD/JMD mutants	6.715217e-01	0.173
R-HSA-418592	ADP signalling through P2Y purinoceptor 1	6.715217e-01	0.173
R-HSA-446652	Interleukin-1 family signaling	6.723113e-01	0.172
R-HSA-912446	Meiotic recombination	6.734989e-01	0.172
R-HSA-72306	tRNA processing	6.790866e-01	0.168
R-HSA-8939902	Regulation of RUNX2 expression and activity	6.813456e-01	0.167
R-HSA-111996	Ca-dependent events	6.823510e-01	0.166
R-HSA-9856530	High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR...	6.836597e-01	0.165
R-HSA-2892245	POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation	6.842922e-01	0.165
R-HSA-163767	PP2A-mediated dephosphorylation of key metabolic factors	6.842922e-01	0.165
R-HSA-9732724	IFNG signaling activates MAPKs	6.842922e-01	0.165
R-HSA-2562578	TRIF-mediated programmed cell death	6.842922e-01	0.165
R-HSA-9031525	NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake	6.842922e-01	0.165
R-HSA-9632974	NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis	6.842922e-01	0.165
R-HSA-111367	SLBP independent Processing of Histone Pre-mRNAs	6.842922e-01	0.165
R-HSA-9031528	NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipo...	6.842922e-01	0.165
R-HSA-163754	Insulin effects increased synthesis of Xylulose-5-Phosphate	6.842922e-01	0.165
R-HSA-167590	Nef Mediated CD4 Down-regulation	6.842922e-01	0.165
R-HSA-5576890	Phase 3 - rapid repolarisation	6.842922e-01	0.165
R-HSA-139915	Activation of PUMA and translocation to mitochondria	6.842922e-01	0.165
R-HSA-8964046	VLDL clearance	6.842922e-01	0.165
R-HSA-426117	Cation-coupled Chloride cotransporters	6.842922e-01	0.165
R-HSA-3371599	Defective HLCS causes multiple carboxylase deficiency	6.842922e-01	0.165
R-HSA-418886	Netrin mediated repulsion signals	6.842922e-01	0.165
R-HSA-381340	Transcriptional regulation of white adipocyte differentiation	6.874179e-01	0.163
R-HSA-174184	Cdc20:Phospho-APC/C mediated degradation of Cyclin A	6.888349e-01	0.162
R-HSA-5339562	Uptake and actions of bacterial toxins	6.888349e-01	0.162
R-HSA-174143	APC/C-mediated degradation of cell cycle proteins	6.888920e-01	0.162
R-HSA-453276	Regulation of mitotic cell cycle	6.888920e-01	0.162
R-HSA-5632684	Hedgehog 'on' state	6.888920e-01	0.162
R-HSA-9759194	Nuclear events mediated by NFE2L2	6.891559e-01	0.162
R-HSA-1482801	Acyl chain remodelling of PS	6.927152e-01	0.159
R-HSA-70221	Glycogen breakdown (glycogenolysis)	6.927152e-01	0.159
R-HSA-9830364	Formation of the nephric duct	6.927152e-01	0.159
R-HSA-9843970	Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex	6.946665e-01	0.158
R-HSA-983170	Antigen Presentation: Folding, assembly and peptide loading of class I MHC	6.946665e-01	0.158
R-HSA-9680350	Signaling by CSF1 (M-CSF) in myeloid cells	6.946665e-01	0.158
R-HSA-5654727	Negative regulation of FGFR2 signaling	6.946665e-01	0.158
R-HSA-1980145	Signaling by NOTCH2	6.946665e-01	0.158
R-HSA-176408	Regulation of APC/C activators between G1/S and early anaphase	6.954086e-01	0.158
R-HSA-9912633	Antigen processing: Ub, ATP-independent proteasomal degradation	6.961775e-01	0.157
R-HSA-399997	Acetylcholine regulates insulin secretion	6.961775e-01	0.157
R-HSA-6804114	TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest	6.961775e-01	0.157
R-HSA-9651496	Defects of contact activation system (CAS) and kallikrein/kinin system (KKS)	6.961775e-01	0.157
R-HSA-199992	trans-Golgi Network Vesicle Budding	7.019188e-01	0.154
R-HSA-73884	Base Excision Repair	7.030797e-01	0.153
R-HSA-179419	APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th...	7.036883e-01	0.153
R-HSA-169911	Regulation of Apoptosis	7.122763e-01	0.147
R-HSA-210500	Glutamate Neurotransmitter Release Cycle	7.128599e-01	0.147
R-HSA-5689901	Metalloprotease DUBs	7.128599e-01	0.147
R-HSA-9022699	MECP2 regulates neuronal receptors and channels	7.128599e-01	0.147
R-HSA-9843745	Adipogenesis	7.156714e-01	0.145
R-HSA-69017	CDK-mediated phosphorylation and removal of Cdc6	7.180546e-01	0.144
R-HSA-112126	ALKBH3 mediated reversal of alkylation damage	7.186825e-01	0.143
R-HSA-111995	phospho-PLA2 pathway	7.186825e-01	0.143
R-HSA-3785653	Myoclonic epilepsy of Lafora	7.186825e-01	0.143
R-HSA-9028335	Activated NTRK2 signals through PI3K	7.186825e-01	0.143
R-HSA-193634	Axonal growth inhibition (RHOA activation)	7.186825e-01	0.143
R-HSA-77588	SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs	7.186825e-01	0.143
R-HSA-8985947	Interleukin-9 signaling	7.186825e-01	0.143
R-HSA-9927354	Co-stimulation by ICOS	7.186825e-01	0.143
R-HSA-425986	Sodium/Proton exchangers	7.186825e-01	0.143
R-HSA-9032500	Activated NTRK2 signals through FYN	7.186825e-01	0.143
R-HSA-5083632	Defective C1GALT1C1 causes TNPS	7.201566e-01	0.143
R-HSA-1660517	Synthesis of PIPs at the late endosome membrane	7.201566e-01	0.143
R-HSA-1963642	PI3K events in ERBB2 signaling	7.201566e-01	0.143
R-HSA-9909505	Modulation of host responses by IFN-stimulated genes	7.201566e-01	0.143
R-HSA-9614085	FOXO-mediated transcription	7.205267e-01	0.142
R-HSA-983169	Class I MHC mediated antigen processing & presentation	7.217852e-01	0.142
R-HSA-9664407	Parasite infection	7.219651e-01	0.141
R-HSA-9664422	FCGR3A-mediated phagocytosis	7.219651e-01	0.141
R-HSA-9664417	Leishmania phagocytosis	7.219651e-01	0.141
R-HSA-983705	Signaling by the B Cell Receptor (BCR)	7.254927e-01	0.139
R-HSA-9013694	Signaling by NOTCH4	7.268960e-01	0.139
R-HSA-3371511	HSF1 activation	7.291303e-01	0.137
R-HSA-111933	Calmodulin induced events	7.291303e-01	0.137
R-HSA-111997	CaM pathway	7.291303e-01	0.137
R-HSA-140877	Formation of Fibrin Clot (Clotting Cascade)	7.291303e-01	0.137
R-HSA-69601	Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A	7.296750e-01	0.137
R-HSA-69613	p53-Independent G1/S DNA Damage Checkpoint	7.296750e-01	0.137
R-HSA-2029482	Regulation of actin dynamics for phagocytic cup formation	7.308156e-01	0.136
R-HSA-176409	APC/C:Cdc20 mediated degradation of mitotic proteins	7.319311e-01	0.136
R-HSA-8866652	Synthesis of active ubiquitin: roles of E1 and E2 enzymes	7.319688e-01	0.136
R-HSA-5655332	Signaling by FGFR3 in disease	7.319688e-01	0.136
R-HSA-69002	DNA Replication Pre-Initiation	7.363456e-01	0.133
R-HSA-5633008	TP53 Regulates Transcription of Cell Death Genes	7.388406e-01	0.131
R-HSA-1592230	Mitochondrial biogenesis	7.415227e-01	0.130
R-HSA-164378	PKA activation in glucagon signalling	7.425187e-01	0.129
R-HSA-163615	PKA activation	7.425187e-01	0.129
R-HSA-181429	Serotonin Neurotransmitter Release Cycle	7.425187e-01	0.129
R-HSA-73980	RNA Polymerase III Transcription Termination	7.425187e-01	0.129
R-HSA-6804760	Regulation of TP53 Activity through Methylation	7.425187e-01	0.129
R-HSA-72695	Formation of the ternary complex, and subsequently, the 43S complex	7.442631e-01	0.128
R-HSA-933541	TRAF6 mediated IRF7 activation	7.452341e-01	0.128
R-HSA-4641258	Degradation of DVL	7.452341e-01	0.128
R-HSA-176814	Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins	7.453175e-01	0.128
R-HSA-6782210	Gap-filling DNA repair synthesis and ligation in TC-NER	7.453175e-01	0.128
R-HSA-5654736	Signaling by FGFR1	7.453175e-01	0.128
R-HSA-112411	MAPK1 (ERK2) activation	7.493285e-01	0.125
R-HSA-193697	p75NTR regulates axonogenesis	7.493285e-01	0.125
R-HSA-9020958	Interleukin-21 signaling	7.493285e-01	0.125
R-HSA-163680	AMPK inhibits chREBP transcriptional activation activity	7.493285e-01	0.125
R-HSA-2465910	MASTL Facilitates Mitotic Progression	7.493285e-01	0.125
R-HSA-75072	mRNA Editing	7.493285e-01	0.125
R-HSA-450520	HuR (ELAVL1) binds and stabilizes mRNA	7.493285e-01	0.125
R-HSA-9834752	Respiratory syncytial virus genome replication	7.493285e-01	0.125
R-HSA-3323169	Defects in biotin (Btn) metabolism	7.493285e-01	0.125
R-HSA-9840373	Cellular response to mitochondrial stress	7.493285e-01	0.125
R-HSA-8851680	Butyrophilin (BTN) family interactions	7.493285e-01	0.125
R-HSA-418889	Caspase activation via Dependence Receptors in the absence of ligand	7.493285e-01	0.125
R-HSA-171319	Telomere Extension By Telomerase	7.500609e-01	0.125
R-HSA-5205685	PINK1-PRKN Mediated Mitophagy	7.500609e-01	0.125
R-HSA-451326	Activation of kainate receptors upon glutamate binding	7.500609e-01	0.125
R-HSA-622312	Inflammasomes	7.500609e-01	0.125
R-HSA-9020591	Interleukin-12 signaling	7.504204e-01	0.125
R-HSA-174154	APC/C:Cdc20 mediated degradation of Securin	7.582616e-01	0.120
R-HSA-5654710	PI-3K cascade:FGFR3	7.633317e-01	0.117
R-HSA-167242	Abortive elongation of HIV-1 transcript in the absence of Tat	7.633317e-01	0.117
R-HSA-113510	E2F mediated regulation of DNA replication	7.633317e-01	0.117
R-HSA-9671793	Diseases of hemostasis	7.633317e-01	0.117
R-HSA-5654708	Downstream signaling of activated FGFR3	7.671595e-01	0.115
R-HSA-168928	DDX58/IFIH1-mediated induction of interferon-alpha/beta	7.672771e-01	0.115
R-HSA-167172	Transcription of the HIV genome	7.710802e-01	0.113
R-HSA-9662360	Sensory processing of sound by inner hair cells of the cochlea	7.710802e-01	0.113
R-HSA-4086400	PCP/CE pathway	7.724860e-01	0.112
R-HSA-167200	Formation of HIV-1 elongation complex containing HIV-1 Tat	7.752292e-01	0.111
R-HSA-69541	Stabilization of p53	7.752292e-01	0.111
R-HSA-168273	Influenza Viral RNA Transcription and Replication	7.763956e-01	0.110
R-HSA-110056	MAPK3 (ERK1) activation	7.766375e-01	0.110
R-HSA-164843	2-LTR circle formation	7.766375e-01	0.110
R-HSA-390450	Folding of actin by CCT/TriC	7.766375e-01	0.110
R-HSA-173107	Binding and entry of HIV virion	7.766375e-01	0.110
R-HSA-5221030	TET1,2,3 and TDG demethylate DNA	7.766375e-01	0.110
R-HSA-140342	Apoptosis induced DNA fragmentation	7.766375e-01	0.110
R-HSA-2179392	EGFR Transactivation by Gastrin	7.766375e-01	0.110
R-HSA-6803544	Ion influx/efflux at host-pathogen interface	7.766375e-01	0.110
R-HSA-2151209	Activation of PPARGC1A (PGC-1alpha) by phosphorylation	7.766375e-01	0.110
R-HSA-9761174	Formation of intermediate mesoderm	7.766375e-01	0.110
R-HSA-1236973	Cross-presentation of particulate exogenous antigens (phagosomes)	7.766375e-01	0.110
R-HSA-9683686	Maturation of spike protein	7.766375e-01	0.110
R-HSA-9022702	MECP2 regulates transcription of neuronal ligands	7.766375e-01	0.110
R-HSA-9820962	Assembly and release of respiratory syncytial virus (RSV) virions	7.766375e-01	0.110
R-HSA-9668250	Defective factor IX causes hemophilia B	7.766375e-01	0.110
R-HSA-9925563	Developmental Lineage of Pancreatic Ductal Cells	7.822359e-01	0.107
R-HSA-5654720	PI-3K cascade:FGFR4	7.826676e-01	0.106
R-HSA-9609523	Insertion of tail-anchored proteins into the endoplasmic reticulum membrane	7.826676e-01	0.106
R-HSA-5620922	BBSome-mediated cargo-targeting to cilium	7.826676e-01	0.106
R-HSA-3322077	Glycogen synthesis	7.826676e-01	0.106
R-HSA-1482922	Acyl chain remodelling of PI	7.826676e-01	0.106
R-HSA-9629569	Protein hydroxylation	7.826676e-01	0.106
R-HSA-140875	Common Pathway of Fibrin Clot Formation	7.826676e-01	0.106
R-HSA-196108	Pregnenolone biosynthesis	7.826676e-01	0.106
R-HSA-456926	Thrombin signalling through proteinase activated receptors (PARs)	7.832919e-01	0.106
R-HSA-5654716	Downstream signaling of activated FGFR4	7.832919e-01	0.106
R-HSA-2424491	DAP12 signaling	7.832919e-01	0.106
R-HSA-9008059	Interleukin-37 signaling	7.832919e-01	0.106
R-HSA-112315	Transmission across Chemical Synapses	7.883263e-01	0.103
R-HSA-2454202	Fc epsilon receptor (FCERI) signaling	7.890626e-01	0.103
R-HSA-167169	HIV Transcription Elongation	7.891468e-01	0.103
R-HSA-167246	Tat-mediated elongation of the HIV-1 transcript	7.891468e-01	0.103
R-HSA-9670095	Inhibition of DNA recombination at telomere	7.891468e-01	0.103
R-HSA-8982491	Glycogen metabolism	7.891468e-01	0.103
R-HSA-157118	Signaling by NOTCH	7.920335e-01	0.101
R-HSA-397014	Muscle contraction	7.928459e-01	0.101
R-HSA-5654738	Signaling by FGFR2	7.931024e-01	0.101
R-HSA-1227986	Signaling by ERBB2	7.940090e-01	0.100
R-HSA-157579	Telomere Maintenance	7.954511e-01	0.099
R-HSA-109704	PI3K Cascade	7.967860e-01	0.099
R-HSA-211733	Regulation of activated PAK-2p34 by proteasome mediated degradation	7.984886e-01	0.098
R-HSA-5694530	Cargo concentration in the ER	7.984886e-01	0.098
R-HSA-140837	Intrinsic Pathway of Fibrin Clot Formation	8.006010e-01	0.097
R-HSA-2979096	NOTCH2 Activation and Transmission of Signal to the Nucleus	8.006010e-01	0.097
R-HSA-264642	Acetylcholine Neurotransmitter Release Cycle	8.006010e-01	0.097
R-HSA-162594	Early Phase of HIV Life Cycle	8.006010e-01	0.097
R-HSA-112308	Presynaptic depolarization and calcium channel opening	8.009729e-01	0.096
R-HSA-1483226	Synthesis of PI	8.009729e-01	0.096
R-HSA-1483248	Synthesis of PIPs at the ER membrane	8.009729e-01	0.096
R-HSA-427601	Inorganic anion exchange by SLC26 transporters	8.009729e-01	0.096
R-HSA-5682910	LGI-ADAM interactions	8.009729e-01	0.096
R-HSA-9758890	Transport of RCbl within the body	8.009729e-01	0.096
R-HSA-5676590	NIK-->noncanonical NF-kB signaling	8.023658e-01	0.096
R-HSA-110313	Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa...	8.023658e-01	0.096
R-HSA-9694548	Maturation of spike protein	8.023658e-01	0.096
R-HSA-9679506	SARS-CoV Infections	8.040636e-01	0.095
R-HSA-2428928	IRS-related events triggered by IGF1R	8.049931e-01	0.094
R-HSA-110330	Recognition and association of DNA glycosylase with site containing an affected ...	8.127821e-01	0.090
R-HSA-69656	Cyclin A:Cdk2-associated events at S phase entry	8.132622e-01	0.090
R-HSA-9755511	KEAP1-NFE2L2 pathway	8.161568e-01	0.088
R-HSA-8949215	Mitochondrial calcium ion transport	8.172081e-01	0.088
R-HSA-168255	Influenza Infection	8.173571e-01	0.088
R-HSA-2514853	Condensation of Prometaphase Chromosomes	8.226582e-01	0.085
R-HSA-433692	Proton-coupled monocarboxylate transport	8.226582e-01	0.085
R-HSA-3772470	Negative regulation of TCF-dependent signaling by WNT ligand antagonists	8.226582e-01	0.085
R-HSA-1234158	Regulation of gene expression by Hypoxia-inducible Factor	8.226582e-01	0.085
R-HSA-202670	ERKs are inactivated	8.226582e-01	0.085
R-HSA-162592	Integration of provirus	8.226582e-01	0.085
R-HSA-110362	POLB-Dependent Long Patch Base Excision Repair	8.226582e-01	0.085
R-HSA-69615	G1/S DNA Damage Checkpoints	8.255860e-01	0.083
R-HSA-5675482	Regulation of necroptotic cell death	8.262069e-01	0.083
R-HSA-73762	RNA Polymerase I Transcription Initiation	8.267822e-01	0.083
R-HSA-389948	Co-inhibition by PD-1	8.285165e-01	0.082
R-HSA-8939236	RUNX1 regulates transcription of genes involved in differentiation of HSCs	8.300934e-01	0.081
R-HSA-9639288	Amino acids regulate mTORC1	8.303117e-01	0.081
R-HSA-114608	Platelet degranulation	8.311847e-01	0.080
R-HSA-5654689	PI-3K cascade:FGFR1	8.325649e-01	0.080
R-HSA-6803529	FGFR2 alternative splicing	8.325649e-01	0.080
R-HSA-9670439	Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m...	8.325649e-01	0.080
R-HSA-112409	RAF-independent MAPK1/3 activation	8.325649e-01	0.080
R-HSA-212676	Dopamine Neurotransmitter Release Cycle	8.325649e-01	0.080
R-HSA-9669938	Signaling by KIT in disease	8.325649e-01	0.080
R-HSA-8964038	LDL clearance	8.325649e-01	0.080
R-HSA-2428924	IGF1R signaling cascade	8.352134e-01	0.078
R-HSA-9818027	NFE2L2 regulating anti-oxidant/detoxification enzymes	8.387988e-01	0.076
R-HSA-390471	Association of TriC/CCT with target proteins during biosynthesis	8.387988e-01	0.076
R-HSA-9754678	SARS-CoV-2 modulates host translation machinery	8.404346e-01	0.075
R-HSA-6781827	Transcription-Coupled Nucleotide Excision Repair (TC-NER)	8.407511e-01	0.075
R-HSA-9865114	Maple Syrup Urine Disease	8.419818e-01	0.075
R-HSA-3000484	Scavenging by Class F Receptors	8.419818e-01	0.075
R-HSA-9028731	Activated NTRK2 signals through FRS2 and FRS3	8.419818e-01	0.075
R-HSA-179812	GRB2 events in EGFR signaling	8.419818e-01	0.075
R-HSA-9634285	Constitutive Signaling by Overexpressed ERBB2	8.419818e-01	0.075
R-HSA-418890	Role of second messengers in netrin-1 signaling	8.419818e-01	0.075
R-HSA-8866427	VLDLR internalisation and degradation	8.419818e-01	0.075
R-HSA-380615	Serotonin clearance from the synaptic cleft	8.419818e-01	0.075
R-HSA-73943	Reversal of alkylation damage by DNA dioxygenases	8.419818e-01	0.075
R-HSA-9842663	Signaling by LTK	8.419818e-01	0.075
R-HSA-1679131	Trafficking and processing of endosomal TLR	8.419818e-01	0.075
R-HSA-879415	Advanced glycosylation endproduct receptor signaling	8.419818e-01	0.075
R-HSA-877312	Regulation of IFNG signaling	8.419818e-01	0.075
R-HSA-1247673	Erythrocytes take up oxygen and release carbon dioxide	8.419818e-01	0.075
R-HSA-2404192	Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)	8.444084e-01	0.073
R-HSA-9006931	Signaling by Nuclear Receptors	8.446129e-01	0.073
R-HSA-912526	Interleukin receptor SHC signaling	8.467465e-01	0.072
R-HSA-167160	RNA Pol II CTD phosphorylation and interaction with CE during HIV infection	8.467465e-01	0.072
R-HSA-77075	RNA Pol II CTD phosphorylation and interaction with CE	8.467465e-01	0.072
R-HSA-977068	Termination of O-glycan biosynthesis	8.467465e-01	0.072
R-HSA-400451	Free fatty acids regulate insulin secretion	8.467465e-01	0.072
R-HSA-9648895	Response of EIF2AK1 (HRI) to heme deficiency	8.467465e-01	0.072
R-HSA-982772	Growth hormone receptor signaling	8.467465e-01	0.072
R-HSA-375280	Amine ligand-binding receptors	8.486409e-01	0.071
R-HSA-9735869	SARS-CoV-1 modulates host translation machinery	8.505941e-01	0.070
R-HSA-392518	Signal amplification	8.505941e-01	0.070
R-HSA-110328	Recognition and association of DNA glycosylase with site containing an affected ...	8.505941e-01	0.070
R-HSA-5607761	Dectin-1 mediated noncanonical NF-kB signaling	8.586661e-01	0.066
R-HSA-4608870	Asymmetric localization of PCP proteins	8.586661e-01	0.066
R-HSA-9029558	NR1H2 & NR1H3 regulate gene expression linked to lipogenesis	8.592009e-01	0.066
R-HSA-170660	Adenylate cyclase activating pathway	8.592009e-01	0.066
R-HSA-6788467	IL-6-type cytokine receptor ligand interactions	8.592009e-01	0.066
R-HSA-6804759	Regulation of TP53 Activity through Association with Co-factors	8.592009e-01	0.066
R-HSA-8949664	Processing of SMDT1	8.592009e-01	0.066
R-HSA-389359	CD28 dependent Vav1 pathway	8.592009e-01	0.066
R-HSA-6811555	PI5P Regulates TP53 Acetylation	8.592009e-01	0.066
R-HSA-75892	Platelet Adhesion to exposed collagen	8.592009e-01	0.066
R-HSA-1059683	Interleukin-6 signaling	8.592009e-01	0.066
R-HSA-181430	Norepinephrine Neurotransmitter Release Cycle	8.598269e-01	0.066
R-HSA-6783589	Interleukin-6 family signaling	8.598269e-01	0.066
R-HSA-174113	SCF-beta-TrCP mediated degradation of Emi1	8.616297e-01	0.065
R-HSA-5654696	Downstream signaling of activated FGFR2	8.616297e-01	0.065
R-HSA-5654687	Downstream signaling of activated FGFR1	8.616297e-01	0.065
R-HSA-8854050	FBXL7 down-regulates AURKA during mitotic entry and in early mitosis	8.616297e-01	0.065
R-HSA-447115	Interleukin-12 family signaling	8.617077e-01	0.065
R-HSA-383280	Nuclear Receptor transcription pathway	8.649070e-01	0.063
R-HSA-112399	IRS-mediated signalling	8.678534e-01	0.062
R-HSA-9645723	Diseases of programmed cell death	8.688206e-01	0.061
R-HSA-9679191	Potential therapeutics for SARS	8.693366e-01	0.061
R-HSA-5654695	PI-3K cascade:FGFR2	8.718774e-01	0.060
R-HSA-203927	MicroRNA (miRNA) biogenesis	8.718774e-01	0.060
R-HSA-3000157	Laminin interactions	8.718774e-01	0.060
R-HSA-2160916	Hyaluronan degradation	8.718774e-01	0.060
R-HSA-432720	Lysosome Vesicle Biogenesis	8.719426e-01	0.060
R-HSA-9659379	Sensory processing of sound	8.722594e-01	0.059
R-HSA-5654227	Phospholipase C-mediated cascade; FGFR3	8.745446e-01	0.058
R-HSA-9859138	BCKDH synthesizes BCAA-CoA from KIC, KMVA, KIV	8.745446e-01	0.058
R-HSA-177504	Retrograde neurotrophin signalling	8.745446e-01	0.058
R-HSA-8847993	ERBB2 Activates PTK6 Signaling	8.745446e-01	0.058
R-HSA-1483115	Hydrolysis of LPC	8.745446e-01	0.058
R-HSA-9828642	Respiratory syncytial virus genome transcription	8.745446e-01	0.058
R-HSA-8963896	HDL assembly	8.745446e-01	0.058
R-HSA-1482798	Acyl chain remodeling of CL	8.745446e-01	0.058
R-HSA-435354	Zinc transporters	8.745446e-01	0.058
R-HSA-76005	Response to elevated platelet cytosolic Ca2+	8.746368e-01	0.058
R-HSA-1236974	ER-Phagosome pathway	8.756321e-01	0.058
R-HSA-6782135	Dual incision in TC-NER	8.760627e-01	0.057
R-HSA-8957275	Post-translational protein phosphorylation	8.793553e-01	0.056
R-HSA-69206	G1/S Transition	8.806797e-01	0.055
R-HSA-110331	Cleavage of the damaged purine	8.815692e-01	0.055
R-HSA-202424	Downstream TCR signaling	8.821502e-01	0.054
R-HSA-9865118	Diseases of branched-chain amino acid catabolism	8.829671e-01	0.054
R-HSA-1660514	Synthesis of PIPs at the Golgi membrane	8.829671e-01	0.054
R-HSA-5357769	Caspase activation via extrinsic apoptotic signalling pathway	8.829671e-01	0.054
R-HSA-1236975	Antigen processing-Cross presentation	8.832596e-01	0.054
R-HSA-69202	Cyclin E associated events during G1/S transition	8.842987e-01	0.053
R-HSA-69306	DNA Replication	8.846512e-01	0.053
R-HSA-9634597	GPER1 signaling	8.854011e-01	0.053
R-HSA-112316	Neuronal System	8.867501e-01	0.052
R-HSA-9673770	Signaling by PDGFRA extracellular domain mutants	8.882170e-01	0.051
R-HSA-9673767	Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants	8.882170e-01	0.051
R-HSA-2173791	TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)	8.882170e-01	0.051
R-HSA-170670	Adenylate cyclase inhibitory pathway	8.882170e-01	0.051
R-HSA-180336	SHC1 events in EGFR signaling	8.882170e-01	0.051
R-HSA-8964315	G beta:gamma signalling through BTK	8.882170e-01	0.051
R-HSA-5654228	Phospholipase C-mediated cascade; FGFR4	8.882170e-01	0.051
R-HSA-6785631	ERBB2 Regulates Cell Motility	8.882170e-01	0.051
R-HSA-110312	Translesion synthesis by REV1	8.882170e-01	0.051
R-HSA-171007	p38MAPK events	8.882170e-01	0.051
R-HSA-73942	DNA Damage Reversal	8.882170e-01	0.051
R-HSA-1502540	Signaling by Activin	8.882170e-01	0.051
R-HSA-9755779	SARS-CoV-2 targets host intracellular signalling and regulatory pathways	8.882170e-01	0.051
R-HSA-174362	Transport and metabolism of PAPS	8.882170e-01	0.051
R-HSA-8876725	Protein methylation	8.882170e-01	0.051
R-HSA-73927	Depurination	8.905456e-01	0.050
R-HSA-5213460	RIPK1-mediated regulated necrosis	8.905456e-01	0.050
R-HSA-5250913	Positive epigenetic regulation of rRNA expression	8.911449e-01	0.050
R-HSA-171306	Packaging Of Telomere Ends	8.931623e-01	0.049
R-HSA-73863	RNA Polymerase I Transcription Termination	8.931623e-01	0.049
R-HSA-264876	Insulin processing	8.931623e-01	0.049
R-HSA-69563	p53-Dependent G1 DNA Damage Response	8.932770e-01	0.049
R-HSA-69580	p53-Dependent G1/S DNA damage checkpoint	8.932770e-01	0.049
R-HSA-9009391	Extra-nuclear estrogen signaling	8.968121e-01	0.047
R-HSA-9793380	Formation of paraxial mesoderm	8.981303e-01	0.047
R-HSA-5668541	TNFR2 non-canonical NF-kB pathway	8.984296e-01	0.047
R-HSA-9707564	Cytoprotection by HMOX1	8.984296e-01	0.047
R-HSA-9820965	Respiratory syncytial virus (RSV) genome replication, transcription and translat...	8.989074e-01	0.046
R-HSA-5656121	Translesion synthesis by POLI	9.004000e-01	0.046
R-HSA-9603798	Class I peroxisomal membrane protein import	9.004000e-01	0.046
R-HSA-9733458	Induction of Cell-Cell Fusion	9.004000e-01	0.046
R-HSA-6803207	TP53 Regulates Transcription of Caspase Activators and Caspases	9.004000e-01	0.046
R-HSA-140534	Caspase activation via Death Receptors in the presence of ligand	9.004000e-01	0.046
R-HSA-5635838	Activation of SMO	9.004000e-01	0.046
R-HSA-9754706	Atorvastatin ADME	9.004000e-01	0.046
R-HSA-5655253	Signaling by FGFR2 in disease	9.006737e-01	0.045
R-HSA-167158	Formation of the HIV-1 Early Elongation Complex	9.025263e-01	0.045
R-HSA-113418	Formation of the Early Elongation Complex	9.025263e-01	0.045
R-HSA-76002	Platelet activation, signaling and aggregation	9.035079e-01	0.044
R-HSA-375165	NCAM signaling for neurite out-growth	9.046881e-01	0.044
R-HSA-73779	RNA Polymerase II Transcription Pre-Initiation And Promoter Opening	9.066889e-01	0.043
R-HSA-451927	Interleukin-2 family signaling	9.066889e-01	0.043
R-HSA-9604323	Negative regulation of NOTCH4 signaling	9.066889e-01	0.043
R-HSA-1251985	Nuclear signaling by ERBB4	9.066889e-01	0.043
R-HSA-72086	mRNA Capping	9.111189e-01	0.040
R-HSA-2892247	POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation	9.112559e-01	0.040
R-HSA-8964616	G beta:gamma signalling through CDC42	9.112559e-01	0.040
R-HSA-5655862	Translesion synthesis by POLK	9.112559e-01	0.040
R-HSA-5576893	Phase 2 - plateau phase	9.112559e-01	0.040
R-HSA-1566977	Fibronectin matrix formation	9.112559e-01	0.040
R-HSA-1963640	GRB2 events in ERBB2 signaling	9.112559e-01	0.040
R-HSA-9702518	STAT5 activation downstream of FLT3 ITD mutants	9.112559e-01	0.040
R-HSA-432047	Passive transport by Aquaporins	9.112559e-01	0.040
R-HSA-3134975	Regulation of innate immune responses to cytosolic DNA	9.112559e-01	0.040
R-HSA-1483148	Synthesis of PG	9.112559e-01	0.040
R-HSA-70370	Galactose catabolism	9.112559e-01	0.040
R-HSA-196783	Coenzyme A biosynthesis	9.112559e-01	0.040
R-HSA-9931269	AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274)	9.141201e-01	0.039
R-HSA-74751	Insulin receptor signalling cascade	9.167060e-01	0.038
R-HSA-936837	Ion transport by P-type ATPases	9.167060e-01	0.038
R-HSA-5619507	Activation of HOX genes during differentiation	9.167600e-01	0.038
R-HSA-5617472	Activation of anterior HOX genes in hindbrain development during early embryogen...	9.167600e-01	0.038
R-HSA-8863795	Downregulation of ERBB2 signaling	9.189972e-01	0.037
R-HSA-5250924	B-WICH complex positively regulates rRNA expression	9.202142e-01	0.036
R-HSA-8948751	Regulation of PTEN stability and activity	9.202142e-01	0.036
R-HSA-167162	RNA Polymerase II HIV Promoter Escape	9.206443e-01	0.036
R-HSA-5610785	GLI3 is processed to GLI3R by the proteasome	9.206443e-01	0.036
R-HSA-5610783	Degradation of GLI2 by the proteasome	9.206443e-01	0.036
R-HSA-167161	HIV Transcription Initiation	9.206443e-01	0.036
R-HSA-75953	RNA Polymerase II Transcription Initiation	9.206443e-01	0.036
R-HSA-9615017	FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes	9.206443e-01	0.036
R-HSA-442660	SLC-mediated transport of neurotransmitters	9.206443e-01	0.036
R-HSA-5654219	Phospholipase C-mediated cascade: FGFR1	9.209291e-01	0.036
R-HSA-3229121	Glycogen storage diseases	9.209291e-01	0.036
R-HSA-139853	Elevation of cytosolic Ca2+ levels	9.209291e-01	0.036
R-HSA-2408550	Metabolism of ingested H2SeO4 and H2SeO3 into H2Se	9.209291e-01	0.036
R-HSA-9824443	Parasitic Infection Pathways	9.244454e-01	0.034
R-HSA-9658195	Leishmania infection	9.244454e-01	0.034
R-HSA-9692914	SARS-CoV-1-host interactions	9.254356e-01	0.034
R-HSA-73929	Base-Excision Repair, AP Site Formation	9.259176e-01	0.033
R-HSA-2129379	Molecules associated with elastic fibres	9.262146e-01	0.033
R-HSA-379716	Cytosolic tRNA aminoacylation	9.268817e-01	0.033
R-HSA-110329	Cleavage of the damaged pyrimidine	9.268817e-01	0.033
R-HSA-73928	Depyrimidination	9.268817e-01	0.033
R-HSA-9851695	Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes	9.279933e-01	0.032
R-HSA-9841922	MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi...	9.279933e-01	0.032
R-HSA-9818564	Epigenetic regulation of gene expression by MLL3 and MLL4 complexes	9.279933e-01	0.032
R-HSA-418217	G beta:gamma signalling through PLC beta	9.295484e-01	0.032
R-HSA-2564830	Cytosolic iron-sulfur cluster assembly	9.295484e-01	0.032
R-HSA-500657	Presynaptic function of Kainate receptors	9.295484e-01	0.032
R-HSA-416993	Trafficking of GluR2-containing AMPA receptors	9.295484e-01	0.032
R-HSA-428643	Organic anion transport by SLC5/17/25 transporters	9.295484e-01	0.032
R-HSA-210993	Tie2 Signaling	9.295484e-01	0.032
R-HSA-9679504	Translation of Replicase and Assembly of the Replication Transcription Complex	9.295484e-01	0.032
R-HSA-3214815	HDACs deacetylate histones	9.312511e-01	0.031
R-HSA-73776	RNA Polymerase II Promoter Escape	9.326660e-01	0.030
R-HSA-350562	Regulation of ornithine decarboxylase (ODC)	9.328217e-01	0.030
R-HSA-190236	Signaling by FGFR	9.330155e-01	0.030
R-HSA-2672351	Stimuli-sensing channels	9.333212e-01	0.030
R-HSA-5578775	Ion homeostasis	9.362348e-01	0.029
R-HSA-109606	Intrinsic Pathway for Apoptosis	9.362348e-01	0.029
R-HSA-163685	Integration of energy metabolism	9.363784e-01	0.029
R-HSA-110320	Translesion Synthesis by POLH	9.372286e-01	0.028
R-HSA-8851708	Signaling by FGFR2 IIIa TM	9.372286e-01	0.028
R-HSA-449836	Other interleukin signaling	9.372286e-01	0.028
R-HSA-1480926	O2/CO2 exchange in erythrocytes	9.372286e-01	0.028
R-HSA-1237044	Erythrocytes take up carbon dioxide and release oxygen	9.372286e-01	0.028
R-HSA-9913635	Strand-asynchronous mitochondrial DNA replication	9.372286e-01	0.028
R-HSA-2172127	DAP12 interactions	9.380258e-01	0.028
R-HSA-69236	G1 Phase	9.380258e-01	0.028
R-HSA-69231	Cyclin D associated events in G1	9.380258e-01	0.028
R-HSA-3214858	RMTs methylate histone arginines	9.380258e-01	0.028
R-HSA-5619115	Disorders of transmembrane transporters	9.391950e-01	0.027
R-HSA-76042	RNA Polymerase II Transcription Initiation And Promoter Clearance	9.429885e-01	0.025
R-HSA-9660821	ADORA2B mediated anti-inflammatory cytokines production	9.429885e-01	0.025
R-HSA-9824272	Somitogenesis	9.429885e-01	0.025
R-HSA-5654221	Phospholipase C-mediated cascade; FGFR2	9.440720e-01	0.025
R-HSA-391903	Eicosanoid ligand-binding receptors	9.440720e-01	0.025
R-HSA-163359	Glucagon signaling in metabolic regulation	9.443907e-01	0.025
R-HSA-1482788	Acyl chain remodelling of PC	9.443907e-01	0.025
R-HSA-114508	Effects of PIP2 hydrolysis	9.443907e-01	0.025
R-HSA-180534	Vpu mediated degradation of CD4	9.443907e-01	0.025
R-HSA-5223345	Miscellaneous transport and binding events	9.443907e-01	0.025
R-HSA-199220	Vitamin B5 (pantothenate) metabolism	9.443907e-01	0.025
R-HSA-9843940	Regulation of endogenous retroelements by KRAB-ZFP proteins	9.451123e-01	0.025
R-HSA-9660826	Purinergic signaling in leishmaniasis infection	9.475802e-01	0.023
R-HSA-9664424	Cell recruitment (pro-inflammatory response)	9.475802e-01	0.023
R-HSA-9033241	Peroxisomal protein import	9.492778e-01	0.023
R-HSA-2022090	Assembly of collagen fibrils and other multimeric structures	9.492778e-01	0.023
R-HSA-2142845	Hyaluronan metabolism	9.494381e-01	0.023
R-HSA-75815	Ubiquitin-dependent degradation of Cyclin D	9.494381e-01	0.023
R-HSA-349425	Autodegradation of the E3 ubiquitin ligase COP1	9.494381e-01	0.023
R-HSA-901042	Calnexin/calreticulin cycle	9.494381e-01	0.023
R-HSA-202040	G-protein activation	9.501696e-01	0.022
R-HSA-167044	Signalling to RAS	9.501696e-01	0.022
R-HSA-9931295	PD-L1(CD274) glycosylation and translocation to plasma membrane	9.501696e-01	0.022
R-HSA-1482925	Acyl chain remodelling of PG	9.501696e-01	0.022
R-HSA-9636383	Prevention of phagosomal-lysosomal fusion	9.501696e-01	0.022
R-HSA-983695	Antigen activates B Cell Receptor (BCR) leading to generation of second messenge...	9.513083e-01	0.022
R-HSA-1482839	Acyl chain remodelling of PE	9.540463e-01	0.020
R-HSA-381426	Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l...	9.554872e-01	0.020
R-HSA-5654706	FRS-mediated FGFR3 signaling	9.556028e-01	0.020
R-HSA-947581	Molybdenum cofactor biosynthesis	9.556028e-01	0.020
R-HSA-212300	PRC2 methylates histones and DNA	9.582512e-01	0.019
R-HSA-180585	Vif-mediated degradation of APOBEC3G	9.582512e-01	0.019
R-HSA-9845576	Glycosphingolipid transport	9.582512e-01	0.019
R-HSA-69205	G1/S-Specific Transcription	9.582512e-01	0.019
R-HSA-114604	GPVI-mediated activation cascade	9.582512e-01	0.019
R-HSA-1236394	Signaling by ERBB4	9.588414e-01	0.018
R-HSA-532668	N-glycan trimming in the ER and Calnexin/Calreticulin cycle	9.593700e-01	0.018
R-HSA-76071	RNA Polymerase III Transcription Initiation From Type 3 Promoter	9.604438e-01	0.018
R-HSA-5654712	FRS-mediated FGFR4 signaling	9.604438e-01	0.018
R-HSA-71384	Ethanol oxidation	9.604438e-01	0.018
R-HSA-6807062	Cholesterol biosynthesis via lathosterol	9.604438e-01	0.018
R-HSA-189200	Cellular hexose transport	9.604438e-01	0.018
R-HSA-9694676	Translation of Replicase and Assembly of the Replication Transcription Complex	9.604438e-01	0.018
R-HSA-2871809	FCERI mediated Ca+2 mobilization	9.604806e-01	0.018
R-HSA-1989781	PPARA activates gene expression	9.606805e-01	0.017
R-HSA-1296072	Voltage gated Potassium channels	9.620857e-01	0.017
R-HSA-4641257	Degradation of AXIN	9.620857e-01	0.017
R-HSA-9762114	GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2	9.620857e-01	0.017
R-HSA-400206	Regulation of lipid metabolism by PPARalpha	9.646165e-01	0.016
R-HSA-392451	G beta:gamma signalling through PI3Kgamma	9.647573e-01	0.016
R-HSA-8854691	Interleukin-20 family signaling	9.647573e-01	0.016
R-HSA-452723	Transcriptional regulation of pluripotent stem cells	9.655807e-01	0.015
R-HSA-1566948	Elastic fibre formation	9.655807e-01	0.015
R-HSA-1234176	Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha	9.657941e-01	0.015
R-HSA-9820952	Respiratory Syncytial Virus Infection Pathway	9.662875e-01	0.015
R-HSA-1234174	Cellular response to hypoxia	9.683156e-01	0.014
R-HSA-9821993	Replacement of protamines by nucleosomes in the male pronucleus	9.686006e-01	0.014
R-HSA-9703648	Signaling by FLT3 ITD and TKD mutants	9.686006e-01	0.014
R-HSA-428930	Thromboxane signalling through TP receptor	9.686006e-01	0.014
R-HSA-5669034	TNFs bind their physiological receptors	9.686006e-01	0.014
R-HSA-8963898	Plasma lipoprotein assembly	9.686006e-01	0.014
R-HSA-9692916	SARS-CoV-1 activates/modulates innate immune responses	9.686347e-01	0.014
R-HSA-1236978	Cross-presentation of soluble exogenous antigens (endosomes)	9.687646e-01	0.014
R-HSA-71336	Pentose phosphate pathway	9.687646e-01	0.014
R-HSA-8964043	Plasma lipoprotein clearance	9.687646e-01	0.014
R-HSA-9929356	GSK3B-mediated proteasomal degradation of PD-L1(CD274)	9.687646e-01	0.014
R-HSA-381771	Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)	9.687646e-01	0.014
R-HSA-427389	ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression	9.716636e-01	0.012
R-HSA-5654693	FRS-mediated FGFR1 signaling	9.720250e-01	0.012
R-HSA-420029	Tight junction interactions	9.720250e-01	0.012
R-HSA-389887	Beta-oxidation of pristanoyl-CoA	9.720250e-01	0.012
R-HSA-1912408	Pre-NOTCH Transcription and Translation	9.730476e-01	0.012
R-HSA-5625886	Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene...	9.743021e-01	0.011
R-HSA-9821002	Chromatin modifications during the maternal to zygotic transition (MZT)	9.743021e-01	0.011
R-HSA-5362768	Hh mutants are degraded by ERAD	9.743021e-01	0.011
R-HSA-9929491	SPOP-mediated proteasomal degradation of PD-L1(CD274)	9.743021e-01	0.011
R-HSA-9711123	Cellular response to chemical stress	9.748799e-01	0.011
R-HSA-1855183	Synthesis of IP2, IP, and Ins in the cytosol	9.750761e-01	0.011
R-HSA-3295583	TRP channels	9.750761e-01	0.011
R-HSA-70635	Urea cycle	9.750761e-01	0.011
R-HSA-2161522	Abacavir ADME	9.750761e-01	0.011
R-HSA-9845614	Sphingolipid catabolism	9.750761e-01	0.011
R-HSA-9637687	Suppression of phagosomal maturation	9.750761e-01	0.011
R-HSA-5218859	Regulated Necrosis	9.751043e-01	0.011
R-HSA-74752	Signaling by Insulin receptor	9.766374e-01	0.010
R-HSA-6809371	Formation of the cornified envelope	9.772787e-01	0.010
R-HSA-8949613	Cristae formation	9.777945e-01	0.010
R-HSA-202427	Phosphorylation of CD3 and TCR zeta chains	9.777945e-01	0.010
R-HSA-201451	Signaling by BMP	9.777945e-01	0.010
R-HSA-193807	Synthesis of bile acids and bile salts via 27-hydroxycholesterol	9.777945e-01	0.010
R-HSA-9828806	Maturation of hRSV A proteins	9.777945e-01	0.010
R-HSA-3299685	Detoxification of Reactive Oxygen Species	9.779146e-01	0.010
R-HSA-204005	COPII-mediated vesicle transport	9.788436e-01	0.009
R-HSA-381676	Glucagon-like Peptide-1 (GLP1) regulates insulin secretion	9.788848e-01	0.009
R-HSA-400508	Incretin synthesis, secretion, and inactivation	9.788848e-01	0.009
R-HSA-9833110	RSV-host interactions	9.795198e-01	0.009
R-HSA-5654700	FRS-mediated FGFR2 signaling	9.802167e-01	0.009
R-HSA-5576892	Phase 0 - rapid depolarisation	9.802167e-01	0.009
R-HSA-9757110	Prednisone ADME	9.802167e-01	0.009
R-HSA-77387	Insulin receptor recycling	9.802167e-01	0.009
R-HSA-9638334	Iron assimilation using enterobactin	9.802167e-01	0.009
R-HSA-5620971	Pyroptosis	9.802167e-01	0.009
R-HSA-5387390	Hh mutants abrogate ligand secretion	9.808686e-01	0.008
R-HSA-418360	Platelet calcium homeostasis	9.823747e-01	0.008
R-HSA-9674555	Signaling by CSF3 (G-CSF)	9.823747e-01	0.008
R-HSA-1592389	Activation of Matrix Metalloproteinases	9.823747e-01	0.008
R-HSA-9907900	Proteasome assembly	9.826710e-01	0.008
R-HSA-187577	SCF(Skp2)-mediated degradation of p27/p21	9.826710e-01	0.008
R-HSA-9909615	Regulation of PD-L1(CD274) Post-translational modification	9.833399e-01	0.007
R-HSA-168256	Immune System	9.835880e-01	0.007
R-HSA-1250196	SHC1 events in ERBB2 signaling	9.842975e-01	0.007
R-HSA-888590	GABA synthesis, release, reuptake and degradation	9.842975e-01	0.007
R-HSA-112311	Neurotransmitter clearance	9.842975e-01	0.007
R-HSA-432040	Vasopressin regulates renal water homeostasis via Aquaporins	9.843079e-01	0.007
R-HSA-5678895	Defective CFTR causes cystic fibrosis	9.843079e-01	0.007
R-HSA-72706	GTP hydrolysis and joining of the 60S ribosomal subunit	9.845075e-01	0.007
R-HSA-156827	L13a-mediated translational silencing of Ceruloplasmin expression	9.845075e-01	0.007
R-HSA-1474244	Extracellular matrix organization	9.845149e-01	0.007
R-HSA-379724	tRNA Aminoacylation	9.845408e-01	0.007
R-HSA-445717	Aquaporin-mediated transport	9.858719e-01	0.006
R-HSA-9820960	Respiratory syncytial virus (RSV) attachment and entry	9.860106e-01	0.006
R-HSA-9820448	Developmental Cell Lineages of the Exocrine Pancreas	9.869293e-01	0.006
R-HSA-109582	Hemostasis	9.869955e-01	0.006
R-HSA-192105	Synthesis of bile acids and bile salts	9.870026e-01	0.006
R-HSA-73854	RNA Polymerase I Promoter Clearance	9.871314e-01	0.006
R-HSA-382556	ABC-family proteins mediated transport	9.879400e-01	0.005
R-HSA-9694635	Translation of Structural Proteins	9.881692e-01	0.005
R-HSA-425410	Metal ion SLC transporters	9.883665e-01	0.005
R-HSA-68616	Assembly of the ORC complex at the origin of replication	9.888967e-01	0.005
R-HSA-159418	Recycling of bile acids and salts	9.888967e-01	0.005
R-HSA-5609975	Diseases associated with glycosylation precursor biosynthesis	9.888967e-01	0.005
R-HSA-73864	RNA Polymerase I Transcription	9.891268e-01	0.005
R-HSA-983712	Ion channel transport	9.895216e-01	0.005
R-HSA-189483	Heme degradation	9.901083e-01	0.004
R-HSA-9748787	Azathioprine ADME	9.904825e-01	0.004
R-HSA-5250941	Negative epigenetic regulation of rRNA expression	9.908247e-01	0.004
R-HSA-9772573	Late SARS-CoV-2 Infection Events	9.911481e-01	0.004
R-HSA-6814122	Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding	9.911877e-01	0.004
R-HSA-5686938	Regulation of TLR by endogenous ligand	9.911877e-01	0.004
R-HSA-70895	Branched-chain amino acid catabolism	9.913945e-01	0.004
R-HSA-5358346	Hedgehog ligand biogenesis	9.913945e-01	0.004
R-HSA-9664323	FCGR3A-mediated IL10 synthesis	9.916143e-01	0.004
R-HSA-3296482	Defects in vitamin and cofactor metabolism	9.921494e-01	0.003
R-HSA-73772	RNA Polymerase I Promoter Escape	9.922209e-01	0.003
R-HSA-72737	Cap-dependent Translation Initiation	9.924644e-01	0.003
R-HSA-72613	Eukaryotic Translation Initiation	9.924644e-01	0.003
R-HSA-163560	Triglyceride catabolism	9.930062e-01	0.003
R-HSA-1839126	FGFR2 mutant receptor activation	9.930062e-01	0.003
R-HSA-72689	Formation of a pool of free 40S subunits	9.935971e-01	0.003
R-HSA-416476	G alpha (q) signalling events	9.936336e-01	0.003
R-HSA-427359	SIRT1 negatively regulates rRNA expression	9.937695e-01	0.003
R-HSA-549127	SLC-mediated transport of organic cations	9.937695e-01	0.003
R-HSA-390247	Beta-oxidation of very long chain fatty acids	9.937695e-01	0.003
R-HSA-8948216	Collagen chain trimerization	9.937695e-01	0.003
R-HSA-9753281	Paracetamol ADME	9.942610e-01	0.002
R-HSA-427413	NoRC negatively regulates rRNA expression	9.943535e-01	0.002
R-HSA-6785470	tRNA processing in the mitochondrion	9.944495e-01	0.002
R-HSA-2046106	alpha-linolenic acid (ALA) metabolism	9.944495e-01	0.002
R-HSA-5576891	Cardiac conduction	9.945284e-01	0.002
R-HSA-194068	Bile acid and bile salt metabolism	9.948148e-01	0.002
R-HSA-499943	Interconversion of nucleotide di- and triphosphates	9.948562e-01	0.002
R-HSA-422356	Regulation of insulin secretion	9.949934e-01	0.002
R-HSA-1483166	Synthesis of PA	9.953191e-01	0.002
R-HSA-5621480	Dectin-2 family	9.953191e-01	0.002
R-HSA-2871837	FCERI mediated NF-kB activation	9.954257e-01	0.002
R-HSA-927802	Nonsense-Mediated Decay (NMD)	9.955695e-01	0.002
R-HSA-975957	Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)	9.955695e-01	0.002
R-HSA-8868766	rRNA processing in the mitochondrion	9.955951e-01	0.002
R-HSA-71240	Tryptophan catabolism	9.955951e-01	0.002
R-HSA-1912422	Pre-NOTCH Expression and Processing	9.959062e-01	0.002
R-HSA-9711097	Cellular response to starvation	9.959242e-01	0.002
R-HSA-73817	Purine ribonucleoside monophosphate biosynthesis	9.960760e-01	0.002
R-HSA-6791226	Major pathway of rRNA processing in the nucleolus and cytosol	9.961420e-01	0.002
R-HSA-352230	Amino acid transport across the plasma membrane	9.961850e-01	0.002
R-HSA-112310	Neurotransmitter release cycle	9.964688e-01	0.002
R-HSA-3000480	Scavenging by Class A Receptors	9.965044e-01	0.002
R-HSA-9683701	Translation of Structural Proteins	9.965044e-01	0.002
R-HSA-977443	GABA receptor activation	9.965569e-01	0.001
R-HSA-351202	Metabolism of polyamines	9.965569e-01	0.001
R-HSA-597592	Post-translational protein modification	9.968801e-01	0.001
R-HSA-991365	Activation of GABAB receptors	9.968861e-01	0.001
R-HSA-977444	GABA B receptor activation	9.968861e-01	0.001
R-HSA-9633012	Response of EIF2AK4 (GCN2) to amino acid deficiency	9.969617e-01	0.001
R-HSA-191273	Cholesterol biosynthesis	9.970753e-01	0.001
R-HSA-1268020	Mitochondrial protein import	9.971969e-01	0.001
R-HSA-9710421	Defective pyroptosis	9.972261e-01	0.001
R-HSA-9637690	Response of Mtb to phagocytosis	9.972261e-01	0.001
R-HSA-9678108	SARS-CoV-1 Infection	9.972438e-01	0.001
R-HSA-9925561	Developmental Lineage of Pancreatic Acinar Cells	9.973401e-01	0.001
R-HSA-8868773	rRNA processing in the nucleus and cytosol	9.973908e-01	0.001
R-HSA-9010553	Regulation of expression of SLITs and ROBOs	9.974122e-01	0.001
R-HSA-6790901	rRNA modification in the nucleus and cytosol	9.974714e-01	0.001
R-HSA-2142691	Synthesis of Leukotrienes (LT) and Eoxins (EX)	9.975290e-01	0.001
R-HSA-196741	Cobalamin (Cbl, vitamin B12) transport and metabolism	9.975290e-01	0.001
R-HSA-1474290	Collagen formation	9.977363e-01	0.001
R-HSA-3560782	Diseases associated with glycosaminoglycan metabolism	9.977988e-01	0.001
R-HSA-2299718	Condensation of Prophase Chromosomes	9.980392e-01	0.001
R-HSA-6781823	Formation of TC-NER Pre-Incision Complex	9.980392e-01	0.001
R-HSA-9861718	Regulation of pyruvate metabolism	9.980392e-01	0.001
R-HSA-1474228	Degradation of the extracellular matrix	9.980841e-01	0.001
R-HSA-2046104	alpha-linolenic (omega3) and linoleic (omega6) acid metabolism	9.982533e-01	0.001
R-HSA-9958863	SLC-mediated transport of amino acids	9.983284e-01	0.001
R-HSA-193368	Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol	9.983284e-01	0.001
R-HSA-196071	Metabolism of steroid hormones	9.983284e-01	0.001
R-HSA-70263	Gluconeogenesis	9.984441e-01	0.001
R-HSA-913709	O-linked glycosylation of mucins	9.984933e-01	0.001
R-HSA-2871796	FCERI mediated MAPK activation	9.985878e-01	0.001
R-HSA-380108	Chemokine receptors bind chemokines	9.986140e-01	0.001
R-HSA-75105	Fatty acyl-CoA biosynthesis	9.987765e-01	0.001
R-HSA-1483257	Phospholipid metabolism	9.988807e-01	0.000
R-HSA-3906995	Diseases associated with O-glycosylation of proteins	9.988976e-01	0.000
R-HSA-3000178	ECM proteoglycans	9.988976e-01	0.000
R-HSA-9864848	Complex IV assembly	9.989003e-01	0.000
R-HSA-9609507	Protein localization	9.990959e-01	0.000
R-HSA-8956320	Nucleotide biosynthesis	9.991274e-01	0.000
R-HSA-9954714	PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA	9.992399e-01	0.000
R-HSA-9824446	Viral Infection Pathways	9.992435e-01	0.000
R-HSA-418597	G alpha (z) signalling events	9.993077e-01	0.000
R-HSA-975956	Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)	9.993106e-01	0.000
R-HSA-418346	Platelet homeostasis	9.993673e-01	0.000
R-HSA-156842	Eukaryotic Translation Elongation	9.993748e-01	0.000
R-HSA-174824	Plasma lipoprotein assembly, remodeling, and clearance	9.993748e-01	0.000
R-HSA-8951664	Neddylation	9.993999e-01	0.000
R-HSA-9955298	SLC-mediated transport of organic anions	9.994707e-01	0.000
R-HSA-6783783	Interleukin-10 signaling	9.994707e-01	0.000
R-HSA-5619084	ABC transporter disorders	9.994707e-01	0.000
R-HSA-9772572	Early SARS-CoV-2 Infection Events	9.995108e-01	0.000
R-HSA-9954716	ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri...	9.995343e-01	0.000
R-HSA-6798695	Neutrophil degranulation	9.995460e-01	0.000
R-HSA-8979227	Triglyceride metabolism	9.995642e-01	0.000
R-HSA-8873719	RAB geranylgeranylation	9.996119e-01	0.000
R-HSA-5362517	Signaling by Retinoic Acid	9.996119e-01	0.000
R-HSA-977225	Amyloid fiber formation	9.996142e-01	0.000
R-HSA-211976	Endogenous sterols	9.996543e-01	0.000
R-HSA-1442490	Collagen degradation	9.996543e-01	0.000
R-HSA-9948299	Ribosome-associated quality control	9.996581e-01	0.000
R-HSA-72312	rRNA processing	9.997225e-01	0.000
R-HSA-446203	Asparagine N-linked glycosylation	9.997329e-01	0.000
R-HSA-163841	Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation	9.997957e-01	0.000
R-HSA-418555	G alpha (s) signalling events	9.998010e-01	0.000
R-HSA-6782315	tRNA modification in the nucleus and cytosol	9.998062e-01	0.000
R-HSA-8957322	Metabolism of steroids	9.998111e-01	0.000
R-HSA-2980736	Peptide hormone metabolism	9.998127e-01	0.000
R-HSA-70268	Pyruvate metabolism	9.998163e-01	0.000
R-HSA-196807	Nicotinate metabolism	9.998274e-01	0.000
R-HSA-9662851	Anti-inflammatory response favouring Leishmania parasite infection	9.998310e-01	0.000
R-HSA-9664433	Leishmania parasite growth and survival	9.998310e-01	0.000
R-HSA-156902	Peptide chain elongation	9.998348e-01	0.000
R-HSA-1650814	Collagen biosynthesis and modifying enzymes	9.998463e-01	0.000
R-HSA-9840310	Glycosphingolipid catabolism	9.998781e-01	0.000
R-HSA-1799339	SRP-dependent cotranslational protein targeting to membrane	9.998842e-01	0.000
R-HSA-9638482	Metal ion assimilation from the host	9.998914e-01	0.000
R-HSA-975634	Retinoid metabolism and transport	9.998914e-01	0.000
R-HSA-8978934	Metabolism of cofactors	9.998914e-01	0.000
R-HSA-189445	Metabolism of porphyrins	9.998914e-01	0.000
R-HSA-2029481	FCGR activation	9.999129e-01	0.000
R-HSA-5663084	Diseases of carbohydrate metabolism	9.999139e-01	0.000
R-HSA-9749641	Aspirin ADME	9.999139e-01	0.000
R-HSA-168249	Innate Immune System	9.999184e-01	0.000
R-HSA-9837999	Mitochondrial protein degradation	9.999218e-01	0.000
R-HSA-1222556	ROS and RNS production in phagocytes	9.999233e-01	0.000
R-HSA-202733	Cell surface interactions at the vascular wall	9.999259e-01	0.000
R-HSA-71403	Citric acid cycle (TCA cycle)	9.999317e-01	0.000
R-HSA-917937	Iron uptake and transport	9.999317e-01	0.000
R-HSA-72764	Eukaryotic Translation Termination	9.999369e-01	0.000
R-HSA-9954709	Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide	9.999369e-01	0.000
R-HSA-1296071	Potassium Channels	9.999433e-01	0.000
R-HSA-428157	Sphingolipid metabolism	9.999459e-01	0.000
R-HSA-2029485	Role of phospholipids in phagocytosis	9.999578e-01	0.000
R-HSA-6806667	Metabolism of fat-soluble vitamins	9.999659e-01	0.000
R-HSA-2408557	Selenocysteine synthesis	9.999669e-01	0.000
R-HSA-6805567	Keratinization	9.999670e-01	0.000
R-HSA-192823	Viral mRNA Translation	9.999733e-01	0.000
R-HSA-390918	Peroxisomal lipid metabolism	9.999759e-01	0.000
R-HSA-373080	Class B/2 (Secretin family receptors)	9.999893e-01	0.000
R-HSA-71387	Metabolism of carbohydrates and carbohydrate derivatives	9.999910e-01	0.000
R-HSA-2168880	Scavenging of heme from plasma	9.999953e-01	0.000
R-HSA-2730905	Role of LAT2/NTAL/LAB on calcium mobilization	9.999958e-01	0.000
R-HSA-1483206	Glycerophospholipid biosynthesis	9.999965e-01	0.000
R-HSA-388396	GPCR downstream signalling	9.999970e-01	0.000
R-HSA-163125	Post-translational modification: synthesis of GPI-anchored proteins	9.999985e-01	0.000
R-HSA-418594	G alpha (i) signalling events	9.999985e-01	0.000
R-HSA-2408522	Selenoamino acid metabolism	9.999987e-01	0.000
R-HSA-2173782	Binding and Uptake of Ligands by Scavenger Receptors	9.999993e-01	0.000
R-HSA-9717189	Sensory perception of taste	9.999993e-01	0.000
R-HSA-6803157	Antimicrobial peptides	9.999993e-01	0.000
R-HSA-5663205	Infectious disease	9.999995e-01	0.000
R-HSA-5173105	O-linked glycosylation	9.999997e-01	0.000
R-HSA-198933	Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	9.999997e-01	0.000
R-HSA-196849	Metabolism of water-soluble vitamins and cofactors	9.999997e-01	0.000
R-HSA-9635486	Infection with Mycobacterium tuberculosis	9.999998e-01	0.000
R-HSA-3781865	Diseases of glycosylation	9.999999e-01	0.000
R-HSA-9717207	Sensory perception of sweet, bitter, and umami (glutamate) taste	9.999999e-01	0.000
R-HSA-1660662	Glycosphingolipid metabolism	9.999999e-01	0.000
R-HSA-977606	Regulation of Complement cascade	9.999999e-01	0.000
R-HSA-372790	Signaling by GPCR	9.999999e-01	0.000
R-HSA-9824439	Bacterial Infection Pathways	9.999999e-01	0.000
R-HSA-1643685	Disease	9.999999e-01	0.000
R-HSA-2142753	Arachidonate metabolism	9.999999e-01	0.000
R-HSA-8956319	Nucleotide catabolism	9.999999e-01	0.000
R-HSA-425407	SLC-mediated transmembrane transport	9.999999e-01	0.000
R-HSA-9748784	Drug ADME	1.000000e+00	0.000
R-HSA-375276	Peptide ligand-binding receptors	1.000000e+00	0.000
R-HSA-1630316	Glycosaminoglycan metabolism	1.000000e+00	0.000
R-HSA-166658	Complement cascade	1.000000e+00	0.000
R-HSA-2187338	Visual phototransduction	1.000000e+00	0.000
R-HSA-15869	Metabolism of nucleotides	1.000000e+00	0.000
R-HSA-611105	Respiratory electron transport	1.000000e+00	0.000
R-HSA-72766	Translation	1.000000e+00	0.000
R-HSA-211897	Cytochrome P450 - arranged by substrate type	1.000000e+00	0.000
R-HSA-373076	Class A/1 (Rhodopsin-like receptors)	1.000000e+00	0.000
R-HSA-392499	Metabolism of proteins	1.000000e+00	0.000
R-HSA-196854	Metabolism of vitamins and cofactors	1.000000e+00	0.000
R-HSA-211945	Phase I - Functionalization of compounds	1.000000e+00	0.000
R-HSA-9640148	Infection with Enterobacteria	1.000000e+00	0.000
R-HSA-382551	Transport of small molecules	1.000000e+00	0.000
R-HSA-1428517	Aerobic respiration and respiratory electron transport	1.000000e+00	0.000
R-HSA-8978868	Fatty acid metabolism	1.000000e+00	0.000
R-HSA-5668914	Diseases of metabolism	1.000000e+00	0.000
R-HSA-9752946	Expression and translocation of olfactory receptors	1.000000e+00	-0.000
R-HSA-556833	Metabolism of lipids	1.000000e+00	-0.000
R-HSA-381753	Olfactory Signaling Pathway	1.000000e+00	-0.000
R-HSA-1430728	Metabolism	1.000000e+00	-0.000
R-HSA-500792	GPCR ligand binding	1.000000e+00	-0.000
R-HSA-9709957	Sensory Perception	1.000000e+00	-0.000
R-HSA-71291	Metabolism of amino acids and derivatives	1.000000e+00	-0.000
R-HSA-211859	Biological oxidations	1.000000e+00	-0.000

Download

kinase	JSD_mean	pearson_surrounding	kinase_max_IC_position	max_position_JSD
KIS	0.880	0.324	1	0.809
COT	0.879	0.264	2	0.897
GRK1	0.875	0.362	-2	0.869
MOS	0.870	0.291	1	0.890
CLK3	0.870	0.228	1	0.895
CK1E	0.866	0.447	-3	0.788
CK1D	0.865	0.477	-3	0.755
CDC7	0.864	0.120	1	0.864
IKKB	0.862	0.113	-2	0.769
MTOR	0.860	0.113	1	0.818
BMPR1B	0.860	0.278	1	0.834
GRK7	0.858	0.273	1	0.786
CK1A2	0.857	0.446	-3	0.755
GRK5	0.856	0.181	-3	0.827
NLK	0.854	0.144	1	0.901
GRK6	0.854	0.227	1	0.846
PRPK	0.853	-0.050	-1	0.847
DSTYK	0.853	0.037	2	0.907
ERK5	0.852	0.108	1	0.869
PIM3	0.851	0.014	-3	0.741
IKKA	0.851	0.078	-2	0.768
CDK1	0.851	0.228	1	0.775
RAF1	0.850	-0.004	1	0.834
GRK4	0.850	0.170	-2	0.879
CK1G1	0.849	0.367	-3	0.776
ATR	0.849	0.020	1	0.816
CAMK2G	0.848	0.002	2	0.834
BMPR2	0.847	-0.023	-2	0.891
SKMLCK	0.847	0.065	-2	0.859
MLK1	0.846	0.073	2	0.833
CDKL1	0.846	0.022	-3	0.701
HIPK4	0.846	0.097	1	0.866
NDR2	0.846	-0.026	-3	0.736
SRPK1	0.846	0.080	-3	0.661
PDHK4	0.844	-0.199	1	0.854
JNK3	0.844	0.213	1	0.784
TBK1	0.843	-0.076	1	0.722
GCN2	0.843	-0.142	2	0.822
CDK8	0.843	0.141	1	0.788
CAMK1B	0.843	-0.057	-3	0.747
IKKE	0.843	-0.060	1	0.719
DYRK2	0.843	0.158	1	0.821
CK1A	0.842	0.440	-3	0.696
JNK2	0.842	0.212	1	0.756
FAM20C	0.842	0.081	2	0.619
ACVR2B	0.841	0.167	-2	0.829
GRK2	0.840	0.158	-2	0.768
RIPK3	0.840	-0.009	3	0.765
TGFBR1	0.840	0.106	-2	0.845
CDKL5	0.840	0.027	-3	0.686
CHAK2	0.840	-0.002	-1	0.808
NEK6	0.839	-0.071	-2	0.864
P38B	0.839	0.208	1	0.768
ICK	0.838	0.054	-3	0.728
BMPR1A	0.838	0.198	1	0.809
HIPK2	0.838	0.187	1	0.751
DLK	0.838	0.057	1	0.825
ACVR2A	0.838	0.145	-2	0.814
GRK3	0.838	0.206	-2	0.740
CDK19	0.838	0.140	1	0.756
TGFBR2	0.838	-0.043	-2	0.827
CLK2	0.837	0.157	-3	0.658
NEK7	0.837	-0.109	-3	0.746
P38G	0.837	0.200	1	0.695
ALK4	0.837	0.079	-2	0.865
ERK1	0.837	0.187	1	0.757
PIM1	0.836	0.010	-3	0.700
RSK2	0.836	-0.016	-3	0.658
CDK18	0.836	0.175	1	0.743
MST4	0.836	-0.017	2	0.874
NIK	0.835	-0.109	-3	0.766
CDK5	0.835	0.166	1	0.814
NUAK2	0.835	-0.046	-3	0.733
ALK2	0.835	0.120	-2	0.859
PDHK1	0.834	-0.246	1	0.831
SRPK3	0.834	0.056	-3	0.648
ULK2	0.834	-0.219	2	0.801
MLK3	0.833	0.029	2	0.763
PRKD1	0.833	-0.055	-3	0.685
DAPK2	0.833	-0.064	-3	0.748
CAMLCK	0.833	-0.068	-2	0.837
ATM	0.833	-0.006	1	0.749
PKN3	0.833	-0.084	-3	0.711
P38A	0.832	0.165	1	0.821
CDK13	0.832	0.132	1	0.778
P38D	0.832	0.214	1	0.699
PKN2	0.832	-0.042	-3	0.728
SRPK2	0.831	0.034	-3	0.590
BCKDK	0.831	-0.130	-1	0.799
NDR1	0.831	-0.103	-3	0.721
HIPK1	0.831	0.145	1	0.832
HUNK	0.831	-0.128	2	0.835
TTBK2	0.831	-0.035	2	0.720
MASTL	0.831	-0.176	-2	0.821
WNK1	0.831	-0.099	-2	0.872
PRP4	0.831	0.134	-3	0.712
CLK4	0.830	0.068	-3	0.673
ANKRD3	0.830	-0.061	1	0.836
CDK3	0.830	0.176	1	0.718
CAMK2B	0.830	0.013	2	0.805
CDK7	0.830	0.104	1	0.802
CDK17	0.830	0.164	1	0.700
P90RSK	0.829	-0.058	-3	0.663
MEKK3	0.829	0.169	1	0.793
PLK1	0.829	-0.010	-2	0.811
GSK3A	0.829	0.170	4	0.557
MLK4	0.828	0.037	2	0.741
LATS1	0.828	0.001	-3	0.738
MARK4	0.828	-0.095	4	0.856
MAPKAPK2	0.828	-0.031	-3	0.618
CAMK2D	0.827	-0.097	-3	0.706
DYRK4	0.827	0.164	1	0.763
PRKD2	0.827	-0.054	-3	0.638
CK2A2	0.827	0.179	1	0.760
MLK2	0.827	-0.105	2	0.836
ERK2	0.827	0.144	1	0.793
CAMK2A	0.827	0.004	2	0.826
MEK1	0.826	-0.007	2	0.861
LATS2	0.826	-0.090	-5	0.691
TLK2	0.826	0.005	1	0.779
JNK1	0.826	0.189	1	0.750
AMPKA1	0.826	-0.103	-3	0.735
PKACG	0.826	-0.053	-2	0.716
AURC	0.826	-0.002	-2	0.634
YSK4	0.826	-0.036	1	0.762
CDK12	0.825	0.129	1	0.754
PKCD	0.825	-0.066	2	0.807
CDK2	0.824	0.095	1	0.833
ULK1	0.824	-0.219	-3	0.711
RIPK1	0.824	-0.138	1	0.791
NEK9	0.824	-0.184	2	0.852
PKR	0.824	-0.036	1	0.827
PASK	0.824	0.103	-3	0.765
P70S6KB	0.823	-0.087	-3	0.680
TSSK2	0.822	-0.089	-5	0.807
IRE1	0.822	-0.085	1	0.774
VRK2	0.822	-0.111	1	0.871
RSK4	0.822	-0.014	-3	0.643
RSK3	0.822	-0.089	-3	0.647
SMG1	0.822	-0.047	1	0.760
MAPKAPK3	0.821	-0.125	-3	0.645
CLK1	0.821	0.043	-3	0.632
CK2A1	0.820	0.182	1	0.742
PKACB	0.820	-0.002	-2	0.644
DYRK1A	0.820	0.084	1	0.839
CDK14	0.820	0.141	1	0.779
MST3	0.819	0.091	2	0.862
PRKX	0.819	0.020	-3	0.595
WNK3	0.819	-0.282	1	0.794
GSK3B	0.819	0.098	4	0.550
MSK2	0.819	-0.072	-3	0.650
PLK3	0.818	-0.057	2	0.796
GAK	0.818	0.172	1	0.850
MSK1	0.818	-0.024	-3	0.646
PKCB	0.818	-0.044	2	0.757
PAK1	0.818	-0.079	-2	0.768
AMPKA2	0.818	-0.109	-3	0.700
MEKK2	0.817	0.045	2	0.819
CDK16	0.817	0.148	1	0.715
TSSK1	0.817	-0.104	-3	0.744
DYRK1B	0.817	0.109	1	0.784
MYLK4	0.816	-0.036	-2	0.757
PKCG	0.816	-0.062	2	0.759
DNAPK	0.816	-0.027	1	0.686
CDK9	0.816	0.079	1	0.781
CDK10	0.816	0.142	1	0.768
NIM1	0.815	-0.152	3	0.793
DRAK1	0.815	-0.028	1	0.783
PKCA	0.815	-0.052	2	0.749
AURA	0.815	-0.011	-2	0.612
HIPK3	0.815	0.081	1	0.818
TAO3	0.814	0.031	1	0.790
CAMK4	0.814	-0.165	-3	0.707
MPSK1	0.814	0.061	1	0.794
DYRK3	0.813	0.080	1	0.827
MEK5	0.813	-0.101	2	0.843
QSK	0.813	-0.081	4	0.829
TLK1	0.813	-0.026	-2	0.864
CK1G3	0.813	0.404	-3	0.659
AKT2	0.812	-0.028	-3	0.593
BRAF	0.812	-0.104	-4	0.759
ZAK	0.812	-0.067	1	0.761
MAK	0.812	0.148	-2	0.765
PKCZ	0.811	-0.094	2	0.798
PINK1	0.810	-0.119	1	0.861
PAK3	0.810	-0.144	-2	0.759
AURB	0.810	-0.051	-2	0.630
CHAK1	0.810	-0.158	2	0.791
IRE2	0.810	-0.138	2	0.764
MNK2	0.810	-0.110	-2	0.759
MEKK1	0.810	-0.125	1	0.787
QIK	0.809	-0.171	-3	0.710
PRKD3	0.809	-0.104	-3	0.619
PAK2	0.809	-0.113	-2	0.754
PERK	0.808	-0.145	-2	0.860
GCK	0.808	0.071	1	0.805
NEK5	0.808	-0.105	1	0.803
PLK2	0.808	0.036	-3	0.725
PHKG1	0.808	-0.136	-3	0.712
PKCH	0.808	-0.109	2	0.741
MARK3	0.807	-0.074	4	0.789
NUAK1	0.807	-0.147	-3	0.665
SGK3	0.807	-0.073	-3	0.651
MNK1	0.807	-0.103	-2	0.767
SIK	0.807	-0.110	-3	0.647
NEK2	0.806	-0.206	2	0.830
PLK4	0.806	-0.125	2	0.648
PKG2	0.806	-0.070	-2	0.641
NEK11	0.806	-0.030	1	0.784
PIM2	0.806	-0.066	-3	0.635
TAK1	0.805	0.083	1	0.811
BRSK1	0.805	-0.130	-3	0.669
MST2	0.804	0.002	1	0.799
ERK7	0.804	0.048	2	0.567
MARK2	0.804	-0.103	4	0.751
MELK	0.804	-0.189	-3	0.671
CAMK1G	0.803	-0.098	-3	0.647
DCAMKL1	0.803	-0.114	-3	0.668
NEK8	0.802	-0.098	2	0.835
PAK6	0.801	-0.086	-2	0.679
HRI	0.801	-0.239	-2	0.853
CK1G2	0.801	0.360	-3	0.723
LKB1	0.800	-0.079	-3	0.723
HPK1	0.800	0.043	1	0.789
EEF2K	0.800	0.002	3	0.854
CDK6	0.800	0.113	1	0.756
CHK1	0.800	-0.207	-3	0.681
SMMLCK	0.799	-0.104	-3	0.699
CAMKK1	0.799	-0.147	-2	0.770
MAPKAPK5	0.799	-0.182	-3	0.604
TTBK1	0.799	-0.121	2	0.639
PDK1	0.799	-0.085	1	0.781
MINK	0.798	-0.008	1	0.778
BRSK2	0.798	-0.186	-3	0.683
PKACA	0.798	-0.046	-2	0.588
DAPK3	0.798	-0.039	-3	0.696
MARK1	0.798	-0.135	4	0.806
WNK4	0.797	-0.200	-2	0.863
DAPK1	0.796	-0.013	-3	0.690
IRAK4	0.796	-0.179	1	0.768
AKT1	0.796	-0.052	-3	0.603
TNIK	0.796	-0.020	3	0.880
TAO2	0.795	-0.128	2	0.864
SNRK	0.795	-0.260	2	0.699
PDHK4_TYR	0.794	0.284	2	0.905
PDHK3_TYR	0.794	0.187	4	0.926
CAMKK2	0.794	-0.161	-2	0.760
MOK	0.794	0.069	1	0.832
CDK4	0.794	0.094	1	0.744
SSTK	0.793	-0.114	4	0.814
MAP2K6_TYR	0.793	0.280	-1	0.879
MAP3K15	0.793	-0.094	1	0.746
KHS2	0.793	0.040	1	0.791
HGK	0.793	-0.071	3	0.878
YANK3	0.792	0.067	2	0.423
BMPR2_TYR	0.792	0.221	-1	0.900
DCAMKL2	0.791	-0.150	-3	0.678
PKCT	0.791	-0.131	2	0.748
PKCE	0.791	-0.055	2	0.744
PDHK1_TYR	0.790	0.249	-1	0.887
LRRK2	0.790	-0.155	2	0.865
TTK	0.789	0.065	-2	0.842
KHS1	0.789	-0.015	1	0.772
OSR1	0.789	0.037	2	0.819
MAP2K4_TYR	0.789	0.179	-1	0.869
VRK1	0.789	-0.133	2	0.856
P70S6K	0.789	-0.131	-3	0.592
MST1	0.788	-0.088	1	0.777
CAMK1D	0.788	-0.111	-3	0.572
MEKK6	0.788	-0.160	1	0.779
PKCI	0.788	-0.117	2	0.765
NEK4	0.787	-0.189	1	0.768
SGK1	0.787	-0.039	-3	0.526
ALPHAK3	0.786	0.080	-1	0.774
IRAK1	0.785	-0.280	-1	0.722
SLK	0.785	-0.087	-2	0.705
AKT3	0.785	-0.043	-3	0.540
NEK1	0.783	-0.195	1	0.774
PAK5	0.783	-0.112	-2	0.620
ROCK2	0.783	-0.062	-3	0.679
CHK2	0.782	-0.085	-3	0.534
PHKG2	0.782	-0.193	-3	0.670
STK33	0.782	-0.138	2	0.638
PAK4	0.781	-0.094	-2	0.628
TESK1_TYR	0.780	-0.054	3	0.900
PBK	0.780	-0.061	1	0.768
LOK	0.780	-0.158	-2	0.743
TXK	0.779	0.162	1	0.849
MAP2K7_TYR	0.778	-0.090	2	0.878
MRCKB	0.778	-0.085	-3	0.625
SBK	0.778	-0.051	-3	0.474
BUB1	0.778	-0.049	-5	0.767
YSK1	0.778	-0.132	2	0.825
MRCKA	0.777	-0.100	-3	0.640
PKMYT1_TYR	0.777	-0.081	3	0.867
PKN1	0.775	-0.127	-3	0.604
DMPK1	0.775	-0.048	-3	0.653
HASPIN	0.775	-0.036	-1	0.653
MEK2	0.774	-0.294	2	0.825
CAMK1A	0.773	-0.105	-3	0.547
PINK1_TYR	0.773	-0.126	1	0.840
RIPK2	0.773	-0.267	1	0.714
EPHA6	0.773	0.024	-1	0.880
FGR	0.772	0.052	1	0.842
SYK	0.772	0.263	-1	0.833
EPHB4	0.771	0.010	-1	0.840
FYN	0.770	0.164	-1	0.837
BLK	0.770	0.125	-1	0.844
LCK	0.770	0.102	-1	0.846
ASK1	0.768	-0.148	1	0.734
MYO3A	0.768	-0.077	1	0.770
PTK2	0.768	0.203	-1	0.861
MYO3B	0.768	-0.096	2	0.840
ABL2	0.768	0.010	-1	0.791
FER	0.767	-0.030	1	0.861
YES1	0.767	-0.005	-1	0.823
LIMK2_TYR	0.767	-0.148	-3	0.754
YANK2	0.766	0.084	2	0.437
HCK	0.766	0.021	-1	0.835
CSF1R	0.766	-0.041	3	0.791
INSRR	0.765	0.002	3	0.752
BIKE	0.765	-0.046	1	0.733
EPHA4	0.765	0.007	2	0.801
ROCK1	0.765	-0.088	-3	0.641
FLT1	0.765	0.107	-1	0.856
RET	0.765	-0.154	1	0.786
SRMS	0.764	-0.004	1	0.846
ABL1	0.763	-0.008	-1	0.779
KIT	0.763	0.002	3	0.794
CRIK	0.762	-0.086	-3	0.598
MET	0.762	0.048	3	0.782
JAK3	0.762	-0.050	1	0.766
ITK	0.761	-0.012	-1	0.797
TYK2	0.761	-0.211	1	0.778
MST1R	0.761	-0.169	3	0.813
JAK2	0.761	-0.149	1	0.776
ROS1	0.761	-0.148	3	0.775
TYRO3	0.761	-0.161	3	0.801
LIMK1_TYR	0.760	-0.257	2	0.866
EPHB1	0.760	-0.043	1	0.833
EPHB2	0.760	-0.007	-1	0.823
STLK3	0.760	-0.135	1	0.727
BMX	0.760	0.022	-1	0.723
NEK3	0.759	-0.290	1	0.731
KDR	0.758	-0.036	3	0.758
EPHB3	0.757	-0.053	-1	0.826
TAO1	0.757	-0.176	1	0.706
PKG1	0.756	-0.129	-2	0.548
FGFR2	0.755	-0.116	3	0.803
DDR1	0.755	-0.240	4	0.832
SRC	0.754	0.046	-1	0.810
ERBB2	0.753	-0.038	1	0.752
ZAP70	0.753	0.181	-1	0.750
TNK2	0.753	-0.123	3	0.755
LYN	0.752	-0.007	3	0.718
MERTK	0.752	-0.082	3	0.774
TEC	0.752	-0.067	-1	0.713
FGFR3	0.752	-0.038	3	0.773
FLT3	0.751	-0.150	3	0.795
EGFR	0.750	0.003	1	0.662
EPHA7	0.750	-0.051	2	0.799
WEE1_TYR	0.750	-0.078	-1	0.732
FRK	0.749	-0.040	-1	0.835
EPHA3	0.749	-0.084	2	0.771
JAK1	0.748	-0.125	1	0.720
BTK	0.748	-0.169	-1	0.747
PDGFRB	0.748	-0.226	3	0.805
EPHA8	0.747	-0.011	-1	0.828
FGFR4	0.747	0.005	-1	0.765
EPHA5	0.747	-0.024	2	0.784
AAK1	0.747	-0.014	1	0.636
ERBB4	0.746	0.080	1	0.694
NTRK1	0.746	-0.165	-1	0.813
MATK	0.746	-0.056	-1	0.713
FGFR1	0.745	-0.194	3	0.765
TNNI3K_TYR	0.745	-0.148	1	0.790
TEK	0.744	-0.198	3	0.734
NEK10_TYR	0.744	-0.202	1	0.671
PTK6	0.743	-0.203	-1	0.708
NTRK3	0.743	-0.114	-1	0.770
AXL	0.743	-0.205	3	0.776
INSR	0.742	-0.129	3	0.729
PTK2B	0.742	-0.070	-1	0.745
ALK	0.741	-0.184	3	0.712
FLT4	0.741	-0.148	3	0.757
LTK	0.740	-0.189	3	0.737
EPHA2	0.739	-0.009	-1	0.805
TNK1	0.738	-0.248	3	0.782
NTRK2	0.738	-0.220	3	0.756
CSK	0.737	-0.115	2	0.800
PDGFRA	0.737	-0.310	3	0.801
DDR2	0.736	-0.123	3	0.737
EPHA1	0.736	-0.182	3	0.757
IGF1R	0.733	-0.078	3	0.668
FES	0.721	-0.087	-1	0.694
MUSK	0.720	-0.187	1	0.652