Motif 856 (n=1,069)
Position-wise Probabilities
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| uniprot | genes | site | source | protein | function |
|---|---|---|---|---|---|
| A0A0B4J1R7 | BORCS7-ASMT | S46 | ochoa | BLOC-1-related complex subunit 7 | None |
| A0A1B0GU03 | None | S350 | ochoa | Cathepsin D (EC 3.4.23.5) | None |
| A0AVT1 | UBA6 | S951 | ochoa | Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Monocyte protein 4) (MOP-4) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2) | 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:35970836, PubMed:35986001). Specific for ubiquitin, does not activate ubiquitin-like peptides. Also activates UBD/FAT10 conjugation via adenylation of its C-terminal glycine (PubMed:17889673, PubMed:35970836, PubMed:35986001). Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility. {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759, ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:35970836, ECO:0000269|PubMed:35986001}. |
| A0JNW5 | BLTP3B | S1058 | 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}. |
| A1L170 | C1orf226 | S72 | ochoa | Uncharacterized protein C1orf226 | None |
| A1L390 | PLEKHG3 | S647 | 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}. |
| A6ND36 | FAM83G | S356 | ochoa|psp | 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}. |
| A6NDB9 | PALM3 | S544 | ochoa | Paralemmin-3 | ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}. |
| A6NMY6 | ANXA2P2 | S22 | ochoa | Putative annexin A2-like protein (Annexin A2 pseudogene 2) (Lipocortin II pseudogene) | Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. {ECO:0000250}. |
| A8K0R7 | ZNF839 | S670 | ochoa | Zinc finger protein 839 (Renal carcinoma antigen NY-REN-50) | None |
| B5ME19 | EIF3CL | S530 | ochoa | Eukaryotic translation initiation factor 3 subunit C-like protein | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. 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. 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. {ECO:0000250|UniProtKB:Q99613}. |
| D6RIA3 | C4orf54 | S687 | ochoa | Uncharacterized protein C4orf54 (Familial obliterative portal venopathy) | None |
| E9PCH4 | None | S1487 | ochoa | Rap guanine nucleotide exchange factor 6 | None |
| O00116 | AGPS | S589 | ochoa | Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Aging-associated gene 5 protein) (Alkylglycerone-phosphate synthase) | Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis. {ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9553082}. |
| O00124 | UBXN8 | S144 | ochoa | UBX domain-containing protein 8 (Reproduction 8 protein) (Rep-8 protein) (UBX domain-containing protein 6) | Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction. {ECO:0000269|PubMed:21949850}. |
| O00141 | SGK1 | S401 | 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}. |
| O00299 | CLIC1 | S163 | ochoa | Chloride intracellular channel protein 1 (Chloride channel ABP) (Glutaredoxin-like oxidoreductase CLIC1) (EC 1.8.-.-) (Glutathione-dependent dehydroascorbate reductase CLIC1) (EC 1.8.5.1) (Nuclear chloride ion channel 27) (NCC27) (Regulatory nuclear chloride ion channel protein) (hRNCC) | In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Reduces selenite and dehydroascorbate and may act as an antioxidant during oxidative stress response (PubMed:25581026, PubMed:37759794). Can insert into membranes and form voltage-dependent multi-ion conductive channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:10874038, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:16339885, ECO:0000269|PubMed:25581026, ECO:0000269|PubMed:37759794, ECO:0000269|PubMed:9139710}. |
| O00425 | IGF2BP3 | S243 | ochoa | Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (IGF-II mRNA-binding protein 3) (KH domain-containing protein overexpressed in cancer) (hKOC) (VICKZ family member 3) | RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152}. |
| O14513 | NCKAP5 | S128 | ochoa | Nck-associated protein 5 (NAP-5) (Peripheral clock protein) | None |
| O14595 | CTDSP2 | S56 | ochoa | Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2 (EC 3.1.3.16) (Nuclear LIM interactor-interacting factor 2) (NLI-interacting factor 2) (Protein OS-4) (Small C-terminal domain phosphatase 2) (Small CTD phosphatase 2) (SCP2) | Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas. {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}. |
| O14613 | CDC42EP2 | S101 | ochoa | Cdc42 effector protein 2 (Binder of Rho GTPases 1) | 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 in fibroblasts in a CDC42-dependent manner. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}. |
| O14646 | CHD1 | S471 | 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}. |
| O14908 | GIPC1 | S225 | ochoa | PDZ domain-containing protein GIPC1 (GAIP C-terminus-interacting protein) (RGS-GAIP-interacting protein) (RGS19-interacting protein 1) (Synectin) (Tax interaction protein 2) (TIP-2) | May be involved in G protein-linked signaling. |
| O14924 | RGS12 | S195 | 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}. |
| O14924 | RGS12 | S715 | 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}. |
| O14936 | CASK | S151 | psp | Peripheral plasma membrane protein CASK (hCASK) (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) (Protein lin-2 homolog) | Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (PubMed:18423203). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). {ECO:0000250|UniProtKB:O70589, ECO:0000269|PubMed:18423203}. |
| O14981 | BTAF1 | S1479 | ochoa | TATA-binding protein-associated factor 172 (EC 3.6.4.-) (ATP-dependent helicase BTAF1) (B-TFIID transcription factor-associated 170 kDa subunit) (TAF(II)170) (TBP-associated factor 172) (TAF-172) | Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner. |
| O14983 | ATP2A1 | S338 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2+)-ATPase 1) (EC 7.2.2.10) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) | Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (By similarity). Contributes to calcium sequestration involved in muscular excitation/contraction (PubMed:10914677). {ECO:0000250|UniProtKB:P04191, ECO:0000269|PubMed:10914677}. |
| O15014 | ZNF609 | S609 | 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}. |
| O15061 | SYNM | S699 | 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}. |
| O15063 | GARRE1 | S574 | ochoa | Granule associated Rac and RHOG effector protein 1 (GARRE1) | Acts as an effector of RAC1 (PubMed:31871319). Associates with 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 (PubMed:29395067). May also play a role in miRNA silencing machinery (PubMed:29395067). {ECO:0000269|PubMed:29395067, ECO:0000269|PubMed:31871319}. |
| O15117 | FYB1 | S558 | ochoa | FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein) | Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity). {ECO:0000250|UniProtKB:D3ZIE4, ECO:0000250|UniProtKB:O35601, ECO:0000269|PubMed:10747096, ECO:0000269|PubMed:15849195, ECO:0000269|PubMed:16980616}. |
| O15169 | AXIN1 | S511 | ochoa | Axin-1 (Axis inhibition protein 1) (hAxin) | Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (PubMed:16601693). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development (PubMed:17210684). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (PubMed:17210684). {ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17210684, ECO:0000269|PubMed:27098453, ECO:0000269|PubMed:28546513}. |
| O15400 | STX7 | S147 | 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. |
| O15409 | FOXP2 | S696 | ochoa | Forkhead box protein P2 (CAG repeat protein 44) (Trinucleotide repeat-containing gene 10 protein) | Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays a role in synapse formation by regulating SRPX2 levels. Involved in neural mechanisms mediating the development of speech and language. |
| O15503 | INSIG1 | S125 | psp | Insulin-induced gene 1 protein (INSIG-1) | Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR (PubMed:12202038, PubMed:12535518, PubMed:16168377, PubMed:16399501, PubMed:16606821, PubMed:32322062). Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:12202038, PubMed:16399501, PubMed:26311497, PubMed:32322062). Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum (PubMed:32322062). In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi (PubMed:15899885, PubMed:32322062). Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:26311497, PubMed:32322062). Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139 (PubMed:12535518, PubMed:16168377, PubMed:22143767). Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78 (PubMed:28604676). {ECO:0000269|PubMed:12202038, ECO:0000269|PubMed:12535518, ECO:0000269|PubMed:15899885, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16399501, ECO:0000269|PubMed:16606821, ECO:0000269|PubMed:22143767, ECO:0000269|PubMed:26311497, ECO:0000269|PubMed:28604676, ECO:0000269|PubMed:32322062}. |
| O15553 | MEFV | S242 | ochoa|psp | Pyrin (Marenostrin) | Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:16037825, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:26347139, PubMed:27030597, PubMed:28835462). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). {ECO:0000250|UniProtKB:Q9JJ26, ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:16037825, ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:28835462}. |
| O43164 | PJA2 | S342 | psp | E3 ubiquitin-protein ligase Praja-2 (Praja2) (EC 2.3.2.27) (RING finger protein 131) (RING-type E3 ubiquitin transferase Praja-2) | Has E2-dependent E3 ubiquitin-protein ligase activity (PubMed:12036302, PubMed:21423175). Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes (PubMed:21423175). Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype (PubMed:28471450). Plays a role in ciliogenesis by ubiquitinating OFD1 (PubMed:33934390). {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:28471450, ECO:0000269|PubMed:33934390}. |
| O43166 | SIPA1L1 | S1366 | 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}. |
| O43379 | WDR62 | S614 | 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}. |
| O43543 | XRCC2 | S247 | psp | DNA repair protein XRCC2 (X-ray repair cross-complementing protein 2) | Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:21276791, ECO:0000269|PubMed:23149936, ECO:0000269|PubMed:27233470}. |
| O43561 | LAT | S209 | 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}. |
| O43598 | DNPH1 | S28 | ochoa | 5-hydroxymethyl-dUMP N-hydrolase (EC 3.2.2.-) (2'-deoxynucleoside 5'-phosphate N-hydrolase 1) (c-Myc-responsive protein RCL) | Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118). {ECO:0000269|PubMed:33833118}. |
| O43670 | ZNF207 | S361 | ochoa | BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (hBuGZ) (Zinc finger protein 207) | Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly (PubMed:24462186, PubMed:24462187, PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187). Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187). {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187, ECO:0000269|PubMed:26388440}. |
| O43752 | STX6 | S129 | 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}. |
| O43852 | CALU | S35 | ochoa | Calumenin (Crocalbin) (IEF SSP 9302) | Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250}. |
| O43933 | PEX1 | S1216 | ochoa | Peroxisomal ATPase PEX1 (EC 3.6.4.-) (Peroxin-1) (Peroxisome biogenesis disorder protein 1) (Peroxisome biogenesis factor 1) | Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:11439091, PubMed:16314507, PubMed:16854980, PubMed:21362118, PubMed:29884772). Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (PubMed:29884772). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (PubMed:29884772). {ECO:0000269|PubMed:11439091, ECO:0000269|PubMed:16314507, ECO:0000269|PubMed:16854980, ECO:0000269|PubMed:21362118, ECO:0000269|PubMed:29884772}. |
| O60260 | PRKN | S101 | psp | E3 ubiquitin-protein ligase parkin (Parkin) (EC 2.3.2.31) (Parkin RBR E3 ubiquitin-protein ligase) (Parkinson juvenile disease protein 2) (Parkinson disease protein 2) | Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539). {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23685073, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:33499712}. |
| O60292 | SIPA1L3 | S204 | 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}. |
| O60315 | ZEB2 | S641 | 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}. |
| O60333 | KIF1B | S649 | ochoa | Kinesin-like protein KIF1B (Klp) (EC 5.6.1.3) | Has a plus-end-directed microtubule motor activity and functions as a motor for transport of vesicles and organelles along microtubules. {ECO:0000269|PubMed:16225668}.; FUNCTION: [Isoform 2]: Has a plus-end-directed microtubule motor activity and functions as a motor for anterograde synaptic vesicle transport along axonal microtubules from the cell body to the presynapse in neuronal cells (By similarity). Functions as a downstream effector in a developmental apoptotic pathway that is activated when nerve growth factor (NGF) becomes limiting for neuronal progenitor cells (PubMed:18334619). {ECO:0000250|UniProtKB:Q60575, ECO:0000269|PubMed:18334619}.; FUNCTION: [Isoform 3]: Has a plus-end-directed microtubule motor activity and functions as a motor for anterograde transport of mitochondria. {ECO:0000269|PubMed:16225668}. |
| O60437 | PPL | S1670 | ochoa | Periplakin (190 kDa paraneoplastic pemphigus antigen) (195 kDa cornified envelope precursor protein) | Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling. {ECO:0000269|PubMed:9412476}. |
| O60488 | ACSL4 | S352 | ochoa | Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4) | Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590). {ECO:0000250|UniProtKB:O35547, ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233}. |
| O60610 | DIAPH1 | S154 | psp | Protein diaphanous homolog 1 (Diaphanous-related formin-1) (DRF1) | Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (By similarity). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (By similarity). Required for cytokinesis, and transcriptional activation of the serum response factor (By similarity). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells (PubMed:20937854, PubMed:21834987, PubMed:26912466). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854, PubMed:21834987). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (PubMed:20937854, PubMed:21834987). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854, PubMed:21834987). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (PubMed:20937854, PubMed:21834987). Plays a role in brain development (PubMed:24781755). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (By similarity). {ECO:0000250|UniProtKB:O08808, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24781755, ECO:0000269|PubMed:26912466}. |
| O60701 | UGDH | S88 | ochoa | UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) | Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). {ECO:0000250|UniProtKB:O70475, ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21961565, ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:25478983, ECO:0000269|PubMed:27966912, ECO:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329, ECO:0000269|PubMed:32001716}. |
| O60701 | UGDH | S275 | ochoa | UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) | Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). {ECO:0000250|UniProtKB:O70475, ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21961565, ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:25478983, ECO:0000269|PubMed:27966912, ECO:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329, ECO:0000269|PubMed:32001716}. |
| O60716 | CTNND1 | S300 | 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}. |
| O60759 | CYTIP | S222 | ochoa | Cytohesin-interacting protein (Cytohesin binder and regulator) (CYBR) (Cytohesin-associated scaffolding protein) (CASP) (Cytohesin-binding protein HE) (Cbp HE) (Pleckstrin homology Sec7 and coiled-coil domains-binding protein) | By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm. |
| O60763 | USO1 | S717 | ochoa | General vesicular transport factor p115 (Protein USO1 homolog) (Transcytosis-associated protein) (TAP) (Vesicle-docking protein) | General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity. {ECO:0000250|UniProtKB:P41542}. |
| O75140 | DEPDC5 | S579 | 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}. |
| O75154 | RAB11FIP3 | S348 | psp | Rab11 family-interacting protein 3 (FIP3) (FIP3-Rab11) (Rab11-FIP3) (Arfophilin-1) (EF hands-containing Rab-interacting protein) (Eferin) (MU-MB-17.148) | Downstream effector molecule for Rab11 GTPase which is involved in endocytic trafficking, cytokinesis and intracellular ciliogenesis by participating in membrane delivery (PubMed:15601896, PubMed:16148947, PubMed:17394487, PubMed:17628206, PubMed:18511905, PubMed:19327867, PubMed:20026645, PubMed:25673879, PubMed:26258637, PubMed:31204173). Recruited by Rab11 to endosomes where it links Rab11 to dynein motor complex (PubMed:20026645). The functional Rab11-RAB11FIP3-dynein complex regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endocytic recycling compartment (ERC) during interphase of cell cycle (PubMed:17394487, PubMed:20026645). Facilitates the interaction between dynein and dynactin and activates dynein processivity (PubMed:25035494). Binding with ASAP1 is needed to regulate the pericentrosomal localization of recycling endosomes (By similarity). The Rab11-RAB11FIP3 complex is also implicated in the transport during telophase of vesicles derived from recycling endosomes to the cleavage furrow via centrosome-anchored microtubules, where the vesicles function to deliver membrane during late cytokinesis and abscission (PubMed:15601896, PubMed:16148947). The recruitment of Rab11-RAB11FIP3-containing endosomes to the cleavage furrow and tethering to the midbody is co-mediated by RAB11FIP3 interaction with ARF6-exocyst and RACGAP1-MKLP1 tethering complexes (PubMed:17628206, PubMed:18511905). Also involved in the Rab11-Rabin8-Rab8 ciliogenesis cascade by facilitating the orderly assembly of a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which directs preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:26258637, PubMed:31204173). Also promotes the activity of Rab11 and ASAP1 in the ARF4-dependent Golgi-to-cilia transport of the sensory receptor rhodopsin (PubMed:25673879). Competes with WDR44 for binding to Rab11, which controls intracellular ciliogenesis pathway (PubMed:31204173). May play a role in breast cancer cell motility by regulating actin cytoskeleton (PubMed:19327867). {ECO:0000250|UniProtKB:Q8CHD8, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19327867, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26258637, ECO:0000269|PubMed:31204173}. |
| O75154 | RAB11FIP3 | S451 | psp | Rab11 family-interacting protein 3 (FIP3) (FIP3-Rab11) (Rab11-FIP3) (Arfophilin-1) (EF hands-containing Rab-interacting protein) (Eferin) (MU-MB-17.148) | Downstream effector molecule for Rab11 GTPase which is involved in endocytic trafficking, cytokinesis and intracellular ciliogenesis by participating in membrane delivery (PubMed:15601896, PubMed:16148947, PubMed:17394487, PubMed:17628206, PubMed:18511905, PubMed:19327867, PubMed:20026645, PubMed:25673879, PubMed:26258637, PubMed:31204173). Recruited by Rab11 to endosomes where it links Rab11 to dynein motor complex (PubMed:20026645). The functional Rab11-RAB11FIP3-dynein complex regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endocytic recycling compartment (ERC) during interphase of cell cycle (PubMed:17394487, PubMed:20026645). Facilitates the interaction between dynein and dynactin and activates dynein processivity (PubMed:25035494). Binding with ASAP1 is needed to regulate the pericentrosomal localization of recycling endosomes (By similarity). The Rab11-RAB11FIP3 complex is also implicated in the transport during telophase of vesicles derived from recycling endosomes to the cleavage furrow via centrosome-anchored microtubules, where the vesicles function to deliver membrane during late cytokinesis and abscission (PubMed:15601896, PubMed:16148947). The recruitment of Rab11-RAB11FIP3-containing endosomes to the cleavage furrow and tethering to the midbody is co-mediated by RAB11FIP3 interaction with ARF6-exocyst and RACGAP1-MKLP1 tethering complexes (PubMed:17628206, PubMed:18511905). Also involved in the Rab11-Rabin8-Rab8 ciliogenesis cascade by facilitating the orderly assembly of a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which directs preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:26258637, PubMed:31204173). Also promotes the activity of Rab11 and ASAP1 in the ARF4-dependent Golgi-to-cilia transport of the sensory receptor rhodopsin (PubMed:25673879). Competes with WDR44 for binding to Rab11, which controls intracellular ciliogenesis pathway (PubMed:31204173). May play a role in breast cancer cell motility by regulating actin cytoskeleton (PubMed:19327867). {ECO:0000250|UniProtKB:Q8CHD8, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19327867, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26258637, ECO:0000269|PubMed:31204173}. |
| O75376 | NCOR1 | S1143 | 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}. |
| O75391 | SPAG7 | S63 | ochoa | Sperm-associated antigen 7 | None |
| O75533 | SF3B1 | S72 | ochoa | Splicing factor 3B subunit 1 (Pre-mRNA-splicing factor SF3b 155 kDa subunit) (SF3b155) (Spliceosome-associated protein 155) (SAP 155) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, 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:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B1 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). 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). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). {ECO:0000250|UniProtKB:Q99NB9, 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}. |
| O75533 | SF3B1 | S73 | ochoa | Splicing factor 3B subunit 1 (Pre-mRNA-splicing factor SF3b 155 kDa subunit) (SF3b155) (Spliceosome-associated protein 155) (SAP 155) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, 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:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B1 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). 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). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). {ECO:0000250|UniProtKB:Q99NB9, 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}. |
| O75582 | RPS6KA5 | S376 | ochoa|psp | Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RSKL) | 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 factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes (PubMed:11909979, PubMed:12569367, PubMed:12763138, PubMed:18511904, PubMed:9687510, PubMed:9873047). Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin (PubMed:11909979, PubMed:9873047). Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression (PubMed:12628924, PubMed:18511904). In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress (PubMed:12628924). In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential (PubMed:12763138). Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation (PubMed:12569367). Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A (PubMed:15010469). 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 (PubMed:12773393). May also phosphorylate 'Ser-28' of histone H3 (PubMed:12773393). Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14) (PubMed:12773393). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines (By similarity). 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 (By similarity). Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (PubMed:25851810). {ECO:0000250|UniProtKB:Q8C050, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12569367, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:18511904, ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}. |
| O75643 | SNRNP200 | S835 | ochoa | U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13) (Activating signal cointegrator 1 complex subunit 3-like 1) (BRR2 homolog) (U5 snRNP-specific 200 kDa protein) (U5-200KD) | Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (PubMed:35241646). Plays a role in pre-mRNA splicing as a core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:35241646, ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711, ECO:0000305|PubMed:33509932}. |
| O75694 | NUP155 | S914 | ochoa | Nuclear pore complex protein Nup155 (155 kDa nucleoporin) (Nucleoporin Nup155) | Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}. |
| O75914 | PAK3 | S120 | ochoa | Serine/threonine-protein kinase PAK 3 (EC 2.7.11.1) (Beta-PAK) (Oligophrenin-3) (p21-activated kinase 3) (PAK-3) | Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as a downstream effector of the small GTPases CDC42 and RAC1. 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. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). {ECO:0000250|UniProtKB:Q61036, ECO:0000269|PubMed:21177870}. |
| O75962 | TRIO | S520 | ochoa | Triple functional domain protein (EC 2.7.11.1) (PTPRF-interacting protein) | Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases (PubMed:22155786, PubMed:27418539, PubMed:8643598). Involved in coordinating actin remodeling, which is necessary for cell migration and growth (PubMed:10341202, PubMed:22155786). Plays a key role in the regulation of neurite outgrowth and lamellipodia formation (PubMed:32109419). In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (By similarity). {ECO:0000250|UniProtKB:F1M0Z1, ECO:0000269|PubMed:10341202, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:27418539, ECO:0000269|PubMed:32109419, ECO:0000269|PubMed:8643598}. |
| O94778 | AQP8 | S21 | ochoa | Aquaporin-8 (AQP-8) | Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues (PubMed:15948717, PubMed:18948439, PubMed:23541115, PubMed:26972385, PubMed:29732408, PubMed:30579780). The transport of the ammonia neutral form induces a parallel transport of proton, at alkaline pH when the concentration of ammonia is high (By similarity). However, it is unclear whether the transport of proton takes place via the aquaporin or via an endogenous pathway (By similarity). Also, may transport ammonia analogs such as formamide and methylamine, a transport favourited at basic pH due to the increase of unprotonated (neutral) form, which is expected to favor diffusion (PubMed:15948717). Does not transport urea or glycerol (PubMed:15948717). The water transport mechanism is mercury- and copper-sensitive and passive in response to osmotic driving forces (PubMed:15948717). At the canicular plasma membrane, mediates the osmotic transport of water toward the bile canaliculus and facilitates the cAMP-induced bile canalicular water secretion, a process involved in bile formation (PubMed:18948439). In addition, mediates the hydrogen peroxide release from hepatocyte mitochondria that modulates the SREBF2-mediated cholesterol synthesis and facilitates the mitochondrial ammonia uptake which is metabolized into urea, mainly under glucagon stimulation (PubMed:30579780, PubMed:34292591). In B cells, transports the CYBB-generated hydrogen peroxide from the external leaflet of the plasma membrane to the cytosol to promote B cell activation and differentiation for signal amplification (By similarity). In the small intestine and colon system, mediates water transport through mitochondria and apical membrane of epithelial cells (By similarity). May play an important role in the adaptive response of proximal tubule cells to acidosis possibly by facilitating the mitochondrial ammonia transport (PubMed:22622463). {ECO:0000250|UniProtKB:P56404, ECO:0000250|UniProtKB:P56405, ECO:0000269|PubMed:15948717, ECO:0000269|PubMed:18948439, ECO:0000269|PubMed:22622463, ECO:0000269|PubMed:23541115, ECO:0000269|PubMed:26972385, ECO:0000269|PubMed:29732408, ECO:0000269|PubMed:30579780, ECO:0000269|PubMed:34292591}. |
| O94906 | PRPF6 | S279 | ochoa | Pre-mRNA-processing factor 6 (Androgen receptor N-terminal domain-transactivating protein 1) (ANT-1) (PRP6 homolog) (U5 snRNP-associated 102 kDa protein) (U5-102 kDa protein) | Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:20118938, PubMed:21549338, PubMed:28781166). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:20118938, ECO:0000269|PubMed:21549338, ECO:0000269|PubMed:28781166}. |
| O94915 | FRYL | S1928 | 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 | S1197 | psp | 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}. |
| O94953 | KDM4B | S352 | ochoa|psp | Lysine-specific demethylase 4B (EC 1.14.11.66) (JmjC domain-containing histone demethylation protein 3B) (Jumonji domain-containing protein 2B) ([histone H3]-trimethyl-L-lysine(9) demethylase 4B) | Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate (PubMed:16603238, PubMed:28262558). Plays a critical role in the development of the central nervous system (CNS). {ECO:0000250|UniProtKB:Q91VY5, ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:28262558}. |
| O94955 | RHOBTB3 | S215 | ochoa | Rho-related BTB domain-containing protein 3 (EC 3.6.1.-) | Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9. {ECO:0000269|PubMed:19490898}. |
| O94967 | WDR47 | S344 | ochoa | WD repeat-containing protein 47 (Neuronal enriched MAP-interacting protein) (Nemitin) | None |
| O94967 | WDR47 | S374 | ochoa | WD repeat-containing protein 47 (Neuronal enriched MAP-interacting protein) (Nemitin) | None |
| O94967 | WDR47 | S422 | ochoa | WD repeat-containing protein 47 (Neuronal enriched MAP-interacting protein) (Nemitin) | None |
| O95071 | UBR5 | S2080 | 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 | S2241 | 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}. |
| O95180 | CACNA1H | S44 | ochoa | Voltage-dependent T-type calcium channel subunit alpha-1H (Low-voltage-activated calcium channel alpha1 3.2 subunit) (Voltage-gated calcium channel subunit alpha Cav3.2) | Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation (PubMed:27149520, PubMed:9670923, PubMed:9930755). T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle (Probable). They may also be involved in the modulation of firing patterns of neurons (PubMed:15048902). In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia (PubMed:25907736, PubMed:27729216). {ECO:0000269|PubMed:24277868, ECO:0000269|PubMed:25907736, ECO:0000269|PubMed:27149520, ECO:0000269|PubMed:27729216, ECO:0000269|PubMed:9670923, ECO:0000269|PubMed:9930755, ECO:0000305, ECO:0000305|PubMed:15048902}. |
| O95229 | ZWINT | S81 | ochoa | Outer kinetochore KNL1 complex subunit ZWINT (ZW10 interactor) (ZW10-interacting protein 1) (Zwint-1) | 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:15094189, PubMed:15485811, PubMed:15824131, PubMed:16732327, PubMed:24530301, PubMed:27881301, PubMed:38459127, PubMed:38459128). 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:15094189, PubMed:15485811, PubMed:16732327). 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:15094189, PubMed:15485811, PubMed:15824131, PubMed:16732327, PubMed:24530301, PubMed:38459127, PubMed:38459128). Targets the RZZ complex to the kinetochore at prometaphase (PubMed:15485811). Recruits MAD2L1 to the kinetochore, but is not required for BUB1B localization (By similarity). 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 (PubMed:15485811). {ECO:0000250|UniProtKB:Q9CQU5, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:24530301, ECO:0000269|PubMed:27881301, ECO:0000269|PubMed:38459127, ECO:0000269|PubMed:38459128}. |
| O95235 | KIF20A | S61 | 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 | S556 | 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 | S757 | 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}. |
| O95239 | KIF4A | S1017 | ochoa | Chromosome-associated kinesin KIF4A (Chromokinesin-A) | Iron-sulfur (Fe-S) cluster binding motor protein that has a role in chromosome segregation during mitosis (PubMed:29848660). Translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis (PubMed:15297875, PubMed:15625105). May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity). {ECO:0000250|UniProtKB:P33174, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}. |
| O95251 | KAT7 | S403 | 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}. |
| O95259 | KCNH1 | S904 | ochoa | Voltage-gated delayed rectifier potassium channel KCNH1 (Ether-a-go-go potassium channel 1) (EAG channel 1) (h-eag) (hEAG1) (Potassium voltage-gated channel subfamily H member 1) (Voltage-gated potassium channel subunit Kv10.1) | Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel that mediates outward-rectifying potassium currents which, on depolarization, reaches a steady-state level and do not inactivate (PubMed:10880439, PubMed:11943152, PubMed:22732247, PubMed:25420144, PubMed:25556795, PubMed:25915598, PubMed:27005320, PubMed:27325704, PubMed:27618660, PubMed:30149017, PubMed:9738473). The activation kinetics depend on the prepulse potential and external divalent cation concentration (PubMed:11943152). With negative prepulses, the current activation is delayed and slowed down several fold, whereas more positive prepulses speed up activation (PubMed:11943152). The time course of activation is biphasic with a fast and a slowly activating current component (PubMed:11943152). Activates at more positive membrane potentials and exhibit a steeper activation curve (PubMed:11943152). Channel properties are modulated by subunit assembly (PubMed:11943152). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:25420144, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:25915598, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:30149017, ECO:0000269|PubMed:9738473}. |
| O95453 | PARN | S583 | ochoa | Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Deadenylating nuclease) (Deadenylation nuclease) (Polyadenylate-specific ribonuclease) | 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (PubMed:10882133, PubMed:11359775, PubMed:12748283, PubMed:15175153, PubMed:9736620). Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (PubMed:22442037, PubMed:25049417). {ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:22442037, ECO:0000269|PubMed:25049417, ECO:0000269|PubMed:9736620}. |
| O95573 | ACSL3 | S361 | ochoa | Fatty acid CoA ligase Acsl3 (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 3) (LACS 3) (Long-chain-fatty-acid--CoA ligase 3) (EC 6.2.1.3) (Medium-chain acyl-CoA ligase Acsl3) (EC 6.2.1.2) | Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (PubMed:18003621). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity (By similarity). {ECO:0000250|UniProtKB:Q63151, ECO:0000269|PubMed:18003621, ECO:0000269|PubMed:22633490}. |
| O95613 | PCNT | S1245 | 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}. |
| O95772 | STARD3NL | S39 | 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}. |
| O95793 | STAU1 | S390 | ochoa | Double-stranded RNA-binding protein Staufen homolog 1 | Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.; FUNCTION: (Microbial infection) Plays a role in virus particles production of many viruses including of HIV-1, HERV-K, ebola virus and influenza virus. Acts by interacting with various viral proteins involved in particle budding process. {ECO:0000269|PubMed:10325410, ECO:0000269|PubMed:18498651, ECO:0000269|PubMed:23926355, ECO:0000269|PubMed:30301857}. |
| O96028 | NSD2 | S30 | ochoa | Histone-lysine N-methyltransferase NSD2 (EC 2.1.1.357) (Multiple myeloma SET domain-containing protein) (MMSET) (Nuclear SET domain-containing protein 2) (Protein trithorax-5) (Wolf-Hirschhorn syndrome candidate 1 protein) | Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity). During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity). Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617). During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity). During B-cell development, required for the generation of the B1 lineage (By similarity). During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity). Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity). By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity). {ECO:0000250|UniProtKB:Q8BVE8, ECO:0000269|PubMed:16115125, ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:27571355, ECO:0000269|PubMed:29728617, ECO:0000269|PubMed:33941880}.; FUNCTION: [Isoform 1]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:22099308}.; FUNCTION: [Isoform 4]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:22099308). Methylation of histone H3 at 'Lys-27' is controversial (PubMed:18172012, PubMed:22099308). Mono-, di- or tri-methylates histone H3 at 'Lys-27' (H3K27me, H3K27me2 and H3K27me3) (PubMed:18172012). Does not methylate histone H3 at 'Lys-27' (PubMed:22099308). May act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment (PubMed:11152655, PubMed:18172012). {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:18172012, ECO:0000269|PubMed:22099308}. |
| P00338 | LDHA | S89 | ochoa | L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59) | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:11276087}. |
| P00367 | GLUD1 | S370 | psp | Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3) | Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:11032875, PubMed:11254391, PubMed:16023112, PubMed:16959573). Plays a role in insulin homeostasis (PubMed:11297618, PubMed:9571255). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). {ECO:0000250|UniProtKB:P10860, ECO:0000269|PubMed:11032875, ECO:0000269|PubMed:11254391, ECO:0000269|PubMed:11297618, ECO:0000269|PubMed:16023112, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:9571255}. |
| P01033 | TIMP1 | S178 | ochoa | Metalloproteinase inhibitor 1 (Erythroid-potentiating activity) (EPA) (Fibroblast collagenase inhibitor) (Collagenase inhibitor) (Tissue inhibitor of metalloproteinases 1) (TIMP-1) | Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. {ECO:0000269|PubMed:1420137, ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:17050530, ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}. |
| P01241 | GH1 | S132 | psp | Somatotropin (Growth hormone) (GH) (GH-N) (Growth hormone 1) (Pituitary growth hormone) | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
| P02144 | MB | S59 | ochoa | Myoglobin (Nitrite reductase MB) (EC 1.7.-.-) (Pseudoperoxidase MB) (EC 1.11.1.-) | Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218). {ECO:0000269|PubMed:30918256, ECO:0000269|PubMed:32891753, ECO:0000269|PubMed:34679218}. |
| P02511 | CRYAB | S76 | ochoa | Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Heat shock protein family B member 5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component) | May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P23927}. |
| P02545 | LMNA | S525 | ochoa|psp | 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}. |
| P02730 | SLC4A1 | S303 | psp | 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}. |
| P04004 | VTN | S386 | psp | 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. |
| P04035 | HMGCR | S420 | ochoa | 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) | Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is the main target of statins, a class of cholesterol-lowering drugs (PubMed:11349148, PubMed:18540668, PubMed:36745799). {ECO:0000269|PubMed:11349148, ECO:0000269|PubMed:18540668, ECO:0000269|PubMed:21357570, ECO:0000269|PubMed:2991281, ECO:0000269|PubMed:36745799, ECO:0000269|PubMed:6995544}. |
| P04049 | RAF1 | S359 | 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 | S471 | 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}. |
| P04114 | APOB | S1775 | ochoa | Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)] | Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. |
| P04183 | TK1 | S63 | ochoa | Thymidine kinase, cytosolic (EC 2.7.1.21) | Cell-cycle-regulated enzyme of importance in nucleotide metabolism (PubMed:9575153). Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate (PubMed:22385435). Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation in the intracellular dTTP concentration (Probable). Also important for the activation of anticancer and antiviral nucleoside analog prodrugs such as 1-b-d-arabinofuranosylcytosine (AraC) and 3c-azido-3c-deoxythymidine (AZT) (PubMed:22385435). {ECO:0000269|PubMed:22385435, ECO:0000269|PubMed:9575153, ECO:0000305|PubMed:17407781}. |
| P04406 | GAPDH | S210 | ochoa|psp | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. |
| P04406 | GAPDH | S292 | ochoa | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. |
| P04637 | TP53 | S183 | ochoa|psp | Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53) | Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:38653238, PubMed:9840937). Negatively regulates cell division by controlling expression of a set of genes required for this process (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:9840937). One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (PubMed:12524540, PubMed:17189187). Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:24652652, ECO:0000269|PubMed:35618207, ECO:0000269|PubMed:36634798, ECO:0000269|PubMed:38653238, ECO:0000269|PubMed:9840937}. |
| P05181 | CYP2E1 | S431 | psp | Cytochrome P450 2E1 (EC 1.14.14.1) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-J) | A cytochrome P450 monooxygenase involved in the metabolism of fatty acids (PubMed:10553002, PubMed:18577768). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10553002, PubMed:18577768). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids (PubMed:10553002, PubMed:18577768). May be involved in the oxidative metabolism of xenobiotics (Probable). {ECO:0000269|PubMed:10553002, ECO:0000269|PubMed:18577768, ECO:0000305|PubMed:9348445}. |
| P05198 | EIF2S1 | S158 | ochoa | Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha) (eIF2-alpha) | Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:16289705, PubMed:38340717). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC) (PubMed:16289705). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (PubMed:16289705). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (PubMed:16289705). EIF2S1/eIF2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF2-alpha in a global protein synthesis inhibitor, leading to an attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming (PubMed:19131336, PubMed:33384352, PubMed:38340717). EIF2S1/eIF2-alpha also acts as an activator of mitophagy in response to mitochondrial damage: phosphorylation by EIF2AK1/HRI promotes relocalization to the mitochondrial surface, thereby triggering PRKN-independent mitophagy (PubMed:38340717). {ECO:0000269|PubMed:16289705, ECO:0000269|PubMed:19131336, ECO:0000269|PubMed:33384352, ECO:0000269|PubMed:38340717}. |
| P05387 | RPLP2 | S44 | ochoa | Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Renal carcinoma antigen NY-REN-44) | Plays an important role in the elongation step of protein synthesis. |
| P06127 | CD5 | S454 | ochoa | T-cell surface glycoprotein CD5 (Lymphocyte antigen T1/Leu-1) (CD antigen CD5) | Lymphoid-specific receptor expressed by all T-cells and in a subset of B-cells known as B1a cells. Plays a role in the regulation of TCR and BCR signaling, thymocyte selection, T-cell effector differentiation and immune tolerance. Acts by interacting with several ligands expressed on B-cells such as CD5L or CD72 and thereby plays an important role in contact-mediated, T-dependent B-cell activation and in the maintenance of regulatory T and B-cell homeostasis. Functions as a negative regulator of TCR signaling during thymocyte development by associating with several signaling proteins including LCK, CD3Z chain, PI3K or CBL (PubMed:1384049, PubMed:1385158). Mechanistically, co-engagement of CD3 with CD5 enhances phosphorylated CBL recruitment leading to increased VAV1 phosphorylation and degradation (PubMed:23376399). Modulates B-cell biology through ERK1/2 activation in a Ca(2+)-dependent pathway via the non-selective Ca(2+) channel TRPC1, leading to IL-10 production (PubMed:27499044). {ECO:0000250|UniProtKB:P13379, ECO:0000269|PubMed:1384049, ECO:0000269|PubMed:1385158, ECO:0000269|PubMed:23376399, ECO:0000269|PubMed:27499044}. |
| P06748 | NPM1 | S243 | 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}. |
| P07101 | TH | S502 | ochoa | Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) | Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of catecholamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:15287903, PubMed:1680128, PubMed:17391063, PubMed:24753243, PubMed:34922205, PubMed:8528210, Ref.18). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P24529, ECO:0000269|PubMed:15287903, ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:17391063, ECO:0000269|PubMed:24753243, ECO:0000269|PubMed:34922205, ECO:0000269|PubMed:8528210, ECO:0000269|Ref.18}.; FUNCTION: [Isoform 5]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}.; FUNCTION: [Isoform 6]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}. |
| P07355 | ANXA2 | S22 | ochoa|psp | Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) | Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic surveillance and neoangiogenesis (By similarity). {ECO:0000250|UniProtKB:P07356, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.; FUNCTION: (Microbial infection) Binds M.pneumoniae CARDS toxin, probably serves as one receptor for this pathogen. When ANXA2 is down-regulated by siRNA, less toxin binds to human cells and less vacuolization (a symptom of M.pneumoniae infection) is seen. {ECO:0000269|PubMed:25139904}. |
| P08758 | ANXA5 | S295 | ochoa | Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CPB-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. |
| P09601 | HMOX1 | S241 | ochoa | Heme oxygenase 1 (HO-1) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 1 soluble form] | [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707). {ECO:0000269|PubMed:11121422, ECO:0000269|PubMed:19556236, ECO:0000269|PubMed:7703255, ECO:0000303|PubMed:20055707}.; FUNCTION: [Heme oxygenase 1]: (Microbial infection) During SARS-COV-2 infection, promotes SARS-CoV-2 ORF3A-mediated autophagy but is unlikely to be required for ORF3A-mediated induction of reticulophagy. {ECO:0000269|PubMed:35239449}.; FUNCTION: [Heme oxygenase 1 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:7703255}. |
| P09629 | HOXB7 | S132 | psp | Homeobox protein Hox-B7 (Homeobox protein HHO.C1) (Homeobox protein Hox-2C) | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
| P09651 | HNRNPA1 | S22 | 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}. |
| P09874 | PARP1 | S274 | ochoa | Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (DNA ADP-ribosyltransferase PARP1) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (Protein poly-ADP-ribosyltransferase PARP1) (EC 2.4.2.-) [Cleaved into: Poly [ADP-ribose] polymerase 1, processed C-terminus (Poly [ADP-ribose] polymerase 1, 89-kDa form); Poly [ADP-ribose] polymerase 1, processed N-terminus (NT-PARP-1) (Poly [ADP-ribose] polymerase 1, 24-kDa form) (Poly [ADP-ribose] polymerase 1, 28-kDa form)] | Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:26626479, PubMed:26626480, PubMed:30104678, PubMed:31796734, PubMed:32028527, PubMed:32241924, PubMed:32358582, PubMed:33186521, PubMed:34465625, PubMed:34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:19764761, PubMed:25043379, PubMed:28190768, PubMed:29954836, PubMed:35393539, PubMed:7852410, PubMed:9315851). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521, PubMed:34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:29954836, PubMed:30257210). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600, PubMed:34465625, PubMed:34874266). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed:33683197, PubMed:34732825, PubMed:34795260). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed:26344098, PubMed:30356214). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed:17396150, PubMed:19764761, PubMed:24906880, PubMed:34049076). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed:27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). 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). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed:15607977, PubMed:17177976, PubMed:19344625, PubMed:27256882, PubMed:32315358, PubMed:32844745, PubMed:35124853, PubMed:35393539, PubMed:35460603). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed:15607977, PubMed:22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed:27256882, PubMed:35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed:27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed:35393539). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed:33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed:32315358, PubMed:32844745, PubMed:35460603). Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed:35460603). Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). {ECO:0000250|UniProtKB:P11103, ECO:0000269|PubMed:15607977, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:19764761, ECO:0000269|PubMed:20388712, ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:26626479, ECO:0000269|PubMed:26626480, ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:27256882, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:27471034, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30257210, ECO:0000269|PubMed:30356214, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:32241924, ECO:0000269|PubMed:32315358, ECO:0000269|PubMed:32358582, ECO:0000269|PubMed:32844745, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:33412112, ECO:0000269|PubMed:33589610, ECO:0000269|PubMed:33683197, ECO:0000269|PubMed:34049076, ECO:0000269|PubMed:34465625, ECO:0000269|PubMed:34625544, ECO:0000269|PubMed:34732825, ECO:0000269|PubMed:34737271, ECO:0000269|PubMed:34795260, ECO:0000269|PubMed:34874266, ECO:0000269|PubMed:35124853, ECO:0000269|PubMed:35393539, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:7852410, ECO:0000269|PubMed:9315851}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed C-terminus]: Promotes AIFM1-mediated apoptosis (PubMed:33168626). This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis (PubMed:33168626). {ECO:0000269|PubMed:33168626}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed N-terminus]: This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis. {ECO:0000269|PubMed:35104452}. |
| P09917 | ALOX5 | S272 | psp | Polyunsaturated fatty acid 5-lipoxygenase (EC 1.13.11.-) (Arachidonate 5-lipoxygenase) (5-LO) (5-lipoxygenase) (EC 1.13.11.34) | Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMed:19022417, PubMed:21233389, PubMed:22516296, PubMed:23246375, PubMed:24282679, PubMed:24893149, PubMed:31664810, PubMed:8615788, PubMed:8631361). Also catalyzes the oxygenation of arachidonate into 8-hydroperoxyicosatetraenoate (8-HPETE) and 12-hydroperoxyicosatetraenoate (12-HPETE) (PubMed:23246375). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (PubMed:31664810). Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (PubMed:17114001, PubMed:21206090, PubMed:31664810, PubMed:32404334, PubMed:8615788). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma) (By similarity). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers (PubMed:31664810). In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (By similarity). Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21200133). May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK (By similarity). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P48999, ECO:0000269|PubMed:17114001, ECO:0000269|PubMed:19022417, ECO:0000269|PubMed:21200133, ECO:0000269|PubMed:21206090, ECO:0000269|PubMed:21233389, ECO:0000269|PubMed:22516296, ECO:0000269|PubMed:23246375, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:24893149, ECO:0000269|PubMed:31664810, ECO:0000269|PubMed:32404334, ECO:0000269|PubMed:8615788, ECO:0000269|PubMed:8631361}. |
| P0DMV8 | HSPA1A | S106 | ochoa | Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1) (Heat shock protein family A member 1A) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. 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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558). {ECO:0000250|UniProtKB:P0DMW0, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:9499401, ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. {ECO:0000269|PubMed:16537599}. |
| P0DMV9 | HSPA1B | S106 | ochoa | Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2) (Heat shock protein family A member 1B) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. 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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). {ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. {ECO:0000269|PubMed:16537599}. |
| P10398 | ARAF | S432 | psp | Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) (Proto-oncogene A-Raf-1) (Proto-oncogene Pks) | Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade. Phosphorylates PFKFB2 (PubMed:36402789). {ECO:0000269|PubMed:22609986, ECO:0000269|PubMed:36402789}.; FUNCTION: [Isoform 2]: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation. {ECO:0000269|PubMed:22609986}. |
| P10412 | H1-4 | S41 | ochoa | Histone H1.4 (Histone H1b) (Histone H1s-4) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P10721 | KIT | S746 | psp | Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Piebald trait protein) (PBT) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (p145 c-kit) (v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog) (CD antigen CD117) | Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12511554, ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9528781}. |
| P11308 | ERG | S39 | psp | 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. |
| P11836 | MS4A1 | S231 | ochoa | B-lymphocyte antigen CD20 (B-lymphocyte surface antigen B1) (Bp35) (Leukocyte surface antigen Leu-16) (Membrane-spanning 4-domains subfamily A member 1) (CD antigen CD20) | B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:12920111, PubMed:3925015, PubMed:7684739). Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR (PubMed:12920111, PubMed:18474602, PubMed:7684739). {ECO:0000269|PubMed:12920111, ECO:0000269|PubMed:18474602, ECO:0000269|PubMed:3925015, ECO:0000269|PubMed:7684739}. |
| P12081 | HARS1 | S27 | ochoa | Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS) | Catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP) (PubMed:29235198). Plays a role in axon guidance (PubMed:26072516). {ECO:0000269|PubMed:26072516, ECO:0000269|PubMed:29235198}. |
| P14550 | AKR1A1 | S211 | ochoa | Aldo-keto reductase family 1 member A1 (EC 1.1.1.2) (EC 1.1.1.372) (EC 1.1.1.54) (Alcohol dehydrogenase [NADP(+)]) (Aldehyde reductase) (Glucuronate reductase) (EC 1.1.1.19) (Glucuronolactone reductase) (EC 1.1.1.20) (S-nitroso-CoA reductase) (ScorR) (EC 1.6.-.-) | Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (PubMed:10510318, PubMed:30538128). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes (By similarity). Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN) (PubMed:11306097, PubMed:18276838). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (PubMed:30538128). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (PubMed:31649033). Displays no reductase activity towards retinoids (By similarity). {ECO:0000250|UniProtKB:P50578, ECO:0000250|UniProtKB:P51635, ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:11306097, ECO:0000269|PubMed:18276838, ECO:0000269|PubMed:30538128, ECO:0000269|PubMed:31649033}. |
| P15056 | BRAF | S467 | psp | 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}. |
| P15056 | BRAF | S579 | psp | 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}. |
| P15311 | EZR | S413 | ochoa | Ezrin (Cytovillin) (Villin-2) (p81) | Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. {ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19111582}. |
| P15822 | HIVEP1 | S1180 | 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. |
| P16157 | ANK1 | S759 | ochoa | Ankyrin-1 (ANK-1) (Ankyrin-R) (Erythrocyte ankyrin) | Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. {ECO:0000269|PubMed:12456646, ECO:0000269|PubMed:35835865}.; FUNCTION: [Isoform Mu17]: Together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. {ECO:0000269|PubMed:12527750}. |
| P16284 | PECAM1 | S686 | 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 | S157 | 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}. |
| P16402 | H1-3 | S42 | ochoa | Histone H1.3 (Histone H1c) (Histone H1s-2) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16403 | H1-2 | S41 | ochoa | Histone H1.2 (Histone H1c) (Histone H1d) (Histone H1s-1) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16615 | ATP2A2 | S338 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:O55143, ECO:0000269|PubMed:12542527, ECO:0000269|PubMed:16402920, ECO:0000269|PubMed:28890335}.; FUNCTION: [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation. {ECO:0000250|UniProtKB:O55143}. |
| P17600 | SYN1 | S391 | ochoa | Synapsin-1 (Brain protein 4.1) (Synapsin I) | Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity). {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951, ECO:0000269|PubMed:21441247, ECO:0000269|PubMed:23406870}. |
| P18206 | VCL | S345 | ochoa | Vinculin (Metavinculin) (MV) | Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}. |
| P18433 | PTPRA | S189 | psp | Receptor-type tyrosine-protein phosphatase alpha (Protein-tyrosine phosphatase alpha) (R-PTP-alpha) (EC 3.1.3.48) | Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (By similarity). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (By similarity). {ECO:0000250|UniProtKB:P18052}. |
| P18583 | SON | S55 | 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}. |
| P19525 | EIF2AK2 | S456 | ochoa|psp | 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}. |
| P21399 | ACO1 | S711 | psp | Cytoplasmic aconitate hydratase (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Ferritin repressor protein) (Iron regulatory protein 1) (IRP1) (Iron-responsive element-binding protein 1) (IRE-BP 1) | Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1281544, PubMed:1946430, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788). Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788). {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:8041788}.; FUNCTION: Conversely, when cellular iron levels are high, binds a 4Fe-4S cluster which precludes RNA binding activity and promotes the aconitase activity, the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788}. |
| P21399 | ACO1 | S778 | ochoa | Cytoplasmic aconitate hydratase (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Ferritin repressor protein) (Iron regulatory protein 1) (IRP1) (Iron-responsive element-binding protein 1) (IRE-BP 1) | Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1281544, PubMed:1946430, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788). Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788). {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:8041788}.; FUNCTION: Conversely, when cellular iron levels are high, binds a 4Fe-4S cluster which precludes RNA binding activity and promotes the aconitase activity, the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788}. |
| P21860 | ERBB3 | S1044 | ochoa | Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Tyrosine kinase-type cell surface receptor HER3) | Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (PubMed:20682778). May also be activated by CSPG5 (PubMed:15358134). Involved in the regulation of myeloid cell differentiation (PubMed:27416908). {ECO:0000269|PubMed:15358134, ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:27416908}. |
| P21860 | ERBB3 | S1315 | ochoa | Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Tyrosine kinase-type cell surface receptor HER3) | Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (PubMed:20682778). May also be activated by CSPG5 (PubMed:15358134). Involved in the regulation of myeloid cell differentiation (PubMed:27416908). {ECO:0000269|PubMed:15358134, ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:27416908}. |
| P22090 | RPS4Y1 | S204 | ochoa | Small ribosomal subunit protein eS4, Y isoform 1 (40S ribosomal protein S4) | None |
| P22466 | GAL | S76 | ochoa | Galanin peptides [Cleaved into: Galanin; Galanin message-associated peptide (GMAP)] | Endocrine hormone of the central and peripheral nervous systems that binds and activates the G protein-coupled receptors GALR1, GALR2, and GALR3. This small neuropeptide may regulate diverse physiologic functions including contraction of smooth muscle of the gastrointestinal and genitourinary tract, growth hormone and insulin release and adrenal secretion. {ECO:0000269|PubMed:1370155, ECO:0000269|PubMed:1722333, ECO:0000269|PubMed:25691535}. |
| P22626 | HNRNPA2B1 | S29 | ochoa | Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) | Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). 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). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}. |
| P23258 | TUBG1 | S131 | psp | Tubulin gamma-1 chain (Gamma-1-tubulin) (Gamma-tubulin complex component 1) (GCP-1) | Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:38609661, PubMed:39321809). Gamma-tubulin is a key component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation (PubMed:38305685, PubMed:38609661, PubMed:39321809). The gTuRC regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments, a critical step in centrosome duplication and spindle formation (PubMed:38305685, PubMed:38609661, PubMed:39321809). {ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661, ECO:0000269|PubMed:39321809}. |
| P23458 | JAK1 | S963 | ochoa | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1) | Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). Kinase partner for the interleukin (IL)-2 receptor (PubMed:11909529) as well as interleukin (IL)-10 receptor (PubMed:12133952). Kinase partner for the type I interferon receptor IFNAR2 (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins (PubMed:7759950). Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors (PubMed:16239216, PubMed:32750333, PubMed:8232552). {ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12133952, ECO:0000269|PubMed:16239216, ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7657660, ECO:0000269|PubMed:8232552}. |
| P23975 | SLC6A2 | S259 | psp | Sodium-dependent noradrenaline transporter (Norepinephrine transporter) (NET) (Solute carrier family 6 member 2) | Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline), the primary signaling neurotransmitter in the autonomic sympathetic nervous system (PubMed:2008212, PubMed:8125921, PubMed:38750358). Is responsible for norepinephrine re-uptake and clearance from the synaptic cleft, thus playing a crucial role in norepinephrine inactivation and homeostasis (By similarity). Can also mediate sodium- and chloride-dependent transport of dopamine (PubMed:11093780, PubMed:8125921, PubMed:39395208, PubMed:39048818). {ECO:0000250|UniProtKB:O55192, ECO:0000269|PubMed:11093780, ECO:0000269|PubMed:2008212, ECO:0000269|PubMed:38750358, ECO:0000269|PubMed:39048818, ECO:0000269|PubMed:8125921}. |
| P24864 | CCNE1 | S103 | ochoa|psp | G1/S-specific cyclin-E1 | Essential for the control of the cell cycle at the G1/S (start) transition. {ECO:0000269|PubMed:7739542}. |
| P25054 | APC | S127 | 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}. |
| P25490 | YY1 | S252 | ochoa | Transcriptional repressor protein YY1 (Delta transcription factor) (INO80 complex subunit S) (NF-E1) (Yin and yang 1) (YY-1) | Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence (PubMed:1655281). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed (PubMed:11158321). Involved in DNA repair (PubMed:18026119, PubMed:28575647). In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation (PubMed:28575647). Recruits the PR-DUB complex to specific gene-regulatory regions (PubMed:20805357). {ECO:0000269|PubMed:11158321, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:1655281, ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:20805357, ECO:0000269|PubMed:24326773, ECO:0000269|PubMed:25787250, ECO:0000269|PubMed:28575647}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements. {ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119}. |
| P26232 | CTNNA2 | S42 | ochoa | Catenin alpha-2 (Alpha N-catenin) (Alpha-catenin-related protein) | May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system (By similarity). Required for proper regulation of cortical neuronal migration and neurite growth (PubMed:30013181). It acts as a negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization (PubMed:30013181). It thereby suppresses excessive actin branching which would impair neurite growth and stability (PubMed:30013181). Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation (By similarity). {ECO:0000250|UniProtKB:Q61301, ECO:0000269|PubMed:30013181}. |
| P28290 | ITPRID2 | S98 | 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 | S687 | 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 | S428 | 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}. |
| P29350 | PTPN6 | S294 | ochoa | Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase) (Protein-tyrosine phosphatase 1C) (PTP-1C) (Protein-tyrosine phosphatase SHP-1) (SH-PTP1) | Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis (PubMed:14739280, PubMed:29925997). Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:21258366, PubMed:9733788). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:11907092, PubMed:14739280, PubMed:37932456, PubMed:38166031). Modulates the signaling of several cytokine receptors including IL-4 receptor (PubMed:9065461). Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling (PubMed:34811497, PubMed:38532423). Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Also acts as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A (PubMed:37595871). {ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:29925997, ECO:0000269|PubMed:34811497, ECO:0000269|PubMed:37595871, ECO:0000269|PubMed:37932456, ECO:0000269|PubMed:38166031, ECO:0000269|PubMed:38532423, ECO:0000269|PubMed:9065461, ECO:0000269|PubMed:9733788}. |
| P29466 | CASP1 | S376 | psp | Caspase-1 (CASP-1) (EC 3.4.22.36) (Interleukin-1 beta convertase) (IL-1BC) (Interleukin-1 beta-converting enzyme) (ICE) (IL-1 beta-converting enzyme) (p45) [Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10] | Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides (PubMed:15326478, PubMed:15498465, PubMed:1574116, PubMed:26375003, PubMed:32051255, PubMed:37993714, PubMed:7876192, PubMed:9334240). Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes (PubMed:15326478, PubMed:15498465, PubMed:1574116, PubMed:32051255, PubMed:7876192). Cleaves a tetrapeptide after an Asp residue at position P1 (PubMed:15498465, PubMed:1574116, PubMed:7876192). Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD (PubMed:26375003). In contrast to cleavage of interleukin IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32051255, PubMed:32109412, PubMed:32553275). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (PubMed:22464733). Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590). In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (PubMed:20197547). {ECO:0000269|PubMed:15326478, ECO:0000269|PubMed:15498465, ECO:0000269|PubMed:1574116, ECO:0000269|PubMed:20197547, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:32051255, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:32553275, ECO:0000269|PubMed:37993714, ECO:0000269|PubMed:7876192, ECO:0000269|PubMed:9334240}.; FUNCTION: [Isoform Delta]: Apoptosis inactive. {ECO:0000269|PubMed:7876192}.; FUNCTION: [Isoform Epsilon]: Apoptosis inactive. {ECO:0000269|PubMed:7876192}. |
| P30273 | FCER1G | S61 | ochoa | High affinity immunoglobulin epsilon receptor subunit gamma (Fc receptor gamma-chain) (FcRgamma) (Fc-epsilon RI-gamma) (IgE Fc receptor subunit gamma) (FceRI gamma) | Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils, priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation. {ECO:0000250|UniProtKB:P20491}. |
| P30305 | CDC25B | S465 | psp | M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) | Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner (PubMed:17332740). The three isoforms seem to have a different level of activity (PubMed:1836978). {ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. |
| P30414 | NKTR | S1061 | 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}. |
| P30566 | ADSL | S289 | ochoa | Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) | Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. {ECO:0000269|PubMed:10888601}. |
| P31274 | HOXC9 | S159 | ochoa | Homeobox protein Hox-C9 (Homeobox protein Hox-3B) | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
| P31645 | SLC6A4 | S277 | psp | Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) | Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation (PubMed:17506858, PubMed:18317590). Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity). {ECO:0000250|UniProtKB:P31652, ECO:0000250|UniProtKB:Q60857, ECO:0000269|PubMed:10407194, ECO:0000269|PubMed:12869649, ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:18317590, ECO:0000269|PubMed:21730057, ECO:0000269|PubMed:27049939, ECO:0000269|PubMed:27756841, ECO:0000269|PubMed:34851672}. |
| P31751 | AKT2 | S34 | ochoa | RAC-beta serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-2) (Protein kinase B beta) (PKB beta) (RAC protein kinase beta) (RAC-PK-beta) | Serine/threonine kinase closely related to AKT1 and AKT3. All 3 enzymes, AKT1, AKT2 and AKT3, are collectively known as AKT kinase. AKT regulates many processes including metabolism, proliferation, cell survival, growth and angiogenesis, through the phosphorylation of a range of downstream substrates. Over 100 substrates have been reported so far, although for most of them, the precise AKT kinase catalyzing the reaction was not specified. AKT regulates glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT also regulates the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT also regulates cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor 1 (IGF1). AKT mediates the antiapoptotic effects of IGF1. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development (PubMed:21432781, PubMed:21620960). In response to lysophosphatidic acid stimulation, inhibits the ciliogenesis cascade. In this context, phosphorylates WDR44, hence stabilizing its interaction with Rab11 and preventing the formation of the ciliogenic Rab11-FIP3-RAB3IP complex. Also phosphorylates RAB3IP/Rabin8, thus may affect RAB3IP guanine nucleotide exchange factor (GEF) activity toward Rab8, which is important for cilia growth (PubMed:31204173). Phosphorylates PKP1, facilitating its interaction with YWHAG and translocation to the nucleus, ultimately resulting in a reduction in keratinocyte intercellular adhesion (By similarity). Phosphorylation of PKP1 increases PKP1 protein stability, translocation to the cytoplasm away from desmosome plaques and PKP1-driven cap-dependent translation (PubMed:23444369). {ECO:0000250|UniProtKB:Q60823, ECO:0000269|PubMed:23444369, ECO:0000269|PubMed:31204173, ECO:0000303|PubMed:21432781, ECO:0000303|PubMed:21620960}.; FUNCTION: Several AKT2-specific substrates have been identified, including ANKRD2, C2CD5, CLK2 and PITX2. May play a role in myoblast differentiation. In this context, may act through PITX2 phosphorylation. Unphosphorylated PITX2 associates with an ELAVL1/HuR-containing complex, which stabilizes CCND1 cyclin mRNA, ensuring cell proliferation. Phosphorylation by AKT2 impairs this association, leading to CCND1 mRNA destabilization and progression towards differentiation (By similarity). Also involved in the negative regulation of myogenesis in response to stress conditions. In this context, acts by phosphorylating ANKRD2 (By similarity). May also be a key regulator of glucose uptake. Regulates insulin-stimulated glucose transport by the increase of glucose transporter GLUT4 translocation from intracellular stores to the plasma membrane. In this context, acts by phosphorylating C2CD5/CDP138 on 'Ser-197' in insulin-stimulated adipocytes (By similarity). Through the phosphorylation of CLK2 on 'Thr-343', involved in insulin-regulated suppression of hepatic gluconeogenesis (By similarity). {ECO:0000250|UniProtKB:Q60823}. |
| P31942 | HNRNPH3 | S56 | ochoa | Heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3) (Heterogeneous nuclear ribonucleoprotein 2H9) (hnRNP 2H9) | Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction. |
| P32926 | DSG3 | S771 | ochoa | Desmoglein-3 (130 kDa pemphigus vulgaris antigen) (PVA) (Cadherin family member 6) | A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:31835537). Required for adherens and desmosome junction assembly in response to mechanical force in keratinocytes (PubMed:31835537). Required for desmosome-mediated cell-cell adhesion of cells surrounding the telogen hair club and the basal layer of the outer root sheath epithelium, consequently is essential for the anchoring of telogen hairs in the hair follicle (PubMed:9701552). Required for the maintenance of the epithelial barrier via promoting desmosome-mediated intercellular attachment of suprabasal epithelium to basal cells (By similarity). May play a role in the protein stability of the desmosome plaque components DSP, JUP, PKP1, PKP2 and PKP3 (PubMed:22294297). Required for YAP1 localization at the plasma membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, PKP1 and YWHAG (PubMed:31835537). May also be involved in the positive regulation of YAP1 target gene transcription and as a result cell proliferation (PubMed:31835537). Positively regulates cellular contractility and cell junction formation via organization of cortical F-actin bundles and anchoring of actin to tight junctions, in conjunction with RAC1 (PubMed:22796473). The cytoplasmic pool of DSG3 is required for the localization of CDH1 and CTNNB1 at developing adherens junctions, potentially via modulation of SRC activity (PubMed:22294297). Inhibits keratinocyte migration via suppression of p38MAPK signaling, may therefore play a role in moderating wound healing (PubMed:26763450). {ECO:0000250|UniProtKB:O35902, ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:22796473, ECO:0000269|PubMed:26763450, ECO:0000269|PubMed:31835537, ECO:0000269|PubMed:9701552}. |
| P32926 | DSG3 | S971 | ochoa | Desmoglein-3 (130 kDa pemphigus vulgaris antigen) (PVA) (Cadherin family member 6) | A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:31835537). Required for adherens and desmosome junction assembly in response to mechanical force in keratinocytes (PubMed:31835537). Required for desmosome-mediated cell-cell adhesion of cells surrounding the telogen hair club and the basal layer of the outer root sheath epithelium, consequently is essential for the anchoring of telogen hairs in the hair follicle (PubMed:9701552). Required for the maintenance of the epithelial barrier via promoting desmosome-mediated intercellular attachment of suprabasal epithelium to basal cells (By similarity). May play a role in the protein stability of the desmosome plaque components DSP, JUP, PKP1, PKP2 and PKP3 (PubMed:22294297). Required for YAP1 localization at the plasma membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, PKP1 and YWHAG (PubMed:31835537). May also be involved in the positive regulation of YAP1 target gene transcription and as a result cell proliferation (PubMed:31835537). Positively regulates cellular contractility and cell junction formation via organization of cortical F-actin bundles and anchoring of actin to tight junctions, in conjunction with RAC1 (PubMed:22796473). The cytoplasmic pool of DSG3 is required for the localization of CDH1 and CTNNB1 at developing adherens junctions, potentially via modulation of SRC activity (PubMed:22294297). Inhibits keratinocyte migration via suppression of p38MAPK signaling, may therefore play a role in moderating wound healing (PubMed:26763450). {ECO:0000250|UniProtKB:O35902, ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:22796473, ECO:0000269|PubMed:26763450, ECO:0000269|PubMed:31835537, ECO:0000269|PubMed:9701552}. |
| P33981 | TTK | S321 | ochoa|psp | Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) | Involved in mitotic spindle assembly checkpoint signaling, a process that delays anaphase until chromosomes are bioriented on the spindle, and in the repair of incorrect mitotic kinetochore-spindle microtubule attachments (PubMed:18243099, PubMed:28441529, PubMed:29162720). Phosphorylates MAD1L1 to promote the mitotic spindle assembly checkpoint (PubMed:18243099, PubMed:29162720). Phosphorylates CDCA8/Borealin leading to enhanced AURKB activity at the kinetochore (PubMed:18243099). Phosphorylates SKA3 at 'Ser-34' leading to dissociation of the SKA complex from microtubules and destabilization of microtubule-kinetochore attachments (PubMed:28441529). Phosphorylates KNL1, KNTC1 and autophosphorylates (PubMed:28441529). Phosphorylates MCRS1 which enhances recruitment of KIF2A to the minus end of spindle microtubules and promotes chromosome alignment (PubMed:30785839). {ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:28441529, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:30785839}. |
| P34932 | HSPA4 | S76 | ochoa | Heat shock 70 kDa protein 4 (HSP70RY) (Heat shock 70-related protein APG-2) (Heat shock protein family H member 2) | None |
| 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 |
| P35221 | CTNNA1 | S264 | ochoa | Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13) | Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May play a crucial role in cell differentiation. {ECO:0000250|UniProtKB:P26231, ECO:0000269|PubMed:25653389}. |
| P35232 | PHB1 | S101 | ochoa | Prohibitin 1 | Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus (PubMed:11302691, PubMed:20959514, PubMed:28017329, PubMed:31522117). Plays a role in adipose tissue and glucose homeostasis in a sex-specific manner (By similarity). Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells (By similarity). {ECO:0000250|UniProtKB:P67778, ECO:0000250|UniProtKB:P67779, ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117}.; FUNCTION: In the mitochondria, together with PHB2, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as a chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner (By similarity). Regulates mitochondrial respiration activity playing a role in cellular aging (PubMed:11302691). The prohibitin complex plays a role of mitophagy receptor involved in targeting mitochondria for autophagic degradation (PubMed:28017329). Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6 (PubMed:31522117). {ECO:0000250|UniProtKB:P67778, ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117, ECO:0000305}.; FUNCTION: In the nucleus, acts as a transcription coregulator, enhances promoter binding by TP53, a transcription factor it activates, but reduces the promoter binding by E2F1, a transcription factor it represses (PubMed:14500729). Interacts with STAT3 to affect IL17 secretion in T-helper Th17 cells (PubMed:31899195). {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:31899195}.; FUNCTION: In the plasma membrane, cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates (By similarity). Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation (By similarity). {ECO:0000250|UniProtKB:P67778}. |
| P35241 | RDX | S532 | ochoa | Radixin | Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. |
| P35503 | UGT1A3 | S43 | psp | UDP-glucuronosyltransferase 1A3 (UGT1A3) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-3) (UDPGT 1-3) (UGT1*3) (UGT1-03) (UGT1.3) (UDP-glucuronosyltransferase 1-C) (UGT-1C) (UGT1C) (UDP-glucuronosyltransferase 1A isoform 3) | [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:18674515, PubMed:18719240, PubMed:23288867, PubMed:23756265, PubMed:24641623, PubMed:21422672). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:23756265). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol and estrone (PubMed:15472229, PubMed:18719240, PubMed:23288867). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption (PubMed:23756265). Involved in the glucuronidation of calcidiol, which is the major circulating form of vitamin D3, essential for the regulation of calcium and phosphate homeostasis (PubMed:24641623). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (PubMed:21422672). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonists losartan, candesartan and zolarsartan, which can inhibit the effect of angiotensin II (PubMed:18674515). {ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:21422672, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:23756265, ECO:0000269|PubMed:24641623}.; FUNCTION: [Isoform 2]: Lacks UDP-glucuronosyltransferase (UGT) activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:20610558}. |
| P35573 | AGL | S383 | ochoa | Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)] | Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. |
| P35680 | HNF1B | S80 | ochoa | Hepatocyte nuclear factor 1-beta (HNF-1-beta) (HNF-1B) (Homeoprotein LFB3) (Transcription factor 2) (TCF-2) (Variant hepatic nuclear factor 1) (vHNF1) | Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (PubMed:17924661, PubMed:7900999). Binds to the FPC element in the cAMP regulatory unit of the PLAU gene (By similarity). Transcriptional activity is increased by coactivator PCBD1 (PubMed:24204001). {ECO:0000250|UniProtKB:Q03365, ECO:0000269|PubMed:17924661, ECO:0000269|PubMed:24204001, ECO:0000269|PubMed:7900999}. |
| P35749 | MYH11 | S638 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P35749 | MYH11 | S687 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
| P36873 | PPP1CC | S182 | ochoa | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit) | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:17936702, PubMed:25012651). Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1 (PubMed:17936702). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (By similarity). Regulates the recruitment of the SKA complex to kinetochores (PubMed:28982702). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Together with PPP1CA (PP1-alpha subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35831509). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35831509). Dephosphorylates MKI67 at the onset of anaphase (PubMed:25012651). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:35831509). {ECO:0000250|UniProtKB:P63087, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23499489, ECO:0000269|PubMed:25012651, ECO:0000269|PubMed:28982702, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35831509}. |
| P36896 | ACVR1B | S168 | ochoa | 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}. |
| P38398 | BRCA1 | S398 | 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 | S708 | 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 | S753 | 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 | S956 | 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 | S1211 | 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}. |
| P38432 | COIL | S446 | ochoa | Coilin (p80-coilin) | Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. {ECO:0000269|PubMed:7679389}. |
| P39687 | ANP32A | S29 | ochoa | Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (pp32) (Leucine-rich acidic nuclear protein) (LANP) (Mapmodulin) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A) (Putative HLA-DR-associated protein I) (PHAPI) | Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription (PubMed:10400610, PubMed:11360199, PubMed:16341127, PubMed:18439902). Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation (PubMed:18439902). In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking (PubMed:11830591). Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition (PubMed:16341127). Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R) (PubMed:18180367). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (PubMed:15642345, PubMed:17557114). {ECO:0000269|PubMed:10400610, ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:11830591, ECO:0000269|PubMed:15642345, ECO:0000269|PubMed:16341127, ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:18180367, ECO:0000269|PubMed:18439902}.; FUNCTION: (Microbial infection) Plays an essential role in influenza A, B and C viral genome replication (PubMed:30666459, PubMed:32694517, PubMed:33045004, PubMed:33208942). Mechanistically, mediates the assembly of the viral replicase asymmetric dimers composed of PB1, PB2 and PA via its N-terminal region (PubMed:33208942). Also plays an essential role in foamy virus mRNA export from the nucleus (PubMed:21159877). {ECO:0000269|PubMed:21159877, ECO:0000269|PubMed:30666459, ECO:0000269|PubMed:32694517, ECO:0000269|PubMed:33045004, ECO:0000269|PubMed:33208942}. |
| P40337 | VHL | S183 | psp | von Hippel-Lindau disease tumor suppressor (Protein G7) (pVHL) | Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed:10944113, PubMed:17981124, PubMed:19584355). Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions (PubMed:10944113, PubMed:17981124). Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases (PubMed:10944113, PubMed:17981124). Ubiquitinates, in an oxygen-responsive manner, ADRB2 (PubMed:19584355). Acts as a negative regulator of mTORC1 by promoting ubiquitination and degradation of RPTOR (PubMed:34290272). {ECO:0000269|PubMed:10944113, ECO:0000269|PubMed:17981124, ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:34290272}. |
| P41229 | KDM5C | S1359 | ochoa | Lysine-specific demethylase 5C (EC 1.14.11.67) (Histone demethylase JARID1C) (Jumonji/ARID domain-containing protein 1C) (Protein SmcX) (Protein Xe169) ([histone H3]-trimethyl-L-lysine(4) demethylase 5C) | Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code (PubMed:28262558). 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'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity). {ECO:0000250|UniProtKB:P41230, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17468742, ECO:0000269|PubMed:26645689, ECO:0000269|PubMed:28262558}. |
| P42166 | TMPO | S59 | 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. |
| P42330 | AKR1C3 | S67 | ochoa | Aldo-keto reductase family 1 member C3 (EC 1.1.1.-) (EC 1.1.1.210) (EC 1.1.1.53) (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-HSD type II, brain) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Chlordecone reductase homolog HAKRb) (Dihydrodiol dehydrogenase 3) (DD-3) (DD3) (Dihydrodiol dehydrogenase type I) (HA1753) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239, EC 1.1.1.64) | Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Acts as a NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain and regulates the metabolism of androgens, estrogens and progesterone (PubMed:10622721, PubMed:11165022, PubMed:7650035, PubMed:9415401, PubMed:9927279). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:11165022, PubMed:14672942). Acts preferentially as a 17-ketosteroid reductase and has the highest catalytic efficiency of the AKR1C enzyme for the reduction of delta4-androstenedione to form testosterone (PubMed:20036328). Reduces prostaglandin (PG) D2 to 11beta-prostaglandin F2, progesterone to 20alpha-hydroxyprogesterone and estrone to 17beta-estradiol (PubMed:10622721, PubMed:10998348, PubMed:11165022, PubMed:15047184, PubMed:19010934, PubMed:20036328). Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10557352, PubMed:10998348, PubMed:11165022, PubMed:14672942, PubMed:7650035, PubMed:9415401). Also displays retinaldehyde reductase activity toward 9-cis-retinal (PubMed:21851338). {ECO:0000269|PubMed:10557352, ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:10998348, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:14672942, ECO:0000269|PubMed:15047184, ECO:0000269|PubMed:19010934, ECO:0000269|PubMed:20036328, ECO:0000269|PubMed:21851338, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279}. |
| P42345 | MTOR | S1166 | 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}. |
| P42684 | ABL2 | S97 | 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}. |
| P43121 | MCAM | S606 | ochoa | Cell surface glycoprotein MUC18 (Cell surface glycoprotein P1H12) (Melanoma cell adhesion molecule) (Melanoma-associated antigen A32) (Melanoma-associated antigen MUC18) (S-endo 1 endothelial-associated antigen) (CD antigen CD146) | Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as a surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration. {ECO:0000269|PubMed:11036077, ECO:0000269|PubMed:8292890}. |
| P43243 | MATR3 | S99 | 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 | S206 | 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}. |
| P46013 | MKI67 | S1546 | 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 | S2395 | 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}. |
| 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}. |
| P46939 | UTRN | S1258 | psp | Utrophin (Dystrophin-related protein 1) (DRP-1) | May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. |
| P46939 | UTRN | S2226 | ochoa | Utrophin (Dystrophin-related protein 1) (DRP-1) | May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. |
| P46976 | GYG1 | S46 | ochoa | Glycogenin-1 (GN-1) (GN1) (EC 2.4.1.186) | Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase. {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}. |
| P47712 | PLA2G4A | S454 | ochoa|psp | 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}. |
| P48382 | RFX5 | S313 | ochoa | DNA-binding protein RFX5 (Regulatory factor X 5) | Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters. |
| P48549 | KCNJ3 | S385 | psp | G protein-activated inward rectifier potassium channel 1 (GIRK-1) (Inward rectifier K(+) channel Kir3.1) (Potassium channel, inwardly rectifying subfamily J member 3) | Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This potassium channel is controlled by G proteins (PubMed:8804710, PubMed:8868049). This receptor plays a crucial role in regulating the heartbeat (By similarity). {ECO:0000250|UniProtKB:P63251, ECO:0000269|PubMed:8804710, ECO:0000269|PubMed:8868049}. |
| P48681 | NES | S905 | 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}. |
| P48764 | SLC9A3 | S810 | ochoa | Sodium/hydrogen exchanger 3 (Na(+)/H(+) exchanger 3) (NHE-3) (Solute carrier family 9 member 3) | Plasma membrane Na(+)/H(+) antiporter (PubMed:18829453, PubMed:26358773, PubMed:35613257). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis (By similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption and blood pressure regulation (PubMed:24622516, PubMed:26358773). {ECO:0000250|UniProtKB:G3X939, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:24622516, ECO:0000269|PubMed:26358773, ECO:0000269|PubMed:35613257}. |
| P49247 | RPIA | S106 | ochoa | Ribose-5-phosphate isomerase (EC 5.3.1.6) (Phosphoriboisomerase) | Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate and participates in the first step of the non-oxidative branch of the pentose phosphate pathway. {ECO:0000269|PubMed:14988808}. |
| P49257 | LMAN1 | S425 | ochoa | Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Gp58) (Intracellular mannose-specific lectin MR60) (Lectin mannose-binding 1) | Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:13130098}. |
| P49321 | NASP | S28 | ochoa | Nuclear autoantigenic sperm protein (NASP) | Component of the histone chaperone network (PubMed:22195965). Binds and stabilizes histone H3-H4 not bound to chromatin to maintain a soluble reservoir and modulate degradation by chaperone-mediated autophagy (PubMed:22195965). Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA. {ECO:0000250|UniProtKB:Q99MD9, ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 1]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}.; FUNCTION: [Isoform 2]: Stabilizes soluble histone H3-H4. {ECO:0000269|PubMed:22195965}. |
| P49327 | FASN | S63 | ochoa | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| P49327 | FASN | S1727 | ochoa | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| P49327 | FASN | S2253 | ochoa | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| P49685 | GPR15 | S342 | 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}. |
| P49773 | HINT1 | S72 | ochoa | Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) | Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:15703176, PubMed:16835243, PubMed:17217311, PubMed:17337452, PubMed:22329685, PubMed:23614568, PubMed:28691797, PubMed:29787766, PubMed:31990367). Hydrolyzes adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate) (PubMed:15703176, PubMed:16835243). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester (PubMed:15703176, PubMed:17337452, PubMed:22329685). Hydrolyzes 3-indolepropionic acyl-adenylate, tryptamine adenosine phosphoramidate monoester and other fluorogenic purine nucleoside tryptamine phosphoramidates in vitro (PubMed:17217311, PubMed:17337452, PubMed:23614568, PubMed:28691797, PubMed:29787766, PubMed:31990367). Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide (PubMed:30772266). In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1 (PubMed:16014379, PubMed:22647378). Modulates p53/TP53 levels and p53/TP53-mediated apoptosis (PubMed:16835243). Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (PubMed:19112177). Also exhibits SUMO-specific isopeptidase activity, deconjugating SUMO1 from RGS17 (PubMed:31088288). Deconjugates SUMO1 from RANGAP1 (By similarity). {ECO:0000250|UniProtKB:P80912, ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17217311, ECO:0000269|PubMed:17337452, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:23614568, ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:30772266, ECO:0000269|PubMed:31088288, ECO:0000269|PubMed:31990367}. |
| P49792 | RANBP2 | S700 | 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 | S1160 | 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 | S1514 | 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 | S3059 | 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}. |
| P50851 | LRBA | S1792 | 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}. |
| P50995 | ANXA11 | S480 | ochoa | Annexin A11 (56 kDa autoantigen) (Annexin XI) (Annexin-11) (Calcyclin-associated annexin 50) (CAP-50) | Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250, ECO:0000269|PubMed:15197175}. |
| P51531 | SMARCA2 | S588 | ochoa | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 (SAMRCA2) (EC 3.6.4.-) (BRG1-associated factor 190B) (BAF190B) (Probable global transcription activator SNF2L2) (Protein brahma homolog) (hBRM) (SNF2-alpha) | ATPase 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 (PubMed:15075294, PubMed:22952240, PubMed:26601204). 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:Q6DIC0, ECO:0000269|PubMed:15075294, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| P51531 | SMARCA2 | S700 | ochoa | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 (SAMRCA2) (EC 3.6.4.-) (BRG1-associated factor 190B) (BAF190B) (Probable global transcription activator SNF2L2) (Protein brahma homolog) (hBRM) (SNF2-alpha) | ATPase 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 (PubMed:15075294, PubMed:22952240, PubMed:26601204). 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:Q6DIC0, ECO:0000269|PubMed:15075294, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| P51587 | BRCA2 | S1339 | ochoa | 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}. |
| P51659 | HSD17B4 | S617 | ochoa | Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MFP-2) (Short chain dehydrogenase/reductase family 8C member 1) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)] | Bifunctional enzyme acting on the peroxisomal fatty acid beta-oxidation pathway. Catalyzes two of the four reactions in fatty acid degradation: hydration of 2-enoyl-CoA (trans-2-enoyl-CoA) to produce (3R)-3-hydroxyacyl-CoA, and dehydrogenation of (3R)-3-hydroxyacyl-CoA to produce 3-ketoacyl-CoA (3-oxoacyl-CoA), which is further metabolized by SCPx. Can use straight-chain and branched-chain fatty acids, as well as bile acid intermediates as substrates. {ECO:0000269|PubMed:10671535, ECO:0000269|PubMed:15060085, ECO:0000269|PubMed:8902629, ECO:0000269|PubMed:9089413}. |
| P51674 | GPM6A | S256 | ochoa | Neuronal membrane glycoprotein M6-a (M6a) | Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. GPM6A-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor. {ECO:0000269|PubMed:19298174}. |
| P51812 | RPS6KA3 | S78 | 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}. |
| P51911 | CNN1 | S175 | ochoa | Calponin-1 (Basic calponin) (Calponin H1, smooth muscle) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}. |
| P51911 | CNN1 | S215 | ochoa | Calponin-1 (Basic calponin) (Calponin H1, smooth muscle) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}. |
| P51955 | NEK2 | S184 | ochoa | Serine/threonine-protein kinase Nek2 (EC 2.7.11.1) (HSPK 21) (Never in mitosis A-related kinase 2) (NimA-related protein kinase 2) (NimA-like protein kinase 1) | Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856). Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835). {ECO:0000269|PubMed:11742531, ECO:0000269|PubMed:12857871, ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:15358203, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:17626005, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18297113, ECO:0000269|PubMed:20034488, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:26220856, ECO:0000269|PubMed:30404835}.; FUNCTION: [Isoform 1]: Phosphorylates and activates NEK11 in G1/S-arrested cells. {ECO:0000269|PubMed:15161910}.; FUNCTION: [Isoform 2]: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells. {ECO:0000269|PubMed:15161910}. |
| P51991 | HNRNPA3 | S43 | ochoa | Heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) | Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:11886857}. |
| P52569 | SLC7A2 | S24 | ochoa | Cationic amino acid transporter 2 (CAT-2) (CAT2) (Low affinity cationic amino acid transporter 2) (Solute carrier family 7 member 2) | Functions as a permease involved in the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine); the affinity for its substrates differs between isoforms created by alternative splicing (PubMed:28684763, PubMed:9174363). May play a role in classical or alternative activation of macrophages via its role in arginine transport (By similarity). {ECO:0000250|UniProtKB:P18581, ECO:0000269|PubMed:28684763, ECO:0000269|PubMed:9174363}.; FUNCTION: [Isoform 1]: Functions as a permease that mediates the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine). Shows a much higher affinity for L-arginine and L-homoarginine than isoform 2. {ECO:0000269|PubMed:28684763, ECO:0000269|PubMed:9174363}.; FUNCTION: [Isoform 2]: Functions as a low-affinity, high capacity permease involved in the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine). {ECO:0000269|PubMed:28684763, ECO:0000269|PubMed:9174363}. |
| P52948 | NUP98 | S673 | 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}. |
| P52948 | NUP98 | S683 | 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}. |
| P53004 | BLVRA | S21 | psp | Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase) | Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IXalpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor (PubMed:10858451, PubMed:7929092, PubMed:8424666, PubMed:8631357). Does not reduce bilirubin IXbeta (PubMed:10858451). Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7) (PubMed:7929092, PubMed:8424666, PubMed:8631357). NADPH, however, is the probable reactant in biological systems (PubMed:7929092). {ECO:0000269|PubMed:10858451, ECO:0000269|PubMed:7929092, ECO:0000269|PubMed:8424666, ECO:0000269|PubMed:8631357}. |
| P53778 | MAPK12 | S180 | ochoa | Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3) | Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. {ECO:0000269|PubMed:10848581, ECO:0000269|PubMed:14592936, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:21172807, ECO:0000269|PubMed:8633070, ECO:0000269|PubMed:9430721}. |
| P54136 | RARS1 | S378 | ochoa | Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) | Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:25288775). Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (PubMed:17443684). {ECO:0000269|PubMed:17443684, ECO:0000269|PubMed:25288775}. |
| P54296 | MYOM2 | S762 | ochoa | Myomesin-2 (165 kDa connectin-associated protein) (165 kDa titin-associated protein) (M-protein) (Myomesin family member 2) | Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent. |
| P55042 | RRAD | S290 | psp | GTP-binding protein RAD (RAD1) (Ras associated with diabetes) | May regulate basal voltage-dependent L-type Ca(2+) currents and be required for beta-adrenergic augmentation of Ca(2+) influx in cardiomyocytes, thereby regulating increases in heart rate and contractile force (By similarity). May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents (By similarity). Regulates voltage-dependent L-type calcium channel subunit alpha-1C trafficking to the cell membrane (By similarity). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway (PubMed:18056528). Inhibits phosphorylation and activation of CAMK2D (PubMed:18056528). {ECO:0000250|UniProtKB:O88667, ECO:0000269|PubMed:18056528}. |
| P56470 | LGALS4 | S258 | ochoa | Galectin-4 (Gal-4) (Antigen NY-CO-27) (L-36 lactose-binding protein) (L36LBP) (Lactose-binding lectin 4) | Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. |
| P59923 | ZNF445 | S177 | ochoa | Zinc finger protein 445 (ZFP445) (Zinc finger protein 168) (Zinc finger protein with KRAB and SCAN domains 15) | Transcription regulator required to maintain maternal and paternal gene imprinting, a process by which gene expression is restricted in a parent of origin-specific manner by epigenetic modification of genomic DNA and chromatin, including DNA methylation. Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions (ICRs) (PubMed:30602440). Acts together with ZFP57, but seems to be the major factor in human early embryonic imprinting maintenance. In contrast, in mice, ZFP57 plays the predominant role in imprinting maintenance (PubMed:30602440). {ECO:0000269|PubMed:30602440}. |
| P60484 | PTEN | S229 | psp | Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Inositol polyphosphate 3-phosphatase) (EC 3.1.3.-) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog) | Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins (PubMed:9187108, PubMed:9256433, PubMed:9616126). Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3 (PubMed:16824732, PubMed:26504226, PubMed:9593664, PubMed:9811831). Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate (PubMed:11418101, PubMed:15979280). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:31492966, PubMed:37279284). The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation (PubMed:11707428). In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (PubMed:22279049). Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation (PubMed:22279049). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation (PubMed:26166433). Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation (PubMed:26166433). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (By similarity). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability (PubMed:10468583, PubMed:18716620). {ECO:0000250|UniProtKB:O08586, ECO:0000250|UniProtKB:O54857, ECO:0000269|PubMed:10468583, ECO:0000269|PubMed:11418101, ECO:0000269|PubMed:11707428, ECO:0000269|PubMed:15979280, ECO:0000269|PubMed:16824732, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:26166433, ECO:0000269|PubMed:26504226, ECO:0000269|PubMed:31492966, ECO:0000269|PubMed:37279284, ECO:0000269|PubMed:9187108, ECO:0000269|PubMed:9256433, ECO:0000269|PubMed:9593664, ECO:0000269|PubMed:9616126, ECO:0000269|PubMed:9811831}.; FUNCTION: [Isoform alpha]: Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1. {ECO:0000269|PubMed:23744781}. |
| P61421 | ATP6V0D1 | S283 | ochoa | V-type proton ATPase subunit d 1 (V-ATPase subunit d 1) (32 kDa accessory protein) (V-ATPase 40 kDa accessory protein) (V-ATPase AC39 subunit) (p39) (Vacuolar proton pump subunit d 1) | Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:28296633, PubMed:30374053, PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:30374053). May play a role in coupling of proton transport and ATP hydrolysis (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). {ECO:0000250|UniProtKB:P51863, ECO:0000250|UniProtKB:Q6PGV1, ECO:0000269|PubMed:28296633, ECO:0000269|PubMed:30374053, ECO:0000269|PubMed:33065002}. |
| P61764 | STXBP1 | S313 | psp | Syntaxin-binding protein 1 (MUNC18-1) (N-Sec1) (Protein unc-18 homolog 1) (Unc18-1) (Protein unc-18 homolog A) (Unc-18A) (p67) | Participates in the regulation of synaptic vesicle docking and fusion through interaction with GTP-binding proteins (By similarity). Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. Involved in the release of neurotransmitters from neurons through interacting with SNARE complex component STX1A and mediating the assembly of the SNARE complex at synaptic membranes (By similarity). May play a role in determining the specificity of intracellular fusion reactions. {ECO:0000250|UniProtKB:O08599, ECO:0000250|UniProtKB:P61765}. |
| P62136 | PPP1CA | S22 | ochoa | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16) | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:28216226, PubMed:30158517, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Catalytic 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: 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 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). PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage (PubMed:17283141). Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development (By similarity). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (PubMed:21712997). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323). Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670). {ECO:0000250|UniProtKB:P62137, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23499489, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26083323, ECO:0000269|PubMed:28216226, ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:31677974, ECO:0000269|PubMed:33264625, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35830882, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240}.; FUNCTION: (Microbial infection) Necessary for alphaviruses replication. {ECO:0000269|PubMed:29769351}. |
| P62136 | PPP1CA | S182 | ochoa | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16) | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:28216226, PubMed:30158517, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Catalytic 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: 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 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). PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage (PubMed:17283141). Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development (By similarity). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (PubMed:21712997). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323). Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670). {ECO:0000250|UniProtKB:P62137, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23499489, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26083323, ECO:0000269|PubMed:28216226, ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:31677974, ECO:0000269|PubMed:33264625, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35830882, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240}.; FUNCTION: (Microbial infection) Necessary for alphaviruses replication. {ECO:0000269|PubMed:29769351}. |
| P62140 | PPP1CB | S181 | ochoa | Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (EC 3.1.3.16) (EC 3.1.3.53) | Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670). {ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670}. |
| P62701 | RPS4X | S204 | ochoa | Small ribosomal subunit protein eS4, X isoform (40S ribosomal protein S4) (SCR10) (Single copy abundant mRNA protein) | Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). 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:23636399, ECO:0000269|PubMed:34516797}. |
| P62826 | RAN | S150 | ochoa | GTP-binding nuclear protein Ran (EC 3.6.5.-) (Androgen receptor-associated protein 24) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) | GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:17209048, PubMed:26272610, PubMed:27306458, PubMed:8276887, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:11336674, PubMed:26272610, PubMed:29040603, PubMed:7819259, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport (PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446, PubMed:29040603). Required for normal progress through mitosis (PubMed:12194828, PubMed:29040603, PubMed:8421051). The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases (PubMed:10400640). {ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8276887, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9428644, ECO:0000269|PubMed:9822603, ECO:0000305|PubMed:26272610}. |
| P62857 | RPS28 | S41 | ochoa | Small ribosomal subunit protein eS28 (40S ribosomal protein S28) | Component of the small ribosomal subunit (PubMed:23636399, PubMed:25901680, PubMed:25957688). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688). 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:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:34516797}. |
| P62906 | RPL10A | S50 | ochoa | Large ribosomal subunit protein uL1 (60S ribosomal protein L10a) (CSA-19) (Neural precursor cell expressed developmentally down-regulated protein 6) (NEDD-6) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
| P62937 | PPIA | S21 | ochoa | Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] | Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.; FUNCTION: (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269|PubMed:15688292}.; FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269|PubMed:21593166}. |
| P69891 | HBG1 | S51 | ochoa | Hemoglobin subunit gamma-1 (Gamma-1-globin) (Hb F Agamma) (Hemoglobin gamma-1 chain) (Hemoglobin gamma-A chain) | Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. {ECO:0000269|PubMed:11514664, ECO:0000269|PubMed:22096240, ECO:0000269|PubMed:6198905}. |
| P69892 | HBG2 | S51 | ochoa | Hemoglobin subunit gamma-2 (Gamma-2-globin) (Hb F Ggamma) (Hemoglobin gamma-2 chain) (Hemoglobin gamma-G chain) | Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. {ECO:0000269|PubMed:19065339, ECO:0000269|PubMed:21561349, ECO:0000269|PubMed:24502349}. |
| P78332 | RBM6 | S554 | ochoa | RNA-binding protein 6 (Lung cancer antigen NY-LU-12) (Protein G16) (RNA-binding motif protein 6) (RNA-binding protein DEF-3) | Specifically binds poly(G) RNA homopolymers in vitro. |
| P78332 | RBM6 | S1025 | ochoa | RNA-binding protein 6 (Lung cancer antigen NY-LU-12) (Protein G16) (RNA-binding motif protein 6) (RNA-binding protein DEF-3) | Specifically binds poly(G) RNA homopolymers in vitro. |
| P78380 | OLR1 | S95 | ochoa | Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) (C-type lectin domain family 8 member A) (Lectin-like oxidized LDL receptor 1) (LOX-1) (Lectin-like oxLDL receptor 1) (hLOX-1) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form] | Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. {ECO:0000269|PubMed:11821063, ECO:0000269|PubMed:12354387, ECO:0000269|PubMed:9052782}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A variant 3 (nadA) of N.meningitidis. {ECO:0000305|PubMed:27302108}. |
| P78504 | JAG1 | S1101 | 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}. |
| P78559 | MAP1A | S527 | 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. |
| P79483 | HLA-DRB3 | S211 | ochoa | HLA class II histocompatibility antigen, DR beta 3 chain (MHC class II antigen DRB3) | A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB3-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells. Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:16148104, PubMed:19531622, PubMed:19830726, PubMed:20368442, PubMed:22929521, PubMed:23569328, PubMed:2463305, PubMed:2788702, PubMed:30282837, PubMed:31020640, PubMed:31308093, PubMed:31333679). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (By similarity). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (By similarity). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides. The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (By similarity). {ECO:0000250|UniProtKB:P01911, ECO:0000269|PubMed:16148104, ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2463305, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31020640, ECO:0000269|PubMed:31308093, ECO:0000269|PubMed:31333679}.; FUNCTION: ALLELE DRB3*01:01: Exclusively presents several immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a significant role in immune recognition and long-term protection (PubMed:19830726, PubMed:2463305, PubMed:2788702). Presents viral epitopes derived from HHV-6B U11, TRX2/U56 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). {ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:2463305, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:31020640}.; FUNCTION: ALLELE DRB3*02:02 Exclusively presents several immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a significant role in immune recognition and long-term protection (PubMed:19830726, PubMed:2788702). Upon EBV infection, presents to CD4-positive T cells latent antigen EBNA2 (PRSPTVFYNIPPMPLPPSQL) and lytic antigen BZLF1 (LTAYHVSTAPTGSWF) peptides, driving oligoclonal expansion and selection of virus-specific memory T cell subsets with cytotoxic potential to directly eliminate virus-infected B cells (PubMed:23569328, PubMed:31308093). Presents viral epitopes derived from HHV-6B U11, gB/U39 and gH/U48 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). Plays a minor role in CD4-positive T cell immune response against Dengue virus by presenting conserved peptides from capsid and non-structural NS3 proteins (PubMed:31333679). Displays peptides derived from IAV matrix protein M, implying a role in protection against IAV infection (PubMed:19830726). In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:22929521). Presents to Vbeta2-positive T-helper 1 cells specifically an immunodominant peptide derived from tumor antigen CTAG1A/NY-ESO-1(PGVLLKEFTVSGNILTIRLTAADHR) and confers protective memory response (PubMed:19531622, PubMed:20368442). In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a TP53 neoantigen (HYNYMCNSSCMGSMNRRPILTIITL) carrying G245S hotspot driver mutation and may mediate tumor regression (PubMed:30282837). {ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31020640, ECO:0000269|PubMed:31308093, ECO:0000269|PubMed:31333679}.; FUNCTION: ALLELE DRB3*03:01: Presents a series of conserved peptides derived from the M.tuberculosis PPE family of proteins, in particular PPE29 and PPE33, known to be highly immunogenic (PubMed:32341563). Presents immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a role in immune recognition and long-term protection (PubMed:2788702). Displays immunodominant viral peptides from HCV non-structural protein NS2, as part of a broad range T-helper response to resolve infection (PubMed:16148104). {ECO:0000269|PubMed:16148104, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:32341563}. |
| P98196 | ATP11A | S740 | ochoa | Phospholipid-transporting ATPase IH (EC 7.6.2.1) (ATPase IS) (ATPase class VI type 11A) (P4-ATPase flippase complex alpha subunit ATP11A) | Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:25947375, PubMed:26567335, PubMed:29799007, PubMed:30018401, PubMed:36300302). Does not show flippase activity toward phosphatidylcholine (PC) (PubMed:34403372). Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. {ECO:0000269|PubMed:15860663, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:30018401, ECO:0000269|PubMed:34403372, ECO:0000269|PubMed:36300302, ECO:0000305}. |
| Q00325 | SLC25A3 | S297 | ochoa | Solute carrier family 25 member 3 (Phosphate carrier protein, mitochondrial) (Phosphate transport protein) (PTP) | Inorganic ion transporter that transports phosphate or copper ions across the mitochondrial inner membrane into the matrix compartment (By similarity) (PubMed:17273968, PubMed:29237729). Mediates proton-coupled symport of phosphate ions necessary for mitochondrial oxidative phosphorylation of ADP to ATP (By similarity) (PubMed:17273968). Transports copper ions probably in the form of anionic copper(I) complexes to maintain mitochondrial matrix copper pool and to supply copper for cytochrome C oxidase complex assembly (PubMed:29237729). May also play a role in regulation of the mitochondrial permeability transition pore (mPTP) (By similarity). {ECO:0000250|UniProtKB:P12234, ECO:0000250|UniProtKB:P16036, ECO:0000269|PubMed:17273968, ECO:0000269|PubMed:29237729}. |
| Q00536 | CDK16 | S391 | 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}. |
| Q00537 | CDK17 | S83 | ochoa | Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2) | May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). {ECO:0000250}. |
| Q00610 | CLTC | S147 | ochoa | Clathrin heavy chain 1 (Clathrin heavy chain on chromosome 17) (CLH-17) | Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. 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 (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872). Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (By similarity). {ECO:0000250|UniProtKB:P49951, ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:20639872, ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}. |
| Q00610 | CLTC | S1462 | ochoa | Clathrin heavy chain 1 (Clathrin heavy chain on chromosome 17) (CLH-17) | Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. 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 (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872). Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (By similarity). {ECO:0000250|UniProtKB:P49951, ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:20639872, ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}. |
| Q00978 | IRF9 | S253 | psp | Interferon regulatory factor 9 (IRF-9) (IFN-alpha-responsive transcription factor subunit) (ISGF3 p48 subunit) (Interferon-stimulated gene factor 3 gamma) (ISGF-3 gamma) (Transcriptional regulator ISGF3 subunit gamma) | Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. {ECO:0000269|PubMed:30143481}. |
| Q00987 | MDM2 | S157 | 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}. |
| Q01538 | MYT1 | S94 | ochoa | Myelin transcription factor 1 (MyT1) (Myelin transcription factor I) (MyTI) (PLPB1) (Proteolipid protein-binding protein) | Binds to the promoter region of genes encoding proteolipid proteins of the central nervous system. May play a role in the development of neurons and oligodendroglia in the CNS. May regulate a critical transition point in oligodendrocyte lineage development by modulating oligodendrocyte progenitor proliferation relative to terminal differentiation and up-regulation of myelin gene transcription. {ECO:0000269|PubMed:14962745}. |
| Q01860 | POU5F1 | S111 | psp | POU domain, class 5, transcription factor 1 (Octamer-binding protein 3) (Oct-3) (Octamer-binding protein 4) (Oct-4) (Octamer-binding transcription factor 3) (OTF-3) | Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. {ECO:0000269|PubMed:18035408}. |
| Q02790 | FKBP4 | S229 | ochoa | Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (51 kDa FK506-binding protein) (FKBP51) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed] | Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Also acts as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. {ECO:0000269|PubMed:1279700, ECO:0000269|PubMed:1376003, ECO:0000269|PubMed:19945390, ECO:0000269|PubMed:21730050, ECO:0000269|PubMed:2378870}. |
| Q03169 | TNFAIP2 | S68 | ochoa | Tumor necrosis factor alpha-induced protein 2 (TNF alpha-induced protein 2) (Primary response gene B94 protein) | May play a role as a mediator of inflammation and angiogenesis. |
| Q03188 | CENPC | S189 | 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}. |
| Q03468 | ERCC6 | S1276 | ochoa|psp | DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB) | Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes (PubMed:16246722, PubMed:20541997, PubMed:22483866, PubMed:26620705, PubMed:32355176, PubMed:34526721, PubMed:38316879, PubMed:38600235, PubMed:38600236). Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment (PubMed:32355176, PubMed:34526721, PubMed:38600235, PubMed:38600236). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (PubMed:15548521). Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (PubMed:16246722, PubMed:9565609). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (PubMed:25820262). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (PubMed:25820262). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing premature entry of cells into mitosis following the induction of DNA DSBs (PubMed:25820262). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (PubMed:29203878). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (PubMed:28292928). Also involved in UV-induced translocation of ERCC8 to the nuclear matrix (PubMed:26620705). Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (PubMed:24874740). {ECO:0000269|PubMed:15548521, ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:20541997, ECO:0000269|PubMed:22483866, ECO:0000269|PubMed:24874740, ECO:0000269|PubMed:25820262, ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:28292928, ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:34526721, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:38600235, ECO:0000269|PubMed:38600236, ECO:0000269|PubMed:9565609}. |
| Q04637 | EIF4G1 | S1209 | 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}. |
| Q04828 | AKR1C1 | S67 | ochoa | Aldo-keto reductase family 1 member C1 (EC 1.1.1.-) (EC 1.1.1.112) (EC 1.1.1.209) (EC 1.1.1.210) (EC 1.1.1.357) (EC 1.1.1.51) (EC 1.1.1.53) (EC 1.1.1.62) (EC 1.3.1.20) (20-alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (EC 1.1.1.149) (Chlordecone reductase homolog HAKRC) (Dihydrodiol dehydrogenase 1) (DD1) (High-affinity hepatic bile acid-binding protein) (HBAB) | Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699). {ECO:0000269|PubMed:10998348, ECO:0000269|PubMed:14672942, ECO:0000269|PubMed:19218247, ECO:0000269|PubMed:8486699}. |
| Q05682 | CALD1 | S518 | ochoa | Caldesmon (CDM) | Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250, ECO:0000269|PubMed:8227296}. |
| Q07812 | BAX | S163 | psp | Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4) | Plays a role in the mitochondrial apoptotic process (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:36361894, PubMed:8358790, PubMed:8521816). Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). Promotes activation of CASP3, and thereby apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:11060313, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:16199525, ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:21458670, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:36361894, ECO:0000269|PubMed:8358790, ECO:0000269|PubMed:8521816}. |
| Q08043 | ACTN3 | S116 | ochoa | Alpha-actinin-3 (Alpha-actinin skeletal muscle isoform 3) (F-actin cross-linking protein) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. |
| Q08050 | FOXM1 | S717 | 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}. |
| Q08378 | GOLGA3 | S393 | 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. |
| Q08945 | SSRP1 | S405 | ochoa | FACT complex subunit SSRP1 (Chromatin-specific transcription elongation factor 80 kDa subunit) (Facilitates chromatin transcription complex 80 kDa subunit) (FACT 80 kDa subunit) (FACTp80) (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (hSSRP1) (T160) | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63. {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}. |
| Q08AD1 | CAMSAP2 | S522 | 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}. |
| Q08J23 | NSUN2 | S593 | ochoa | RNA cytosine C(5)-methyltransferase NSUN2 (EC 2.1.1.-) (Myc-induced SUN domain-containing protein) (Misu) (NOL1/NOP2/Sun domain family member 2) (Substrate of AIM1/Aurora kinase B) (mRNA cytosine C(5)-methyltransferase) (EC 2.1.1.-) (tRNA cytosine C(5)-methyltransferase) (EC 2.1.1.-, EC 2.1.1.203) (tRNA methyltransferase 4 homolog) (hTrm4) | RNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs) (PubMed:17071714, PubMed:22995836, PubMed:31199786, PubMed:31358969). Involved in various processes, such as epidermal stem cell differentiation, testis differentiation and maternal to zygotic transition during early development: acts by increasing protein synthesis; cytosine C(5)-methylation promoting tRNA stability and preventing mRNA decay (PubMed:31199786). Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors (PubMed:17071714, PubMed:22995836, PubMed:31199786). tRNA methylation is required generation of RNA fragments derived from tRNAs (tRFs) (PubMed:31199786). Also mediates C(5)-methylation of mitochondrial tRNAs (PubMed:31276587). Catalyzes cytosine C(5)-methylation of mRNAs, leading to stabilize them and prevent mRNA decay: mRNA stabilization involves YBX1 that specifically recognizes and binds m5C-modified transcripts (PubMed:22395603, PubMed:31358969, PubMed:34556860). Cytosine C(5)-methylation of mRNAs also regulates mRNA export: methylated transcripts are specifically recognized by THOC4/ALYREF, which mediates mRNA nucleo-cytoplasmic shuttling (PubMed:28418038). Also mediates cytosine C(5)-methylation of non-coding RNAs, such as vault RNAs (vtRNAs), promoting their processing into regulatory small RNAs (PubMed:23871666). Cytosine C(5)-methylation of vtRNA VTRNA1.1 promotes its processing into small-vault RNA4 (svRNA4) and regulates epidermal differentiation (PubMed:31186410). May act downstream of Myc to regulate epidermal cell growth and proliferation (By similarity). Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity (PubMed:19596847). {ECO:0000250|UniProtKB:Q1HFZ0, ECO:0000269|PubMed:17071714, ECO:0000269|PubMed:19596847, ECO:0000269|PubMed:22395603, ECO:0000269|PubMed:22995836, ECO:0000269|PubMed:23871666, ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:31186410, ECO:0000269|PubMed:31199786, ECO:0000269|PubMed:31276587, ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:34556860}. |
| Q09666 | AHNAK | S658 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
| Q12802 | AKAP13 | S1942 | 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}. |
| Q12888 | TP53BP1 | S103 | 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}. |
| Q12972 | PPP1R8 | S249 | ochoa | Nuclear inhibitor of protein phosphatase 1 (NIPP-1) (Protein phosphatase 1 regulatory inhibitor subunit 8) [Includes: Activator of RNA decay (EC 3.1.4.-) (ARD-1)] | Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.; FUNCTION: Isoform Gamma is a site-specific single-strand endoribonuclease that cleaves single strand RNA 3' to purines and pyrimidines in A+U-rich regions. It generates 5'-phosphate termini at the site of cleavage. This isoform does not inhibit PP-1. May be implicated in mRNA splicing. |
| Q13017 | ARHGAP5 | S1142 | ochoa | Rho GTPase-activating protein 5 (Rho-type GTPase-activating protein 5) (p190-B) | GTPase-activating protein for Rho family members (PubMed:8537347). {ECO:0000269|PubMed:8537347}. |
| Q13085 | ACACA | S1203 | 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}. |
| Q13112 | CHAF1B | S529 | 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}. |
| Q13136 | PPFIA1 | S776 | 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}. |
| Q13153 | PAK1 | S110 | ochoa | Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (p21-activated kinase 1) (PAK-1) (p65-PAK) | Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes (PubMed:10551809, PubMed:11896197, PubMed:12876277, PubMed:14585966, PubMed:15611088, PubMed:17726028, PubMed:17989089, PubMed:30290153, PubMed:17420447). Can directly phosphorylate BAD and protects cells against apoptosis (By similarity). Activated by interaction with CDC42 and RAC1 (PubMed:8805275, PubMed:9528787). Functions as a GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway (PubMed:8805275, PubMed:9528787). Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases (By similarity). Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes (PubMed:9032240, PubMed:9395435). Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton (PubMed:15831477). Plays a role in the regulation of insulin secretion in response to elevated glucose levels (PubMed:22669945). Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (By similarity). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 (PubMed:12624090). Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 (PubMed:11733498). Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus (PubMed:15833848). In podocytes, promotes NR3C2 nuclear localization (By similarity). Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation (By similarity). Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321). In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (PubMed:23260667). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity). In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). Along with GIT1, positively regulates microtubule nucleation during interphase (PubMed:27012601). Phosphorylates FXR1, promoting its localization to stress granules and activity (PubMed:20417602). Phosphorylates ILK on 'Thr-173' and 'Ser-246', promoting nuclear export of ILK (PubMed:17420447). {ECO:0000250|UniProtKB:O88643, ECO:0000250|UniProtKB:P35465, ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:11896197, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:15611088, ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:17420447, ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089, ECO:0000269|PubMed:20417602, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:23633677, ECO:0000269|PubMed:25766321, ECO:0000269|PubMed:27012601, ECO:0000269|PubMed:30290153, ECO:0000269|PubMed:8805275, ECO:0000269|PubMed:9032240, ECO:0000269|PubMed:9395435, ECO:0000269|PubMed:9528787}. |
| Q13177 | PAK2 | S109 | 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}. |
| Q13201 | MMRN1 | S368 | ochoa | Multimerin-1 (EMILIN-4) (Elastin microfibril interface located protein 4) (Elastin microfibril interfacer 4) (Endothelial cell multimerin) [Cleaved into: Platelet glycoprotein Ia*; 155 kDa platelet multimerin (p-155) (p155)] | Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein. {ECO:0000269|PubMed:16363244, ECO:0000269|PubMed:19132231, ECO:0000269|PubMed:7629143}. |
| Q13206 | DDX10 | S840 | ochoa | Probable ATP-dependent RNA helicase DDX10 (EC 3.6.4.13) (DEAD box protein 10) | Putative ATP-dependent RNA helicase that plays various role in innate immunity or inflammation. Plays a role in the enhancement of AIM2-induced inflammasome activation by interacting with AIM2 and stabilizing its protein level (PubMed:32519665). Negatively regulates viral infection by promoting interferon beta production and interferon stimulated genes/ISGs expression (PubMed:36779599). {ECO:0000269|PubMed:32519665, ECO:0000269|PubMed:36779599}. |
| Q13207 | TBX2 | S401 | ochoa | T-box transcription factor TBX2 (T-box protein 2) | Transcription factor which acts as a transcriptional repressor (PubMed:11062467, PubMed:11111039, PubMed:12000749, PubMed:22844464, PubMed:30599067). May also function as a transcriptional activator (By similarity). 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:11111039, PubMed:12000749, PubMed:22844464, PubMed:30599067). Required for cardiac atrioventricular canal formation (PubMed:29726930). May cooperate with NKX2.5 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (By similarity). May play a role as a positive regulator of TGFB2 expression, perhaps acting in concert with GATA4 in the developing outflow tract myocardium (By similarity). Plays a role in limb pattern formation (PubMed:29726930). Acts as a transcriptional repressor of ADAM10 gene expression, perhaps in concert with histone deacetylase HDAC1 as cofactor (PubMed:30599067). Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX3 (By similarity). Required, together with TBX3, 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 TBX3, in different subregions of the developing ear (By similarity). Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537). Acts as a negative regulator of expression of CDKN1A/p21, IL33 and CCN4; repression of CDKN1A is enhanced in response to UV-induced stress, perhaps as a result of phosphorylation by p38 MAPK (By similarity). Negatively modulates expression of CDKN2A/p14ARF and CDH1/E-cadherin (PubMed:11062467, PubMed:12000749, PubMed:22844464). Plays a role in induction of the epithelial-mesenchymal transition (EMT) (PubMed:22844464). Plays a role in melanocyte proliferation, perhaps via regulation of cyclin CCND1 (By similarity). Involved in melanogenesis, acting via negative modulation of expression of DHICA oxidase/TYRP1 and P protein/OCA2 (By similarity). Involved in regulating retinal pigment epithelium (RPE) cell proliferation, perhaps via negatively modulating transcription of the transcription factor CEBPD (PubMed:28910203). {ECO:0000250|UniProtKB:Q60707, ECO:0000269|PubMed:11062467, ECO:0000269|PubMed:11111039, ECO:0000269|PubMed:12000749, ECO:0000269|PubMed:22002537, ECO:0000269|PubMed:22844464, ECO:0000269|PubMed:28910203, ECO:0000269|PubMed:29726930, ECO:0000269|PubMed:30599067}. |
| Q13439 | GOLGA4 | S213 | ochoa | Golgin subfamily A member 4 (256 kDa golgin) (Golgin-245) (Protein 72.1) (Trans-Golgi p230) | Involved in vesicular trafficking at the Golgi apparatus level. May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1. Involved in endosome-to-Golgi trafficking (PubMed:29084197). {ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:29084197}. |
| Q13459 | MYO9B | S2109 | 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}. |
| Q13469 | NFATC2 | S118 | 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}. |
| Q13501 | SQSTM1 | S399 | 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}. |
| Q13507 | TRPC3 | S837 | psp | Short transient receptor potential channel 3 (TrpC3) (Transient receptor protein 3) (TRP-3) (hTrp-3) (hTrp3) | Forms a receptor-activated non-selective calcium permeant cation channel (PubMed:29726814, PubMed:30139744, PubMed:35051376, PubMed:9417057, PubMed:9930701, PubMed:10611319). {ECO:0000269|PubMed:10611319, ECO:0000269|PubMed:29726814, ECO:0000269|PubMed:30139744, ECO:0000269|PubMed:35051376, ECO:0000269|PubMed:9417057, ECO:0000269|PubMed:9930701}.; FUNCTION: [Isoform 2]: Forms a receptor-activated non-selective calcium permeant cation channel. May be operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. {ECO:0000269|PubMed:8646775}. |
| Q13554 | CAMK2B | S235 | ochoa | Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17) | Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle (PubMed:16690701). In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons (PubMed:29100089). Participates in the modulation of skeletal muscle function in response to exercise (PubMed:16690701). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). Phosphorylates reticulophagy regulator RETREG1 at 'Ser-151' under endoplasmic reticulum stress conditions which enhances RETREG1 oligomerization and its membrane scission and reticulophagy activity (PubMed:31930741). {ECO:0000250|UniProtKB:P08413, ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:29100089, ECO:0000269|PubMed:31930741}. |
| Q13555 | CAMK2G | S235 | ochoa | Calcium/calmodulin-dependent protein kinase type II subunit gamma (CaM kinase II subunit gamma) (CaMK-II subunit gamma) (EC 2.7.11.17) | Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (PubMed:16690701). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin (PubMed:16690701). In the central nervous system, it is involved in the regulation of neurite formation and arborization (PubMed:30184290). It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q923T9, ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:30184290}. |
| Q13557 | CAMK2D | S235 | ochoa | Calcium/calmodulin-dependent protein kinase type II subunit delta (CaM kinase II subunit delta) (CaMK-II subunit delta) (EC 2.7.11.17) | Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program (PubMed:17179159). Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis (PubMed:16690701). May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q6PHZ2, ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:17179159}. |
| Q13621 | SLC12A1 | S120 | psp | Solute carrier family 12 member 1 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1) (BSC1) (Kidney-specific Na-K-Cl symporter) (Na-K-2Cl cotransporter 2) (NKCC2) | Renal sodium, potassium and chloride ion cotransporter that mediates the transepithelial NaCl reabsorption in the thick ascending limb and plays an essential role in the urinary concentration and volume regulation (PubMed:21321328). Electrically silent transporter system (By similarity). {ECO:0000250|UniProtKB:P55014, ECO:0000250|UniProtKB:P55016, ECO:0000269|PubMed:21321328}. |
| Q13625 | TP53BP2 | S774 | ochoa | Apoptosis-stimulating of p53 protein 2 (Bcl2-binding protein) (Bbp) (Renal carcinoma antigen NY-REN-51) (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2) | Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (PubMed:12524540). Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of NAE1 to conjugate NEDD8 to CUL1, and thereby decreases NAE1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}. |
| Q13796 | SHROOM2 | S218 | 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 | S1615 | 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. |
| Q14008 | CKAP5 | S1964 | 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 | S754 | 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}. |
| Q14160 | SCRIB | S1600 | 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}. |
| Q14166 | TTLL12 | S317 | ochoa | Tubulin--tyrosine ligase-like protein 12 (Inactive tubulin--tyrosine ligase-like protein 12) | Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues (PubMed:20162578, PubMed:23251473). Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3) (PubMed:23251473). Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability (PubMed:20162578, PubMed:23251473). During RNA virus-mediated infection, acts as a negative regulator of the RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE (PubMed:28011935). {ECO:0000269|PubMed:20162578, ECO:0000269|PubMed:23251473, ECO:0000269|PubMed:28011935}. |
| Q14244 | MAP7 | S188 | 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}. |
| Q14432 | PDE3A | S1003 | 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}. |
| Q14542 | SLC29A2 | S244 | ochoa | Equilibrative nucleoside transporter 2 (hENT2) (36 kDa nucleolar protein HNP36) (Delayed-early response protein 12) (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Hydrophobic nucleolar protein, 36 kDa) (Nucleoside transporter, ei-type) (Solute carrier family 29 member 2) | Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:10722669, PubMed:12527552, PubMed:12590919, PubMed:16214850, PubMed:21795683, PubMed:9396714, PubMed:9478986). Functions as a Na(+)-independent, passive transporter (PubMed:9478986). Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymidine, cytidine and guanosine (PubMed:10722669, PubMed:12527552, PubMed:12590919, PubMed:16214850, PubMed:21795683, PubMed:9396714, PubMed:9478986). Also able to transport purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (PubMed:16214850, PubMed:21795683). Involved in nucleoside transport at basolateral membrane of kidney cells, allowing liver absorption of nucleoside metabolites (PubMed:12527552). Mediates apical nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis-barrier (PubMed:23639800). Mediates both the influx and efflux of hypoxanthine in skeletal muscle microvascular endothelial cells to control the amount of intracellular hypoxanthine available for xanthine oxidase-mediated ROS production (By similarity). {ECO:0000250|UniProtKB:O54699, ECO:0000269|PubMed:10722669, ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:12590919, ECO:0000269|PubMed:16214850, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:23639800, ECO:0000269|PubMed:9396714, ECO:0000269|PubMed:9478986}.; FUNCTION: [Isoform 3]: Non functional nucleoside transporter protein for adenosine or thymidine transport. Does not express on cell membrane. {ECO:0000269|PubMed:12527552}. |
| Q14669 | TRIP12 | S1248 | 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}. |
| Q14674 | ESPL1 | S1305 | psp | Separin (EC 3.4.22.49) (Caspase-like protein ESPL1) (Extra spindle poles-like 1 protein) (Separase) | Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11509732}. |
| Q14676 | MDC1 | S544 | 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}. |
| Q14680 | MELK | S363 | ochoa | Maternal embryonic leucine zipper kinase (hMELK) (EC 2.7.11.1) (Protein kinase Eg3) (pEg3 kinase) (Protein kinase PK38) (hPK38) (Tyrosine-protein kinase MELK) (EC 2.7.10.2) | Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}. |
| Q14684 | RRP1B | S278 | 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}. |
| Q14690 | PDCD11 | S926 | ochoa | Protein RRP5 homolog (NF-kappa-B-binding protein) (NFBP) (Programmed cell death protein 11) | Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.; FUNCTION: Involved in the biogenesis of rRNA. {ECO:0000250}. |
| Q14766 | LTBP1 | S1512 | ochoa | Latent-transforming growth factor beta-binding protein 1 (LTBP-1) (Transforming growth factor beta-1-binding protein 1) (TGF-beta1-BP-1) | Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:2022183, PubMed:8617200, PubMed:8939931). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:15184403, PubMed:8617200, PubMed:8939931). Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta (PubMed:22278742). {ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}. |
| Q14789 | GOLGB1 | S1568 | 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. |
| Q14966 | ZNF638 | S278 | 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 | S560 | 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}. |
| Q14980 | NUMA1 | S77 | 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 | S934 | 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 | S1149 | 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}. |
| Q14997 | PSME4 | S1746 | ochoa | Proteasome activator complex subunit 4 (Proteasome activator PA200) (Protein BLM10 homolog) (Blm10) (hBlm10) | Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks. {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:18845680, ECO:0000269|PubMed:22550082, ECO:0000269|PubMed:23706739}. |
| Q14CZ8 | HEPACAM | S278 | ochoa | Hepatic and glial cell adhesion molecule (glialCAM) (Hepatocyte cell adhesion molecule) (Protein hepaCAM) | Involved in regulating cell motility and cell-matrix interactions. May inhibit cell growth through suppression of cell proliferation (PubMed:15885354, PubMed:15917256). In glia, associates and targets CLCN2 at astrocytic processes and myelinated fiber tracts where it may regulate transcellular chloride flux involved in neuron excitability (PubMed:22405205). {ECO:0000269|PubMed:15885354, ECO:0000269|PubMed:15917256, ECO:0000269|PubMed:22405205}. |
| Q15003 | NCAPH | S256 | 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}. |
| Q15007 | WTAP | S58 | 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 | S38 | 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}. |
| Q15058 | KIF14 | S101 | 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 | S1220 | psp | 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 | S701 | 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 | S3853 | 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}. |
| Q15172 | PPP2R5A | S41 | ochoa|psp | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha) | 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. |
| Q15233 | NONO | S212 | ochoa | Non-POU domain-containing octamer-binding protein (NonO protein) (54 kDa nuclear RNA- and DNA-binding protein) (p54(nrb)) (p54nrb) (55 kDa nuclear protein) (NMT55) (DNA-binding p52/p100 complex, 52 kDa subunit) | DNA- and RNA binding protein, involved in several nuclear processes (PubMed:11525732, PubMed:12403470, PubMed:26571461). Binds the conventional octamer sequence in double-stranded DNA (PubMed:11525732, PubMed:12403470, PubMed:26571461). Also binds single-stranded DNA and RNA at a site independent of the duplex site (PubMed:11525732, PubMed:12403470, PubMed:26571461). Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, PubMed:12403470, PubMed:26571461). Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (PubMed:12403470). Together with PSPC1, required for the formation of nuclear paraspeckles (PubMed:22416126). The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (PubMed:11525732). The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (PubMed:10858305). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends (PubMed:15590677). In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex (PubMed:15590677). NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (PubMed:11897684). NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity). Important for the functional organization of GABAergic synapses (By similarity). Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (By similarity). Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (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, PubMed:30270045). Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (PubMed:30270045). In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway (PubMed:30270045). {ECO:0000250|UniProtKB:Q99K48, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:26571461, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:30270045}. |
| 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 | S662 | 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}. |
| Q15417 | CNN3 | S215 | ochoa | Calponin-3 (Calponin, acidic isoform) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
| Q15418 | RPS6KA1 | S72 | 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}. |
| Q15418 | RPS6KA1 | S687 | 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}. |
| Q15437 | SEC23B | S186 | psp | Protein transport protein Sec23B (hSec23B) (SEC23-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. {ECO:0000250|UniProtKB:Q15436}. |
| Q15554 | TERF2 | S422 | 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}. |
| Q15746 | MYLK | S343 | 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}. |
| Q15835 | GRK1 | S21 | psp | Rhodopsin kinase GRK1 (RK) (EC 2.7.11.14) (G protein-coupled receptor kinase 1) | Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade (PubMed:15946941). This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination (By similarity). May play a role in the maintenance of the outer nuclear layer in the retina (By similarity). {ECO:0000250|UniProtKB:Q9WVL4, ECO:0000269|PubMed:15946941}. |
| Q15878 | CACNA1E | S793 | ochoa | Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3) | Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells (PubMed:30343943). They are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel. They are however insensitive to dihydropyridines (DHP). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing. {ECO:0000269|PubMed:30343943, ECO:0000269|PubMed:7536609}.; FUNCTION: [Isoform 3]: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells. They are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1E gives rise to R-type calcium currents. {ECO:0000269|PubMed:8071363}. |
| Q15916 | ZBTB6 | S202 | ochoa | Zinc finger and BTB domain-containing protein 6 (Zinc finger protein 482) (Zinc finger protein with interaction domain) | May be involved in transcriptional regulation. |
| Q16204 | CCDC6 | S254 | ochoa | Coiled-coil domain-containing protein 6 (Papillary thyroid carcinoma-encoded protein) (Protein H4) | None |
| Q16576 | RBBP7 | S314 | psp | Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46) | Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:28977666}. |
| Q16623 | STX1A | S95 | ochoa | Syntaxin-1A (Neuron-specific antigen HPC-1) | Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:26635000). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (PubMed:23091057). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). {ECO:0000250|UniProtKB:O35526, ECO:0000269|PubMed:23091057, ECO:0000269|PubMed:26635000}. |
| Q16630 | CPSF6 | S38 | ochoa | Cleavage and polyadenylation specificity factor subunit 6 (Cleavage and polyadenylation specificity factor 68 kDa subunit) (CPSF 68 kDa subunit) (Cleavage factor Im complex 68 kDa subunit) (CFIm68) (Pre-mRNA cleavage factor Im 68 kDa subunit) (Protein HPBRII-4/7) | 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:14690600, PubMed:29276085, PubMed:8626397, PubMed:9659921). 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:14690600, PubMed:8626397, PubMed:9659921). 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). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:21295486, PubMed:29276085). Plays a role in mRNA export (PubMed:19864460). {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.; FUNCTION: (Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and might thereby promote the integration of the virus in the nucleus of dividing cells (in vitro). {ECO:0000269|PubMed:24130490}. |
| Q16799 | RTN1 | S164 | ochoa | Reticulon-1 (Neuroendocrine-specific protein) | Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity. {ECO:0000269|PubMed:15286784}. |
| Q16825 | PTPN21 | S484 | ochoa | Tyrosine-protein phosphatase non-receptor type 21 (EC 3.1.3.48) (Protein-tyrosine phosphatase D1) | None |
| Q16891 | IMMT | S528 | psp | MICOS complex subunit MIC60 (Cell proliferation-inducing gene 4/52 protein) (Mitochondrial inner membrane protein) (Mitofilin) (p87/89) | 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:22114354, PubMed:25781180, PubMed:32567732, PubMed:33130824). Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:22114354, PubMed:25781180, PubMed:32567732, PubMed:33130824). {ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:32567732, ECO:0000269|PubMed:33130824}. |
| Q17RB8 | LONRF1 | S412 | ochoa | LON peptidase N-terminal domain and RING finger protein 1 (RING finger protein 191) | None |
| Q2LD37 | BLTP1 | S1971 | ochoa | Bridge-like lipid transfer protein family member 1 (Fragile site-associated protein) | Tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum (Probable). Plays a role in endosomal trafficking and endosome recycling. Also involved in the actin cytoskeleton and cilia structural dynamics (PubMed:30906834). Acts as a regulator of phagocytosis (PubMed:31540829). {ECO:0000269|PubMed:30906834, ECO:0000269|PubMed:31540829, ECO:0000305|PubMed:35015055, ECO:0000305|PubMed:35491307}. |
| Q2M1P5 | KIF7 | S1289 | 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}. |
| Q2PPJ7 | RALGAPA2 | S1350 | 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}. |
| Q32MZ4 | LRRFIP1 | S638 | 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 | S746 | 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}. |
| Q32P51 | HNRNPA1L2 | S22 | ochoa | Heterogeneous nuclear ribonucleoprotein A1-like 2 (hnRNP A1-like 2) (hnRNP core protein A1-like 2) | Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. {ECO:0000250}. |
| Q3KQV3 | ZNF792 | S121 | ochoa | Zinc finger protein 792 | May be involved in transcriptional regulation. |
| Q3MJ13 | WDR72 | S976 | ochoa | WD repeat-containing protein 72 | Plays a major role in formation of tooth enamel (PubMed:19853237, PubMed:25008349). Specifically required during the maturation phase of amelogenesis for normal formation of the enamel matrix and clearance of enamel proteins. May be involved in localization of the calcium transporter SLC24A4 to the ameloblast cell membrane. {ECO:0000250|UniProtKB:D3YYM4, ECO:0000269|PubMed:19853237, ECO:0000269|PubMed:25008349}. |
| Q49AR2 | C5orf22 | S198 | ochoa | UPF0489 protein C5orf22 | None |
| Q4G0F5 | VPS26B | S302 | ochoa | Vacuolar protein sorting-associated protein 26B (Vesicle protein sorting 26B) | Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity). {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}. |
| Q504Q3 | PAN2 | S791 | ochoa | PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (Inactive ubiquitin carboxyl-terminal hydrolase 52) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) | Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:16284618, ECO:0000269|PubMed:23398456}. |
| Q52LW3 | ARHGAP29 | S176 | 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 | S949 | 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 | S317 | ochoa | 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}. |
| Q53ET0 | CRTC2 | S70 | ochoa | CREB-regulated transcription coactivator 2 (Transducer of regulated cAMP response element-binding protein 2) (TORC-2) (Transducer of CREB protein 2) | 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 gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific 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:14536081, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:16809310, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408, ECO:0000269|PubMed:17210223}. |
| Q53EU6 | GPAT3 | S68 | ochoa | Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (hGPAT3) (Lung cancer metastasis-associated protein 1) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) (MAG-1) | Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone (PubMed:17170135). Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:19318427). Protects cells against lipotoxicity (PubMed:30846318). {ECO:0000269|PubMed:17170135, ECO:0000269|PubMed:19318427, ECO:0000269|PubMed:30846318}. |
| Q53HL2 | CDCA8 | S224 | 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}. |
| Q5BKX6 | SLC45A4 | S309 | ochoa | Solute carrier family 45 member 4 | Proton-associated sucrose transporter. May be able to transport also glucose and fructose. {ECO:0000250|UniProtKB:Q0P5V9}. |
| Q5H943 | CT83 | S73 | ochoa | Kita-kyushu lung cancer antigen 1 (KK-LC-1) (Cancer/testis antigen 83) | None |
| Q5H9L2 | TCEAL5 | S141 | ochoa | Transcription elongation factor A protein-like 5 (TCEA-like protein 5) (Transcription elongation factor S-II protein-like 5) | May be involved in transcriptional regulation. |
| Q5PRF9 | SAMD4B | S252 | 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 | S336 | 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}. |
| Q5SSJ5 | HP1BP3 | S176 | ochoa | Heterochromatin protein 1-binding protein 3 (Protein HP1-BP74) | Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity (PubMed:24830416). Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self-renewal (PubMed:25100860). {ECO:0000269|PubMed:24830416, ECO:0000269|PubMed:25100860}. |
| 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}. |
| Q5T0W9 | FAM83B | S686 | 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}. |
| Q5T200 | ZC3H13 | S1501 | 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}. |
| Q5T4S7 | UBR4 | S660 | 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}. |
| 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}. |
| Q5T5C0 | STXBP5 | S193 | ochoa | Syntaxin-binding protein 5 (Lethal(2) giant larvae protein homolog 3) (Tomosyn-1) | Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane. Competes with STXBP1 for STX1 binding (By similarity). {ECO:0000250}. |
| Q5T5P2 | KIAA1217 | S169 | ochoa | Sickle tail protein homolog | Required for normal development of intervertebral disks. {ECO:0000250|UniProtKB:A2AQ25}. |
| Q5T6F2 | UBAP2 | S277 | ochoa | Ubiquitin-associated protein 2 (UBAP-2) (RNA polymerase II degradation factor UBAP2) | 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). May promote the degradation of ANXA2 (PubMed:27121050). {ECO:0000269|PubMed:27121050, ECO:0000269|PubMed:35633597}. |
| Q5TBB1 | RNASEH2B | S252 | ochoa | Ribonuclease H2 subunit B (RNase H2 subunit B) (Aicardi-Goutieres syndrome 2 protein) (AGS2) (Deleted in lymphocytic leukemia 8) (Ribonuclease HI subunit B) | Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}. |
| Q5TGY3 | AHDC1 | S179 | ochoa | Transcription factor Gibbin (AT-hook DNA-binding motif-containing protein 1) | Transcription factor required for the proper patterning of the epidermis, which plays a key role in early epithelial morphogenesis (PubMed:35585237). Directly binds promoter and enhancer regions and acts by maintaining local enhancer-promoter chromatin architecture (PubMed:35585237). Interacts with many sequence-specific zinc-finger transcription factors and methyl-CpG-binding proteins to regulate the expression of mesoderm genes that wire surface ectoderm stratification (PubMed:35585237). {ECO:0000269|PubMed:35585237}. |
| Q5THJ4 | VPS13D | S1707 | ochoa | Intermembrane lipid transfer protein VPS13D (Vacuolar protein sorting-associated protein 13D) | Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Functions in promoting mitochondrial clearance by mitochondrial autophagy (mitophagy), also possibly by positively regulating mitochondrial fission (PubMed:29307555, PubMed:29604224). Mitophagy plays an important role in regulating cell health and mitochondrial size and homeostasis. {ECO:0000250|UniProtKB:Q07878, ECO:0000269|PubMed:29307555, ECO:0000269|PubMed:29604224}. |
| 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 | S1793 | 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 | S1876 | 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 | S1893 | 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}. |
| Q5VTQ0 | TTC39B | S125 | ochoa | Tetratricopeptide repeat protein 39B (TPR repeat protein 39B) | Regulates high density lipoprotein (HDL) cholesterol metabolism by promoting the ubiquitination and degradation of the oxysterols receptors LXR (NR1H2 and NR1H3). {ECO:0000250|UniProtKB:Q8BYY4}. |
| Q5VTQ0 | TTC39B | S127 | ochoa | Tetratricopeptide repeat protein 39B (TPR repeat protein 39B) | Regulates high density lipoprotein (HDL) cholesterol metabolism by promoting the ubiquitination and degradation of the oxysterols receptors LXR (NR1H2 and NR1H3). {ECO:0000250|UniProtKB:Q8BYY4}. |
| Q5VWN6 | TASOR2 | S1268 | ochoa | Protein TASOR 2 | None |
| Q5VZ89 | DENND4C | S1183 | 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 | S1205 | 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 | S1627 | 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}. |
| Q5XPI4 | RNF123 | S711 | ochoa | E3 ubiquitin-protein ligase RNF123 (EC 2.3.2.27) (Kip1 ubiquitination-promoting complex protein 1) (RING finger protein 123) | Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase (PubMed:15531880, PubMed:16227581, PubMed:25860612). Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin-dependent kinase inhibitor at the G0-G1 transition of the cell cycle (PubMed:15531880, PubMed:16227581). Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B: acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit (PubMed:25860612, PubMed:33168738, PubMed:34873064). Also functions as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity (PubMed:27312109). Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS (PubMed:27312109). {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:16227581, ECO:0000269|PubMed:25860612, ECO:0000269|PubMed:27312109, ECO:0000269|PubMed:33168738, ECO:0000269|PubMed:34873064}. |
| Q68DC2 | ANKS6 | S660 | ochoa | Ankyrin repeat and SAM domain-containing protein 6 (Ankyrin repeat domain-containing protein 14) (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6) | Required for renal function. {ECO:0000269|PubMed:23793029}. |
| Q6AI08 | HEATR6 | S635 | ochoa | HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1) | Amplification-dependent oncogene. |
| Q6DN14 | MCTP1 | S403 | 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}. |
| Q6IC98 | GRAMD4 | S33 | ochoa | GRAM domain-containing protein 4 (Death-inducing protein) | Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53 (PubMed:15565177). Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53. Inhibits TLR9 response to nucelic acids and regulates TLR9-mediated innate immune response (By similarity). {ECO:0000250|UniProtKB:Q8CB44, ECO:0000269|PubMed:15565177}. |
| Q6IPX3 | TCEAL6 | S135 | ochoa | Transcription elongation factor A protein-like 6 (TCEA-like protein 6) (Transcription elongation factor S-II protein-like 6) | May be involved in transcriptional regulation. |
| Q6NV74 | CRACDL | S881 | ochoa | CRACD-like protein | None |
| Q6NZI2 | CAVIN1 | S127 | ochoa | Caveolae-associated protein 1 (Cavin-1) (Polymerase I and transcript release factor) | Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity). {ECO:0000250|UniProtKB:O54724, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19726876}. |
| Q6P2E9 | EDC4 | S405 | psp | 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}. |
| Q6PGN9 | PSRC1 | S70 | ochoa|psp | Proline/serine-rich coiled-coil protein 1 | Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression. {ECO:0000269|PubMed:18411309, ECO:0000269|PubMed:19738423, ECO:0000269|PubMed:26820536}. |
| Q6PJP8 | DCLRE1A | S333 | ochoa | DNA cross-link repair 1A protein (Beta-lactamase DCLRE1A) (EC 3.5.2.6) (SNM1 homolog A) (hSNM1) (hSNM1A) | May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (PubMed:31434986). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (PubMed:31434986). {ECO:0000269|PubMed:15542852}. |
| Q6Q0C0 | TRAF7 | S317 | 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}. |
| Q6S5L8 | SHC4 | S132 | ochoa|psp | SHC-transforming protein 4 (Rai-like protein) (RaLP) (SHC-transforming protein D) (hShcD) (Src homology 2 domain-containing-transforming protein C4) (SH2 domain protein C4) | Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1. {ECO:0000269|PubMed:17409413}. |
| Q6STE5 | SMARCD3 | S247 | psp | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 (60 kDa BRG-1/Brm-associated factor subunit C) (BRG1-associated factor 60C) (BAF60C) | 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. Stimulates nuclear receptor mediated transcription. 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:Q6P9Z1, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:8804307, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| Q6UXT9 | ABHD15 | S152 | ochoa | Protein ABHD15 (Alpha/beta hydrolase domain-containing protein 15) (Abhydrolase domain-containing protein 15) | May regulate adipocyte lipolysis and liver lipid accumulation. {ECO:0000250|UniProtKB:Q5F2F2}. |
| Q6UXY8 | TMC5 | S184 | ochoa | Transmembrane channel-like protein 5 | Probable component of an ion channel (Probable). Molecular function hasn't been characterized yet (Probable). {ECO:0000305}. |
| Q6VAB6 | KSR2 | S347 | ochoa | Kinase suppressor of Ras 2 (hKSR2) (EC 2.7.11.1) | Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Acts as MAP2K1/MEK1-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 (PubMed:29433126). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production. {ECO:0000269|PubMed:12975377, ECO:0000269|PubMed:16039990, ECO:0000269|PubMed:21441910, ECO:0000269|PubMed:29433126}. |
| Q6VY07 | PACS1 | S355 | 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}. |
| Q6XYQ8 | SYT10 | S221 | ochoa | Synaptotagmin-10 (Synaptotagmin X) (SytX) | Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis (By similarity). Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). {ECO:0000250|UniProtKB:O08625, ECO:0000250|UniProtKB:Q9R0N4}. |
| Q6ZNL6 | FGD5 | S1221 | 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}. |
| Q6ZRV2 | FAM83H | S516 | 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 | 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}. |
| Q6ZSR9 | None | S186 | ochoa | Uncharacterized protein FLJ45252 | None |
| Q6ZU80 | CEP128 | S1033 | ochoa | Centrosomal protein of 128 kDa (Cep128) | None |
| Q6ZVD8 | PHLPP2 | S299 | ochoa | PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like) | Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (PubMed:21986499). Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). {ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466, ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:20513427, ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24530606}. |
| Q6ZW49 | PAXIP1 | S256 | ochoa | PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein) | Involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. Plays a role in early development. In DNA damage response is required for cell survival after ionizing radiation. In vitro shown to be involved in the homologous recombination mechanism for the repair of double-strand breaks (DSBs). Its localization to DNA damage foci requires RNF8 and UBE2N. Recruits TP53BP1 to DNA damage foci and, at least in particular repair processes, effective DNA damage response appears to require the association with TP53BP1 phosphorylated by ATM at 'Ser-25'. Together with TP53BP1 regulates ATM association. Proposed to recruit PAGR1 to sites of DNA damage and the PAGR1:PAXIP1 complex is required for cell survival in response to DNA damage; the function is probably independent of MLL-containing histone methyltransferase (HMT) complexes. However, this function has been questioned (By similarity). Promotes ubiquitination of PCNA following UV irradiation and may regulate recruitment of polymerase eta and RAD51 to chromatin after DNA damage. Proposed to be involved in transcriptional regulation by linking MLL-containing histone methyltransferase (HMT) complexes to gene promoters by interacting with promoter-bound transcription factors such as PAX2. Associates with gene promoters that are known to be regulated by KMT2D/MLL2. During immunoglobulin class switching in activated B-cells is involved in trimethylation of histone H3 at 'Lys-4' and in transcription initiation of downstream switch regions at the immunoglobulin heavy-chain (Igh) locus; this function appears to involve the recruitment of MLL-containing HMT complexes. Conflictingly, its function in transcriptional regulation during immunoglobulin class switching is reported to be independent of the MLL2/MLL3 complex (By similarity). {ECO:0000250|UniProtKB:Q6NZQ4, ECO:0000269|PubMed:14576432, ECO:0000269|PubMed:15456759, ECO:0000269|PubMed:17690115, ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:18353733, ECO:0000269|PubMed:20088963, ECO:0000269|PubMed:23727112}. |
| Q709C8 | VPS13C | S842 | ochoa | Intermembrane lipid transfer protein VPS13C (Vacuolar protein sorting-associated protein 13C) | Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Necessary for proper mitochondrial function and maintenance of mitochondrial transmembrane potential (PubMed:26942284). Involved in the regulation of PINK1/PRKN-mediated mitophagy in response to mitochondrial depolarization (PubMed:26942284). {ECO:0000250|UniProtKB:Q07878, ECO:0000269|PubMed:26942284}. |
| Q71F23 | CENPU | S171 | ochoa | Centromere protein U (CENP-U) (Centromere protein of 50 kDa) (CENP-50) (Interphase centromere complex protein 24) (KSHV latent nuclear antigen-interacting protein 1) (MLF1-interacting protein) (Polo-box-interacting protein 1) | 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. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:17081991}. |
| Q765P7 | MTSS2 | S649 | 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}. |
| Q7KZI7 | MARK2 | S365 | 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}. |
| Q7L1I2 | SV2B | S73 | ochoa | Synaptic vesicle glycoprotein 2B | Probably plays a role in the control of regulated secretion in neural and endocrine cells. {ECO:0000250}.; FUNCTION: (Microbial infection) Receptor for the C.botulinum neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential but enhances the interaction (PubMed:29649119). Probably also serves as a receptor for the closely related C.botulinum neurotoxin type A1. {ECO:0000269|PubMed:29649119, ECO:0000305|PubMed:29649119}. |
| Q7L2E3 | DHX30 | S226 | ochoa | ATP-dependent RNA helicase DHX30 (EC 3.6.4.13) (DEAH box protein 30) | RNA-dependent helicase (PubMed:29100085). Plays an important role in the assembly of the mitochondrial large ribosomal subunit (PubMed:25683715, PubMed:29100085). Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA (PubMed:18063578). Involved in nervous system development and differentiation through its involvement in the up-regulation of a number of genes which are required for neurogenesis, including GSC, NCAM1, neurogenin, and NEUROD (By similarity). {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q99PU8, ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:25683715, ECO:0000269|PubMed:29100085}. |
| Q7L2J0 | MEPCE | S179 | ochoa | 7SK snRNA methylphosphate capping enzyme (MePCE) (EC 2.1.1.-) (Bicoid-interacting protein 3 homolog) (Bin3 homolog) | S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to stabilize it (PubMed:17643375, PubMed:19906723, PubMed:30559425). Also has a non-enzymatic function as part of the 7SK RNP complex: 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:17643375). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). In the 7SK RNP complex, MEPCE is required to stabilize 7SK RNA and facilitate the assembly of 7SK RNP complex (PubMed:19906723, PubMed:38100593). MEPCE has a non-enzymatic function in the 7SK RNP complex; interaction with LARP7 within the 7SK RNP complex occluding its catalytic center (PubMed:19906723). Also required for stability of U6 snRNAs (PubMed:38100593). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:19906723, ECO:0000269|PubMed:28254838, ECO:0000269|PubMed:30559425, ECO:0000269|PubMed:38100593}. |
| Q7L2J0 | MEPCE | S183 | ochoa | 7SK snRNA methylphosphate capping enzyme (MePCE) (EC 2.1.1.-) (Bicoid-interacting protein 3 homolog) (Bin3 homolog) | S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to stabilize it (PubMed:17643375, PubMed:19906723, PubMed:30559425). Also has a non-enzymatic function as part of the 7SK RNP complex: 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:17643375). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). In the 7SK RNP complex, MEPCE is required to stabilize 7SK RNA and facilitate the assembly of 7SK RNP complex (PubMed:19906723, PubMed:38100593). MEPCE has a non-enzymatic function in the 7SK RNP complex; interaction with LARP7 within the 7SK RNP complex occluding its catalytic center (PubMed:19906723). Also required for stability of U6 snRNAs (PubMed:38100593). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:19906723, ECO:0000269|PubMed:28254838, ECO:0000269|PubMed:30559425, ECO:0000269|PubMed:38100593}. |
| Q7L590 | MCM10 | S488 | ochoa | Protein MCM10 homolog (HsMCM10) | Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 (PubMed:24726359). {ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:15136575, ECO:0000269|PubMed:17699597, ECO:0000269|PubMed:19608746, ECO:0000269|PubMed:24726359, ECO:0000269|PubMed:32865517}. |
| Q7L591 | DOK3 | S383 | ochoa | Docking protein 3 (Downstream of tyrosine kinase 3) | DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity). {ECO:0000250}. |
| Q7LBC6 | KDM3B | S458 | 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}. |
| Q7Z2Z1 | TICRR | S1001 | ochoa|psp | 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}. |
| Q7Z333 | SETX | S2472 | ochoa | Probable helicase senataxin (EC 3.6.4.-) (Amyotrophic lateral sclerosis 4 protein) (SEN1 homolog) (Senataxin) | Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224, PubMed:26700805). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111). {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:19515850, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:26700805}. |
| Q7Z3B3 | KANSL1 | S117 | 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}. |
| Q7Z3G6 | PRICKLE2 | S806 | ochoa | Prickle-like protein 2 | None |
| Q7Z401 | DENND4A | S938 | 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}. |
| Q7Z401 | DENND4A | S1609 | 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}. |
| Q7Z402 | TMC7 | S72 | ochoa | Transmembrane channel-like protein 7 | Acts as an inhibitory modulator of PIEZO2 mechanosensitive channel in dorsal root ganglion (DRG) neurons through physical interactions or interference with the interaction between PIEZO2 and the cytoskeleton. {ECO:0000250|UniProtKB:Q8C428}. |
| Q7Z5K2 | WAPL | S95 | ochoa | Wings apart-like protein homolog (Friend of EBNA2 protein) (WAPL cohesin release factor) | Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin (PubMed:26299517). Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203, ECO:0000269|PubMed:26299517}. |
| Q7Z5K2 | WAPL | S380 | ochoa | Wings apart-like protein homolog (Friend of EBNA2 protein) (WAPL cohesin release factor) | Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin (PubMed:26299517). Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203, ECO:0000269|PubMed:26299517}. |
| Q7Z6Z7 | HUWE1 | S3695 | psp | 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}. |
| Q7Z7L8 | C11orf96 | S399 | ochoa | Uncharacterized protein C11orf96 (Protein Ag2 homolog) | None |
| Q86SX3 | TEDC1 | S35 | ochoa | Tubulin epsilon and delta complex protein 1 | Acts as a positive regulator of ciliary hedgehog signaling. Required for centriole stability (By similarity). May play a role in counteracting perturbation of actin filaments, such as after treatment with the actin depolymerizing microbial metabolite Chivosazole F (PubMed:28796488). {ECO:0000250|UniProtKB:Q3UK37, ECO:0000269|PubMed:28796488}. |
| Q86T24 | ZBTB33 | S264 | ochoa | Transcriptional regulator Kaiso (Zinc finger and BTB domain-containing protein 33) | Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. May contribute to the repression of target genes of the Wnt signaling pathway. May also activate transcription of a subset of target genes by the recruitment of CTNND2. Represses expression of MMP7 in conjunction with transcriptional corepressors CBFA2T3, CBFA2T2 and RUNX1T1 (PubMed:23251453). {ECO:0000269|PubMed:11445535, ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:15548582, ECO:0000269|PubMed:15817151, ECO:0000269|PubMed:16354688, ECO:0000269|PubMed:23251453}. |
| 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}. |
| Q86U44 | METTL3 | S350 | ochoa|psp | N(6)-adenosine-methyltransferase catalytic subunit METTL3 (EC 2.1.1.348) (Methyltransferase-like protein 3) (hMETTL3) (N(6)-adenosine-methyltransferase 70 kDa subunit) (MT-A70) | The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:26321680, PubMed:26593424, PubMed:27281194, PubMed:27373337, PubMed:27627798, PubMed:28297716, PubMed:29348140, PubMed:29506078, PubMed:30428350, PubMed:9409616). In the heterodimer formed with METTL14, METTL3 constitutes the catalytic core (PubMed:27281194, PubMed:27373337, PubMed:27627798). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing, translation efficiency and editing (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:26321680, PubMed:26593424, PubMed:28297716, PubMed:9409616). M6A acts as a key regulator of mRNA stability: methylation is completed upon the release of mRNA into the nucleoplasm and promotes mRNA destabilization and degradation (PubMed:28637692). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization, promoting differentiation of ESCs (By similarity). M6A regulates the length of the circadian clock: acts as an early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop (By similarity). M6A also regulates circadian regulation of hepatic lipid metabolism (PubMed:30428350). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (By similarity). Also required for oogenesis (By similarity). Involved in the response to DNA damage: in response to ultraviolet irradiation, METTL3 rapidly catalyzes the formation of m6A on poly(A) transcripts at DNA damage sites, leading to the recruitment of POLK to DNA damage sites (PubMed:28297716). M6A is also required for T-cell homeostasis and differentiation: m6A methylation of transcripts of SOCS family members (SOCS1, SOCS3 and CISH) in naive T-cells promotes mRNA destabilization and degradation, promoting T-cell differentiation (By similarity). Inhibits the type I interferon response by mediating m6A methylation of IFNB (PubMed:30559377). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (PubMed:25799998). Mediates m6A methylation of Xist RNA, thereby participating in random X inactivation: m6A methylation of Xist leads to target YTHDC1 reader on Xist and promote transcription repression activity of Xist (PubMed:27602518). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (By similarity). METTL3 mediates methylation of pri-miRNAs, marking them for recognition and processing by DGCR8 (PubMed:25799998). Acts as a positive regulator of mRNA translation independently of the methyltransferase activity: promotes translation by interacting with the translation initiation machinery in the cytoplasm (PubMed:27117702). Its overexpression in a number of cancer cells suggests that it may participate in cancer cell proliferation by promoting mRNA translation (PubMed:27117702). During human coronavirus SARS-CoV-2 infection, adds m6A modifications in SARS-CoV-2 RNA leading to decreased RIGI binding and subsequently dampening the sensing and activation of innate immune responses (PubMed:33961823). {ECO:0000250|UniProtKB:Q8C3P7, ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:26321680, ECO:0000269|PubMed:26593424, ECO:0000269|PubMed:27117702, ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:27373337, ECO:0000269|PubMed:27602518, ECO:0000269|PubMed:27627798, ECO:0000269|PubMed:28297716, ECO:0000269|PubMed:28637692, ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078, ECO:0000269|PubMed:30428350, ECO:0000269|PubMed:30559377, ECO:0000269|PubMed:33961823, ECO:0000269|PubMed:9409616}. |
| Q86VF7 | NRAP | S1487 | ochoa | Nebulin-related-anchoring protein (N-RAP) | May be involved in anchoring the terminal actin filaments in the myofibril to the membrane and in transmitting tension from the myofibrils to the extracellular matrix. {ECO:0000250|UniProtKB:Q80XB4}. |
| Q86W92 | PPFIBP1 | S434 | 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}. |
| Q86W92 | PPFIBP1 | S638 | 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}. |
| Q86X02 | CDR2L | S180 | ochoa | Cerebellar degeneration-related protein 2-like (Paraneoplastic 62 kDa antigen) | None |
| Q86XL3 | ANKLE2 | S630 | ochoa | Ankyrin repeat and LEM domain-containing protein 2 (LEM domain-containing protein 4) | Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit (PubMed:22770216). Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly (PubMed:22770216). May regulate nuclear localization of VRK1 in non-dividing cells (PubMed:31735666). It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex (PubMed:22770216). Involved in brain development (PubMed:25259927). {ECO:0000269|PubMed:22770216, ECO:0000269|PubMed:25259927, ECO:0000269|PubMed:31735666}. |
| Q86YP4 | GATAD2A | S512 | 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}. |
| Q8IUD2 | ERC1 | S252 | 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}. |
| Q8IUR7 | ARMC8 | S339 | ochoa | Armadillo repeat-containing protein 8 | 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. {ECO:0000269|PubMed:29911972}. |
| Q8IVF2 | AHNAK2 | S797 | ochoa | Protein AHNAK2 | None |
| Q8IVL1 | NAV2 | S1889 | 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}. |
| Q8IW52 | SLITRK4 | S663 | ochoa | SLIT and NTRK-like protein 4 | It is involved in synaptogenesis and promotes synapse differentiation (PubMed:27812321). Suppresses neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q810B8, ECO:0000269|PubMed:27812321}. |
| Q8IWA0 | WDR75 | S672 | ochoa | WD repeat-containing protein 75 (U3 small nucleolar RNA-associated protein 17 homolog) | Ribosome biogenesis factor. 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. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797}. |
| Q8IWE5 | PLEKHM2 | S283 | ochoa | Pleckstrin homology domain-containing family M member 2 (PH domain-containing family M member 2) (Salmonella-induced filaments A and kinesin-interacting protein) (SifA and kinesin-interacting protein) | Plays a role in lysosomes movement and localization at the cell periphery acting as an effector of ARL8B. Required for ARL8B to exert its effects on lysosome location, recruits kinesin-1 to lysosomes and hence direct their movement toward microtubule plus ends. Binding to ARL8B provides a link from lysosomal membranes to plus-end-directed motility (PubMed:22172677, PubMed:24088571, PubMed:25898167, PubMed:28325809). Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). Required for maintenance of the Golgi apparatus organization (PubMed:22172677). May play a role in membrane tubulation (PubMed:15905402). {ECO:0000269|PubMed:15905402, ECO:0000269|PubMed:22172677, ECO:0000269|PubMed:24088571, ECO:0000269|PubMed:25898167, ECO:0000269|PubMed:28325809}. |
| Q8IWT3 | CUL9 | S947 | ochoa | Cullin-9 (CUL-9) (UbcH7-associated protein 1) (p53-associated parkin-like cytoplasmic protein) | Core component of a Cul9-RING ubiquitin-protein ligase complex composed of CUL9 and RBX1 (PubMed:38605244). The CUL9-RBX1 complex mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits the ubiquitination of BIRC5 (PubMed:24793696). The CUL9-RBX1 complex also mediates mono-ubiquitination of p53/TP53 (PubMed:38605244). Acts as a cytoplasmic anchor protein in p53/TP53-associated protein complex. Regulates the subcellular localization of p53/TP53 and its subsequent function (PubMed:12526791, PubMed:17332328). Ubiquitinates apurinic/apyrimidinic endodeoxyribonuclease APEX2 (PubMed:38605244). Ubiquitination by the CUL9-RBX1 complex is predominantly mediated by E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2D2 (PubMed:38605244). {ECO:0000269|PubMed:12526791, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:24793696, ECO:0000269|PubMed:38605244}. |
| Q8IWZ3 | ANKHD1 | S1611 | 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}. |
| Q8IY18 | SMC5 | S506 | ochoa | Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (hSMC5) | Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. 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). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:26983541}. |
| Q8IY63 | AMOTL1 | S828 | ochoa | 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}. |
| Q8IY92 | SLX4 | S1204 | 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}. |
| Q8IYW5 | RNF168 | S411 | ochoa | E3 ubiquitin-protein ligase RNF168 (hRNF168) (EC 2.3.2.27) (RING finger protein 168) (RING-type E3 ubiquitin transferase RNF168) | E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066, ECO:0000269|PubMed:19203578, ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:20550933, ECO:0000269|PubMed:22373579, ECO:0000269|PubMed:22705371, ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:22980979, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538}. |
| Q8IZA0 | KIAA0319L | S978 | 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}. |
| Q8IZD0 | SAMD14 | S64 | ochoa | Sterile alpha motif domain-containing protein 14 (SAM domain-containing protein 14) | None |
| Q8IZH2 | XRN1 | S844 | 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}. |
| Q8IZQ1 | WDFY3 | S970 | ochoa | WD repeat and FYVE domain-containing protein 3 (Autophagy-linked FYVE protein) (Alfy) | Required for selective macroautophagy (aggrephagy). Acts as an adapter protein by linking specific proteins destined for degradation to the core autophagic machinery members, such as the ATG5-ATG12-ATG16L E3-like ligase, SQSTM1 and LC3 (PubMed:20417604). Along with p62/SQSTM1, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with SQSTM1, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Important for normal brain development. Essential for the formation of axonal tracts throughout the brain and spinal cord, including the formation of the major forebrain commissures. Involved in the ability of neural cells to respond to guidance cues. Required for cortical neurons to respond to the trophic effects of netrin-1/NTN1 (By similarity). Regulates Wnt signaling through the removal of DVL3 aggregates, likely in an autophagy-dependent manner. This process may be important for the determination of brain size during embryonic development (PubMed:27008544). May regulate osteoclastogenesis by acting on the TNFSF11/RANKL - TRAF6 pathway (By similarity). After cytokinetic abscission, involved in midbody remnant degradation (PubMed:24128730). In vitro strongly binds to phosphatidylinositol 3-phosphate (PtdIns3P) (PubMed:15292400). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:27008544}. |
| Q8IZT6 | ASPM | S280 | ochoa | Abnormal spindle-like microcephaly-associated protein (Abnormal spindle protein homolog) (Asp homolog) | Involved in mitotic spindle regulation and coordination of mitotic processes. The function in regulating microtubule dynamics at spindle poles including spindle orientation, astral microtubule density and poleward microtubule flux seems to depend on the association with the katanin complex formed by KATNA1 and KATNB1. Enhances the microtubule lattice severing activity of KATNA1 by recruiting the katanin complex to microtubules. Can block microtubule minus-end growth and reversely this function can be enhanced by the katanin complex (PubMed:28436967). May have a preferential role in regulating neurogenesis. {ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:15972725, ECO:0000269|PubMed:28436967}. |
| Q8IZW8 | TNS4 | S197 | ochoa | Tensin-4 (C-terminal tensin-like protein) | Promotes EGF-induced cell migration by displacing tensin TNS3 from the cytoplasmic tail of integrin ITGB1 which results in dissociation of TNS3 from focal adhesions, disassembly of actin stress fibers and initiation of cell migration (PubMed:17643115). Suppresses ligand-induced degradation of EGFR by reducing EGFR ubiquitination in the presence of EGF (PubMed:23774213). Increases MET protein stability by inhibiting MET endocytosis and subsequent lysosomal degradation which leads to increased cell survival, proliferation and migration (PubMed:24814316). {ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:23774213, ECO:0000269|PubMed:24814316}. |
| Q8N0Z3 | SPICE1 | S644 | 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}. |
| Q8N3D4 | EHBP1L1 | S964 | ochoa | EH domain-binding protein 1-like protein 1 | May act as Rab effector protein and play a role in vesicle trafficking. {ECO:0000305|PubMed:27552051}. |
| Q8N3F8 | MICALL1 | S510 | 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}. |
| Q8N3R9 | PALS1 | S25 | ochoa | Protein PALS1 (MAGUK p55 subfamily member 5) (Membrane protein, palmitoylated 5) (Protein associated with Lin-7 1) | Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (PubMed:16678097, PubMed:25385611). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface (By similarity). Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (PubMed:27466317). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing premature differentiation, and is required for cerebellar histogenesis, fissure formation, cerebellar layer organization and cortical development (By similarity). Plays a role in neuronal progenitor cell survival, potentially via promotion of mTOR signaling (By similarity). Plays a role in the radial and longitudinal extension of the myelin sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter (By similarity). Plays a role in the T-cell receptor-mediated activation of NF-kappa-B (PubMed:21479189). Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). Required for the normal polarized localization of the vesicular marker STX4 (By similarity). Required for the correct trafficking of the myelin proteins PMP22 and MAG (By similarity). Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity). {ECO:0000250|UniProtKB:B4F7E7, ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:21479189, ECO:0000269|PubMed:25385611, ECO:0000269|PubMed:27466317}.; FUNCTION: (Microbial infection) Acts as an interaction partner for human coronaviruses SARS-CoV and, probably, SARS-CoV-2 envelope protein E which results in delayed formation of tight junctions and disregulation of cell polarity. {ECO:0000269|PubMed:20861307, ECO:0000303|PubMed:32891874}. |
| Q8N3X1 | FNBP4 | S508 | ochoa | Formin-binding protein 4 (Formin-binding protein 30) | None |
| Q8N4S0 | CCDC82 | S329 | ochoa | Coiled-coil domain-containing protein 82 | None |
| Q8N680 | ZBTB2 | S483 | ochoa | Zinc finger and BTB domain-containing protein 2 | May be involved in transcriptional regulation. |
| Q8N8R7 | ARL14EP | S183 | ochoa | ARL14 effector protein (ARF7 effector protein) | Through its interaction with ARL14 and MYO1E, may connect MHC class II-containing cytoplasmic vesicles to the actin network and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000269|PubMed:21458045}. |
| Q8N9T8 | KRI1 | S536 | ochoa | Protein KRI1 homolog | None |
| Q8NB90 | AFG2A | S250 | ochoa | ATPase family gene 2 protein homolog A (EC 3.6.4.10) (AFG2 AAA ATPase homolog A) (Ribosome biogenesis protein SPATA5) (Spermatogenesis-associated factor protein) (Spermatogenesis-associated protein 5) | ATP-dependent chaperone part of the 55LCC heterohexameric ATPase complex which is chromatin-associated and promotes replisome proteostasis to maintain replication fork progression and genome stability. Required for replication fork progression, sister chromatid cohesion, and chromosome stability. The ATPase activity is specifically enhanced by replication fork DNA and is coupled to cysteine protease-dependent cleavage of replisome substrates in response to replication fork damage. Uses ATPase activity to process replisome substrates in S-phase, facilitating their proteolytic turnover from chromatin to ensure DNA replication and mitotic fidelity (PubMed:38554706). Plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles (PubMed:35354024, PubMed:38554706). May be involved in morphological and functional mitochondrial transformations during spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q3UMC0, ECO:0000269|PubMed:35354024, ECO:0000269|PubMed:38554706}. |
| Q8NCD3 | HJURP | S128 | 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 | S576 | 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}. |
| Q8NCN2 | ZBTB34 | S207 | ochoa | Zinc finger and BTB domain-containing protein 34 | May be a transcriptional repressor. {ECO:0000269|PubMed:16718364}. |
| Q8NDI1 | EHBP1 | S244 | 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}. |
| Q8NEV8 | EXPH5 | S1501 | ochoa | Exophilin-5 (Synaptotagmin-like protein homolog lacking C2 domains b) (SlaC2-b) (Slp homolog lacking C2 domains b) | May act as Rab effector protein and play a role in vesicle trafficking. |
| Q8NEZ5 | FBXO22 | S128 | ochoa | F-box only protein 22 (F-box protein FBX22p44) | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that is implicated in the control of various cellular processes such as cell cycle control, transcriptional regulation, DNA damage repair, and apoptosis. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. Acts as a key regulator of histone methylation marks namely H3K9 and H3K36 methylation through the regulation of histone demethylase KDM4A protein levels (PubMed:21768309). In complex with KDM4A, also regulates the abundance of TP53 by targeting methylated TP53 for degradation at the late senescent stage (PubMed:26868148). Under oxidative stress, promotes the ubiquitination and degradation of BACH1. Mechanistically, reactive oxygen species (ROS) covalently modify cysteine residues on the bZIP domain of BACH1, leading to its release from chromatin and making it accessible to FBXO22 (PubMed:39504958). Upon amino acid depletion, mediates 'Lys-27'-linked ubiquitination of MTOR and thereby inhibits substrate recruitment to mTORC1 (PubMed:37979583). Also inhibits SARS-CoV-2 replication by inducing NSP5 degradation (PubMed:39223933). {ECO:0000269|PubMed:21768309, ECO:0000269|PubMed:22972877, ECO:0000269|PubMed:26868148, ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933, ECO:0000269|PubMed:39504958}. |
| Q8NF91 | SYNE1 | S5919 | 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}. |
| Q8NFA0 | USP32 | S1423 | ochoa | Ubiquitin carboxyl-terminal hydrolase 32 (EC 3.4.19.12) (Deubiquitinating enzyme 32) (Renal carcinoma antigen NY-REN-60) (Ubiquitin thioesterase 32) (Ubiquitin-specific-processing protease 32) | Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1 (PubMed:36476874). Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex (PubMed:36476874). {ECO:0000269|PubMed:36476874}. |
| Q8NH09 | OR8S1 | S289 | ochoa | Olfactory receptor 8S1 | Odorant receptor. {ECO:0000305}. |
| Q8TAA9 | VANGL1 | S325 | ochoa | Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) | None |
| Q8TBA6 | GOLGA5 | S453 | ochoa | Golgin subfamily A member 5 (Cell proliferation-inducing gene 31 protein) (Golgin-84) (Protein Ret-II) (RET-fused gene 5 protein) | Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport. {ECO:0000269|PubMed:12538640, ECO:0000269|PubMed:15718469}. |
| Q8TBZ3 | WDR20 | S360 | 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}. |
| Q8TBZ3 | WDR20 | S491 | 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}. |
| Q8TC07 | TBC1D15 | S205 | ochoa | TBC1 domain family member 15 (GTPase-activating protein RAB7) (GAP for RAB7) (Rab7-GAP) | Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity). {ECO:0000250}. |
| Q8TC44 | POC1B | S398 | ochoa | POC1 centriolar protein homolog B (Pix1) (Proteome of centriole protein 1B) (WD repeat-containing protein 51B) | Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567, PubMed:32060285). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation (PubMed:32060285). Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745). Acts as a positive regulator of centriole elongation (PubMed:37934472). {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:20008567, ECO:0000269|PubMed:23015594, ECO:0000269|PubMed:25044745, ECO:0000269|PubMed:32060285, ECO:0000269|PubMed:37934472}. |
| Q8TC44 | POC1B | S414 | ochoa | POC1 centriolar protein homolog B (Pix1) (Proteome of centriole protein 1B) (WD repeat-containing protein 51B) | Plays an important role in centriole assembly and/or stability and ciliogenesis (PubMed:20008567, PubMed:32060285). Involved in early steps of centriole duplication, as well as in the later steps of centriole length control (PubMed:19109428). Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation (PubMed:32060285). Required for primary cilia formation, ciliary length and also cell proliferation (PubMed:23015594). Required for retinal integrity (PubMed:25044745). Acts as a positive regulator of centriole elongation (PubMed:37934472). {ECO:0000269|PubMed:19109428, ECO:0000269|PubMed:20008567, ECO:0000269|PubMed:23015594, ECO:0000269|PubMed:25044745, ECO:0000269|PubMed:32060285, ECO:0000269|PubMed:37934472}. |
| Q8TCN5 | ZNF507 | S410 | ochoa | Zinc finger protein 507 | May be involved in transcriptional regulation. |
| Q8TCU6 | PREX1 | S1049 | ochoa | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (P-Rex1) (PtdIns(3,4,5)-dependent Rac exchanger 1) | Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils. |
| Q8TD26 | CHD6 | S1654 | ochoa | Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.-) (ATP-dependent helicase CHD6) (Radiation-induced gene B protein) | ATP-dependent chromatin-remodeling factor (PubMed:17027977, PubMed:28533432). Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin; nucleosome disruption requires ATP (PubMed:28533432). Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000269|PubMed:16314513, ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:28533432}.; FUNCTION: (Microbial infection) Acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. {ECO:0000269|PubMed:20631145, ECO:0000269|PubMed:21899694, ECO:0000269|PubMed:23408615}. |
| Q8TD26 | CHD6 | S2402 | ochoa | Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.-) (ATP-dependent helicase CHD6) (Radiation-induced gene B protein) | ATP-dependent chromatin-remodeling factor (PubMed:17027977, PubMed:28533432). Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin; nucleosome disruption requires ATP (PubMed:28533432). Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000269|PubMed:16314513, ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:28533432}.; FUNCTION: (Microbial infection) Acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. {ECO:0000269|PubMed:20631145, ECO:0000269|PubMed:21899694, ECO:0000269|PubMed:23408615}. |
| Q8TDJ6 | DMXL2 | S462 | 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}. |
| Q8TDM6 | DLG5 | S264 | ochoa | Disks large homolog 5 (Discs large protein P-dlg) (Placenta and prostate DLG) | Acts as a regulator of the Hippo signaling pathway (PubMed:28087714, PubMed:28169360). Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714). Positively regulates the Hippo signaling pathway by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (PubMed:28169360). Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin. Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (By similarity). {ECO:0000250|UniProtKB:E9Q9R9, ECO:0000269|PubMed:28087714, ECO:0000269|PubMed:28169360}. |
| Q8TDX7 | NEK7 | S204 | ochoa|psp | Serine/threonine-protein kinase Nek7 (EC 2.7.11.34) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7) | Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:17101132, PubMed:19941817, PubMed:31409757). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (PubMed:17586473, PubMed:19414596, PubMed:19941817, PubMed:26522158, PubMed:31409757). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (PubMed:31409757). Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (PubMed:26642356, PubMed:36442502, PubMed:39173637). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (PubMed:26642356, PubMed:31189953, PubMed:36442502, PubMed:39173637). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (PubMed:26642356, PubMed:31189953). {ECO:0000250|UniProtKB:D3ZBE5, ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473, ECO:0000269|PubMed:19414596, ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158, ECO:0000269|PubMed:26642356, ECO:0000269|PubMed:31189953, ECO:0000269|PubMed:31409757, ECO:0000269|PubMed:36442502, ECO:0000269|PubMed:39173637}. |
| Q8TDY2 | RB1CC1 | S237 | 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}. |
| Q8TE68 | EPS8L1 | S676 | ochoa | Epidermal growth factor receptor kinase substrate 8-like protein 1 (EPS8-like protein 1) (Epidermal growth factor receptor pathway substrate 8-related protein 1) (EPS8-related protein 1) | Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:14565974}. |
| Q8TEB1 | DCAF11 | S147 | ochoa | DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}. |
| Q8TED9 | AFAP1L1 | S361 | ochoa | Actin filament-associated protein 1-like 1 (AFAP1-like protein 1) | May be involved in podosome and invadosome formation. {ECO:0000269|PubMed:21333378}. |
| Q8TEU7 | RAPGEF6 | S1437 | 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}. |
| Q8WUB8 | PHF10 | S56 | 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}. |
| Q8WUF5 | PPP1R13L | S268 | ochoa | RelA-associated inhibitor (Inhibitor of ASPP protein) (Protein iASPP) (NFkB-interacting protein 1) (PPP1R13B-like protein) | Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis (PubMed:12524540). Is involved in NF-kappa-B dependent negative regulation of inflammatory response (PubMed:28069640). {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:12134007, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15489900, ECO:0000269|PubMed:28069640}. |
| Q8WUM0 | NUP133 | S472 | 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}. |
| Q8WUM9 | SLC20A1 | S472 | ochoa | Sodium-dependent phosphate transporter 1 (Gibbon ape leukemia virus receptor 1) (GLVR-1) (Leukemia virus receptor 1 homolog) (Phosphate transporter 1) (PiT-1) (Solute carrier family 20 member 1) | Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:11009570, PubMed:16790504, PubMed:17494632, PubMed:19726692, PubMed:7929240, PubMed:8041748). May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification (PubMed:11009570). Essential for cell proliferation but this function is independent of its phosphate transporter activity (PubMed:19726692). {ECO:0000269|PubMed:11009570, ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:17494632, ECO:0000269|PubMed:19726692, ECO:0000269|PubMed:7929240, ECO:0000269|PubMed:8041748}.; FUNCTION: (Microbial infection) May function as a retroviral receptor as it confers human cells susceptibility to infection to Gibbon Ape Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup B (FeLV-B) as well as 10A1 murine leukemia virus (10A1 MLV). {ECO:0000269|PubMed:12097582, ECO:0000269|PubMed:1309898, ECO:0000269|PubMed:2078500, ECO:0000269|PubMed:7966619}. |
| Q8WUY3 | PRUNE2 | S1639 | ochoa | Protein prune homolog 2 (BNIP2 motif-containing molecule at the C-terminal region 1) | May play an important role in regulating differentiation, survival and aggressiveness of the tumor cells. {ECO:0000269|PubMed:16288218}. |
| Q8WVB6 | CHTF18 | S92 | 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}. |
| Q8WVV4 | POF1B | S93 | 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}. |
| Q8WXH0 | SYNE2 | S765 | ochoa | Nesprin-2 (KASH domain-containing protein 2) (KASH2) (Nuclear envelope spectrin repeat protein 2) (Nucleus and actin connecting element protein) (Protein NUANCE) (Synaptic nuclear envelope protein 2) (Syne-2) | 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 (PubMed:34818527). 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. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 may act redundantly. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. Facilitates the relaxation of mechanical stress imposed by compressive actin fibers at the rupture site through its nteraction with SYN2 (PubMed:34818527). {ECO:0000250|UniProtKB:Q6ZWQ0, ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:22945352, ECO:0000269|PubMed:34818527}. |
| Q8WY36 | BBX | S844 | 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}. |
| Q8WYP5 | AHCTF1 | S1283 | 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 | S1533 | 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}. |
| Q92499 | DDX1 | S700 | ochoa | ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1) (DEAD box protein retinoblastoma) (DBP-RB) | Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity). {ECO:0000250|UniProtKB:Q91VR5, ECO:0000269|PubMed:12183465, ECO:0000269|PubMed:15567440, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18710941, ECO:0000269|PubMed:20573827, ECO:0000269|PubMed:24870230}.; FUNCTION: (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs. {ECO:0000269|PubMed:15567440}.; FUNCTION: (Microbial infection) Required for Coronavirus IBV replication. {ECO:0000269|PubMed:20573827}. |
| Q92519 | TRIB2 | S83 | psp | Tribbles homolog 2 (TRB-2) | Interacts with MAPK kinases and regulates activation of MAP kinases. Does not display kinase activity (By similarity). {ECO:0000250|UniProtKB:Q28283, ECO:0000250|UniProtKB:Q96RU8}. |
| Q92521 | PIGB | S39 | ochoa | GPI alpha-1,2-mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Phosphatidylinositol-glycan biosynthesis class B protein) (PIG-B) | Alpha-1,2-mannosyltransferase that catalyzes the transfer of the third mannose, via an alpha-1,2 bond, from a dolichol-phosphate-mannose (Dol-P-Man) to an alpha-D-Man-(1->6)-2-PEtn-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol intermediate to generate an alpha-D-Man-(1->2)-alpha-D-Man-(1->6)-2-PEtn-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H6) and participates in the nineth step of the glycosylphosphatidylinositol-anchor biosynthesis (PubMed:8861954). May also add the third mannose to an alpha-D-Man-(1->6)-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H3) intermediate generating an alpha-D-Man-(1->2)-alpha-D-Man-(1->6)-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H4) (Probable). {ECO:0000269|PubMed:8861954, ECO:0000305|PubMed:17311586}. |
| Q92523 | CPT1B | S330 | ochoa | Carnitine O-palmitoyltransferase 1, muscle isoform (CPT1-M) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, muscle isoform) (CPT I) (CPTI-M) (Carnitine palmitoyltransferase 1B) (Carnitine palmitoyltransferase I-like protein) | Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. {ECO:0000250|UniProtKB:Q63704}. |
| Q92536 | SLC7A6 | S35 | ochoa | Y+L amino acid transporter 2 (Cationic amino acid transporter, y+ system) (Solute carrier family 7 member 6) (y(+)L-type amino acid transporter 2) (Y+LAT2) (y+LAT-2) | Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (PubMed:10903140, PubMed:11311135, PubMed:14603368, PubMed:15756301, PubMed:16785209, PubMed:17329401, PubMed:19562367, PubMed:31705628, PubMed:9829974). Also exchanges L-arginine with L-lysine in a sodium-independent manner (PubMed:10903140). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (PubMed:10903140). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (PubMed:17197568). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity). {ECO:0000250|UniProtKB:D3ZMM8, ECO:0000250|UniProtKB:Q8BGK6, ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15756301, ECO:0000269|PubMed:16785209, ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401, ECO:0000269|PubMed:19562367, ECO:0000269|PubMed:31705628, ECO:0000269|PubMed:9829974}. |
| Q92551 | IP6K1 | S174 | ochoa | Inositol hexakisphosphate kinase 1 (InsP6 kinase 1) (EC 2.7.4.21) (Inositol hexaphosphate kinase 1) | Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. |
| Q92560 | BAP1 | S276 | ochoa|psp | Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1) (Cerebral protein 6) | Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1 (PubMed:12485996, PubMed:18757409, PubMed:20436459, PubMed:25451922, PubMed:35051358). Catalytic component of the polycomb repressive deubiquitinase (PR-DUB) complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-120' (H2AK119ub1) (PubMed:20436459, PubMed:25451922, PubMed:30664650, PubMed:35051358). Does not deubiquitinate monoubiquitinated histone H2B (PubMed:20436459, PubMed:30664650). 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:20805357, PubMed:30664650, PubMed:36180891). Antagonizes PRC1 mediated H2AK119ub1 monoubiquitination (PubMed:30664650). As part of the PR-DUB complex, associates with chromatin enriched in histone marks H3K4me1, H3K4me3, and H3K27Ac, but not in H3K27me3 (PubMed:36180891). Recruited to specific gene-regulatory regions by YY1 (PubMed:20805357). Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains (PubMed:19188440, PubMed:19815555). Deubiquitination of HCFC1 does not lead to increase stability of HCFC1 (PubMed:19188440, PubMed:19815555). Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination (PubMed:19117993). It however does not mediate deubiquitination of BRCA1 and BARD1 (PubMed:19117993). Able to mediate autodeubiquitination via intramolecular interactions to counteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). 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:0000269|PubMed:12485996, ECO:0000269|PubMed:18757409, ECO:0000269|PubMed:19117993, ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:20436459, ECO:0000269|PubMed:20805357, ECO:0000269|PubMed:24703950, ECO:0000269|PubMed:25451922, ECO:0000269|PubMed:30664650, ECO:0000269|PubMed:34170818, ECO:0000269|PubMed:35051358, ECO:0000269|PubMed:36180891}. |
| Q92574 | TSC1 | S673 | 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}. |
| Q92622 | RUBCN | S946 | 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}. |
| Q92786 | PROX1 | S451 | ochoa | Prospero homeobox protein 1 (Homeobox prospero-like protein PROX1) (PROX-1) | Transcription factor involved in developmental processes such as cell fate determination, gene transcriptional regulation and progenitor cell regulation in a number of organs. Plays a critical role in embryonic development and functions as a key regulatory protein in neurogenesis and the development of the heart, eye lens, liver, pancreas and the lymphatic system. Involved in the regulation of the circadian rhythm. Represses: transcription of the retinoid-related orphan receptor RORG, transcriptional activator activity of RORA and RORG and the expression of RORA/G-target genes including core clock components: BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and ELOVL3. {ECO:0000269|PubMed:23723244, ECO:0000303|PubMed:22733308}. |
| Q92794 | KAT6A | S828 | ochoa | Histone acetyltransferase KAT6A (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3) (MYST-3) (Monocytic leukemia zinc finger protein) (Runt-related transcription factor-binding protein 2) (Zinc finger protein 220) | Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}. |
| Q92835 | INPP5D | S27 | psp | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) (hp51CN) | Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:10764818, PubMed:8723348, PubMed:8769125). Able also to hydrolyzes the 5-phosphate of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (PubMed:10764818, PubMed:8769125, PubMed:9108392). Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity (PubMed:16682172). Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. {ECO:0000269|PubMed:10764818, ECO:0000269|PubMed:12421919, ECO:0000269|PubMed:16682172, ECO:0000269|PubMed:8723348, ECO:0000269|PubMed:8769125, ECO:0000269|PubMed:9108392}. |
| Q92844 | TANK | S228 | ochoa | TRAF family member-associated NF-kappa-B activator (TRAF-interacting protein) (I-TRAF) | Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. Negatively regulates NF-kappaB signaling and cell survival upon DNA damage (PubMed:25861989). Plays a role as an adapter to assemble ZC3H12A, USP10 in a deubiquitination complex which plays a 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). Promotes UBP10-induced deubiquitination of TRAF6 in response to DNA damage (PubMed:25861989). May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2. {ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:25861989}. |
| Q92870 | APBB2 | S229 | ochoa | Amyloid beta precursor protein binding family B member 2 (Amyloid-beta (A4) precursor protein-binding family B member 2) (Protein Fe65-like 1) | Plays a role in the maintenance of lens transparency, and may also play a role in muscle cell strength (By similarity). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning (By similarity). Activates transcription of APP (PubMed:14527950). {ECO:0000250|UniProtKB:Q9DBR4, ECO:0000269|PubMed:14527950}. |
| Q92997 | DVL3 | S140 | 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}. |
| Q93084 | ATP2A3 | S338 | ochoa | Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 (SERCA3) (SR Ca(2+)-ATPase 3) (EC 7.2.2.10) (Calcium pump 3) | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction. {ECO:0000269|PubMed:11956212, ECO:0000269|PubMed:15028735}. |
| Q969E4 | TCEAL3 | S135 | ochoa | Transcription elongation factor A protein-like 3 (TCEA-like protein 3) (Transcription elongation factor S-II protein-like 3) | May be involved in transcriptional regulation. |
| Q969R5 | L3MBTL2 | S335 | psp | 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}. |
| Q969W3 | VCF1 | S144 | ochoa | Protein VCF1 (VCP nuclear cofactor family member 1) | None |
| Q96BD0 | SLCO4A1 | S356 | ochoa | Solute carrier organic anion transporter family member 4A1 (OATP4A1) (Colon organic anion transporter) (Organic anion transporter polypeptide-related protein 1) (OATP-RP1) (OATPRP1) (POAT) (Organic anion-transporting polypeptide E) (OATP-E) (Sodium-independent organic anion transporter E) (Solute carrier family 21 member 12) | Organic anion antiporter with apparent broad substrate specificity. Recognizes various substrates including thyroid hormones 3,3',5-triiodo-L-thyronine (T3), L-thyroxine (T4) and 3,3',5'-triiodo-L-thyronine (rT3), conjugated steroids such as estrone 3-sulfate and estradiol 17-beta glucuronide, bile acids such as taurocholate and prostanoids such as prostaglandin E2, likely operating in a tissue-specific manner (PubMed:10873595, PubMed:19129463, PubMed:30343886). May be involved in uptake of metabolites from the circulation into organs such as kidney, liver or placenta. Possibly drives the selective transport of thyroid hormones and estrogens coupled to an outward glutamate gradient across the microvillous membrane of the placenta (PubMed:30343886). The transport mechanism, its electrogenicity and potential tissue-specific counterions remain to be elucidated (Probable). {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:19129463, ECO:0000269|PubMed:30343886, ECO:0000305}. |
| Q96BK5 | PINX1 | S117 | psp | PIN2/TERF1-interacting telomerase inhibitor 1 (Liver-related putative tumor suppressor) (Pin2-interacting protein X1) (Protein 67-11-3) (TRF1-interacting protein 1) | Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor. {ECO:0000269|PubMed:15381700, ECO:0000269|PubMed:17198684, ECO:0000269|PubMed:19117989, ECO:0000269|PubMed:19265708, ECO:0000269|PubMed:19393617, ECO:0000269|PubMed:19553660}. |
| Q96BY6 | DOCK10 | S292 | 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}. |
| Q96BY7 | ATG2B | S1160 | ochoa | Autophagy-related protein 2 homolog B | Lipid transfer protein required for both autophagosome formation and regulation of lipid droplet morphology and dispersion (PubMed:22219374, PubMed:31721365). 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:22219374, PubMed:31721365). 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 (By similarity). Lipid transfer activity is enhanced by WDR45/WIPI4, which promotes ATG2B-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31721365). {ECO:0000250|UniProtKB:Q2TAZ0, ECO:0000269|PubMed:22219374, ECO:0000269|PubMed:31721365}. |
| Q96D96 | HVCN1 | S97 | psp | Voltage-gated hydrogen channel 1 (Hydrogen voltage-gated channel 1) (HV1) (Voltage sensor domain-only protein) | Voltage-gated proton-selective channel that conducts outward proton currents in response to intracellular acidification. Lacks a canonical ion-channel pore domain and mediates proton permeability via its voltage sensor domain (PubMed:16554753, PubMed:20037153, PubMed:20548053, PubMed:22020278, PubMed:27859356, PubMed:30478045, PubMed:37669933). Appears to play a dominant role in regulation of CO2/HCO3(-)/H(+) equilibrium in sperm flagellum. Prevents the acidification resulting from HCO3(-) synthesis and thus sustains high HCO3(-) levels inside sperm for capacitation (PubMed:20144758, PubMed:30478045, PubMed:37669933). Provides for proton efflux that compensates for electron charge generated by NADPH oxidase activity either in the extracellular or phagosomal compartments, thus enabling the production of high levels of bactericidal reactive oxygen species during the respiratory burst (PubMed:20037153, PubMed:30478045). Opens when the pH of airway surface liquid exceeds 7 and contributes to respiratory epithelial acid secretion to maintain pH in the mucosa (PubMed:20548053). {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:20144758, ECO:0000269|PubMed:20548053, ECO:0000269|PubMed:22020278, ECO:0000269|PubMed:27859356, ECO:0000269|PubMed:30478045, ECO:0000269|PubMed:37669933}. |
| Q96DR7 | ARHGEF26 | S98 | 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}. |
| Q96DX4 | RSPRY1 | S521 | ochoa | RING finger and SPRY domain-containing protein 1 | None |
| Q96E22 | NUS1 | S168 | ochoa | Dehydrodolichyl diphosphate synthase complex subunit NUS1 (EC 2.5.1.87) (Cis-prenyltransferase subunit NgBR) (Nogo-B receptor) (NgBR) (Nuclear undecaprenyl pyrophosphate synthase 1 homolog) | With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (PubMed:32817466). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (PubMed:21572394). Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator (PubMed:16835300). {ECO:0000269|PubMed:16835300, ECO:0000269|PubMed:21572394, ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:28842490, ECO:0000269|PubMed:32817466, ECO:0000269|PubMed:33077723}. |
| Q96EY1 | DNAJA3 | S398 | ochoa | DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57) (Tumorous imaginal discs protein Tid56 homolog) | Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway. |
| Q96F07 | CYFIP2 | S927 | ochoa | Cytoplasmic FMR1-interacting protein 2 (p53-inducible protein 121) | Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:17245118}. |
| Q96FF9 | CDCA5 | S154 | ochoa | 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}. |
| Q96FI4 | NEIL1 | S207 | ochoa|psp | Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (FPG1) (Nei homolog 1) (NEH1) (Nei-like protein 1) | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000269|PubMed:11904416, ECO:0000269|PubMed:12200441, ECO:0000269|PubMed:12509226, ECO:0000269|PubMed:14522990}. |
| Q96FL8 | SLC47A1 | S23 | ochoa | Multidrug and toxin extrusion protein 1 (MATE-1) (hMATE-1) (Solute carrier family 47 member 1) | Multidrug efflux pump that functions as a H(+)/organic cation antiporter (PubMed:16330770, PubMed:17509534). Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively (PubMed:16330770, PubMed:17495125, PubMed:17509534, PubMed:17582384, PubMed:18305230, PubMed:19158817, PubMed:21128598, PubMed:24961373). Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate (PubMed:16330770, PubMed:17495125, PubMed:17509534, PubMed:17582384, PubMed:18305230, PubMed:19158817, PubMed:21128598, PubMed:24961373). May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable). {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:17495125, ECO:0000269|PubMed:17509534, ECO:0000269|PubMed:17582384, ECO:0000269|PubMed:18305230, ECO:0000269|PubMed:19158817, ECO:0000269|PubMed:21128598, ECO:0000269|PubMed:24961373, ECO:0000305|PubMed:35307651}. |
| Q96GN5 | CDCA7L | S162 | ochoa | Cell division cycle-associated 7-like protein (Protein JPO2) (Transcription factor RAM2) | Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1. {ECO:0000269|PubMed:15654081, ECO:0000269|PubMed:15994933, ECO:0000269|PubMed:16829576}. |
| Q96GX5 | MASTL | S217 | 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}. |
| Q96GX5 | MASTL | S660 | 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}. |
| Q96GY0 | ZC2HC1A | S278 | ochoa | Zinc finger C2HC domain-containing protein 1A | None |
| Q96HB5 | CCDC120 | S256 | 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}. |
| Q96I25 | RBM17 | S291 | ochoa|psp | Splicing factor 45 (45 kDa-splicing factor) (RNA-binding motif protein 17) | Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia. {ECO:0000269|PubMed:12015979, ECO:0000269|PubMed:17589525}. |
| Q96IG2 | FBXL20 | S143 | psp | F-box/LRR-repeat protein 20 (F-box and leucine-rich repeat protein 20) (F-box/LRR-repeat protein 2-like) | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Role in neural transmission (By similarity). {ECO:0000250}. |
| Q96IQ9 | ZNF414 | S112 | ochoa | Zinc finger protein 414 | May be involved in transcriptional regulation. |
| Q96JK2 | DCAF5 | S528 | 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}. |
| Q96K21 | ZFYVE19 | S290 | ochoa | Abscission/NoCut checkpoint regulator (ANCHR) (MLL partner containing FYVE domain) (Zinc finger FYVE domain-containing protein 19) | Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission. {ECO:0000269|PubMed:24814515}. |
| Q96K76 | USP47 | S865 | 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}. |
| Q96P20 | NLRP3 | S735 | psp | NACHT, LRR and PYD domains-containing protein 3 (EC 3.6.4.-) (Angiotensin/vasopressin receptor AII/AVP-like) (Caterpiller protein 1.1) (CLR1.1) (Cold-induced autoinflammatory syndrome 1 protein) (Cryopyrin) (PYRIN-containing APAF1-like protein 1) | Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis (PubMed:16407889, PubMed:18403674, PubMed:18604214, PubMed:23582325, PubMed:25686105, PubMed:27929086, PubMed:28656979, PubMed:28847925, PubMed:30487600, PubMed:30612879, PubMed:31086327, PubMed:31086329, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353, PubMed:34512673, PubMed:36442502). In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC (PubMed:16407889, PubMed:18403674, PubMed:27432880, PubMed:28847925, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353, PubMed:36142182, PubMed:36442502). Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis (PubMed:23582325, PubMed:28847925, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353). Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses (PubMed:22801494). Under resting conditions, ADP-bound NLRP3 is autoinhibited (PubMed:35114687). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc (PubMed:16407889, PubMed:18403674, PubMed:18604214, PubMed:19414800, PubMed:23871209). Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex (PubMed:36442502, PubMed:39173637). Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P) (PubMed:30487600, PubMed:34554188). Shows ATPase activity (PubMed:17483456). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000269|PubMed:16407889, ECO:0000269|PubMed:17483456, ECO:0000269|PubMed:18403674, ECO:0000269|PubMed:18604214, ECO:0000269|PubMed:19414800, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:23871209, ECO:0000269|PubMed:25686105, ECO:0000269|PubMed:27432880, ECO:0000269|PubMed:27929086, ECO:0000269|PubMed:28656979, ECO:0000269|PubMed:28847925, ECO:0000269|PubMed:30487600, ECO:0000269|PubMed:30612879, ECO:0000269|PubMed:31086327, ECO:0000269|PubMed:31086329, ECO:0000269|PubMed:31189953, ECO:0000269|PubMed:33231615, ECO:0000269|PubMed:34133077, ECO:0000269|PubMed:34341353, ECO:0000269|PubMed:34554188, ECO:0000269|PubMed:35114687, ECO:0000269|PubMed:36142182, ECO:0000269|PubMed:36442502, ECO:0000269|PubMed:39173637}.; FUNCTION: Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth (By similarity). During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription (By similarity). Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3' (By similarity). May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF (By similarity). {ECO:0000250|UniProtKB:Q8R4B8}. |
| Q96P47 | AGAP3 | S121 | ochoa | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1) | GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}. |
| Q96PU8 | QKI | S64 | ochoa | KH domain-containing RNA-binding protein QKI (Protein quaking) (Hqk) (HqkI) | RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as pre-mRNA splicing, circular RNA (circRNA) formation, mRNA export, mRNA stability and/or translation (PubMed:22398723, PubMed:23630077, PubMed:25768908, PubMed:27029405, PubMed:31331967, PubMed:37379838). Involved in various cellular processes, such as mRNA storage into stress granules, apoptosis, lipid deposition, interferon response, glial cell fate and development (PubMed:25768908, PubMed:31829086, PubMed:34428287, PubMed:37379838). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence (PubMed:23630077). Acts as a mRNA modification reader that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (PubMed:37379838). Promotes the formation of circular RNAs (circRNAs) during the epithelial to mesenchymal transition and in cardiomyocytes: acts by binding to sites flanking circRNA-forming exons (PubMed:25768908). CircRNAs are produced by back-splicing circularization of pre-mRNAs (PubMed:25768908). Plays a central role in myelinization via 3 distinct mechanisms (PubMed:16641098). First, acts by protecting and promoting stability of target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes oligodendrocyte differentiation (By similarity). Second, participates in mRNA transport by regulating the nuclear export of MBP mRNA (By similarity). Finally, indirectly regulates mRNA splicing of MAG pre-mRNA during oligodendrocyte differentiation by acting as a negative regulator of MAG exon 12 alternative splicing: acts by binding to HNRNPA1 mRNA splicing factor, preventing its translation (By similarity). Involved in microglia differentiation and remyelination by regulating microexon alternative splicing of the Rho GTPase pathway (By similarity). Involved in macrophage differentiation: promotes monocyte differentiation by regulating pre-mRNA splicing in naive peripheral blood monocytes (PubMed:27029405). Acts as an important regulator of muscle development: required for the contractile function of cardiomyocytes by regulating alternative splicing of cardiomyocyte transcripts (By similarity). Acts as a negative regulator of thermogenesis by decreasing stability, nuclear export and translation of mRNAs encoding PPARGC1A and UCP1 (By similarity). Also required for visceral endoderm function and blood vessel development (By similarity). May also play a role in smooth muscle development (PubMed:31331967). In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2 (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:16641098, ECO:0000269|PubMed:22398723, ECO:0000269|PubMed:23630077, ECO:0000269|PubMed:25768908, ECO:0000269|PubMed:27029405, ECO:0000269|PubMed:31331967, ECO:0000269|PubMed:31829086, ECO:0000269|PubMed:34428287, ECO:0000269|PubMed:37379838}.; FUNCTION: [Isoform QKI5]: Nuclear isoform that acts as an indirect regulator of mRNA splicing (By similarity). Regulates mRNA splicing of MAG pre-mRNA by inhibiting translation of HNRNPA1 mRNA, thereby preventing MAG exon 12 alternative splicing (By similarity). Involved in oligodendrocyte differentiation by promoting stabilization of SIRT2 mRNA (By similarity). Acts as a negative regulator of the interferon response by binding to MAVS mRNA, downregulating its expression (PubMed:31829086). Also inhibits the interferon response by binding to fibrinectin FN1 pre-mRNA, repressing EDA exon inclusion in FN1 (PubMed:34428287). Delays macrophage differentiation by binding to CSF1R mRNA, promoting its degradation (PubMed:22398723). In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2, promoting SREBF2/SREBP2-dependent cholesterol biosynthesis (By similarity). SREBF2/SREBP2-dependent cholesterol biosynthesis participates to myelinization and is required for eye lens transparency (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:22398723, ECO:0000269|PubMed:31829086, ECO:0000269|PubMed:34428287}.; FUNCTION: [Isoform QKI6]: Cytosolic isoform that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (PubMed:37379838). Interaction with G3BP1 promotes localization of m7G-containing mRNAs into stress granules in response to stress, thereby suppressing their translation (PubMed:37379838). Acts as a translational repressor for HNRNPA1 and GLI1 (By similarity). Translation inhibition of HNRNPA1 during oligodendrocyte differentiation prevents inclusion of exon 12 in MAG pre-mRNA splicing (By similarity). Involved in astrocyte differentiation by regulating translation of target mRNAs (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:37379838}.; FUNCTION: [Isoform QKI7]: Cytosolic isoform that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (PubMed:37379838). Interaction with G3BP1 promotes localization of m7G-containing mRNAs into stress granules in response to stress, thereby suppressing their translation (PubMed:37379838). Acts as a negative regulator of angiogenesis by binding to mRNAs encoding CDH5, NLGN1 and TNFAIP6, promoting their degradation (PubMed:32732889). Can also induce apoptosis in the cytoplasm (By similarity). Heterodimerization with other isoforms results in nuclear translocation of isoform QKI7 and suppression of apoptosis (By similarity). Also binds some microRNAs: promotes stabilitation of miR-122 by mediating recruitment of poly(A) RNA polymerase TENT2, leading to 3' adenylation and stabilization of miR-122 (PubMed:31792053). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:31792053, ECO:0000269|PubMed:32732889, ECO:0000269|PubMed:37379838}. |
| Q96PY6 | NEK1 | S874 | ochoa | Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (Renal carcinoma antigen NY-REN-55) | Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity (PubMed:20230784). Involved in DNA damage checkpoint control and for proper DNA damage repair (PubMed:20230784). In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death (PubMed:20230784). May be implicated in the control of meiosis (By similarity). Involved in cilium assembly (PubMed:21211617). {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:21211617}. |
| Q96Q89 | KIF20B | S1712 | 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}. |
| Q96QK1 | VPS35 | S759 | ochoa | Vacuolar protein sorting-associated protein 35 (hVPS35) (Maternal-embryonic 3) (Vesicle protein sorting 35) | Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:30213940). The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for endosomal localization of WASHC2C (PubMed:22070227, PubMed:28892079). Mediates the association of the CSC with the WASH complex via WASHC2 (PubMed:22070227, PubMed:24819384, PubMed:24980502). Required for the endosomal localization of TBC1D5 (PubMed:20923837). {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:20164305, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502, ECO:0000269|PubMed:28892079, ECO:0000269|PubMed:30213940, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:22070227, ECO:0000303|PubMed:22513087, ECO:0000303|PubMed:23563491}.; FUNCTION: (Microbial infection) The heterotrimeric retromer cargo-selective complex (CSC) mediates the exit of human papillomavirus from the early endosome and the delivery to the Golgi apparatus. {ECO:0000269|PubMed:25693203, ECO:0000269|PubMed:30122350}. |
| Q96QR8 | PURB | S101 | ochoa | Transcriptional regulator protein Pur-beta (Purine-rich element-binding protein B) | Transcriptional regulator which can act as an activator or a repressor. Represses the transcription of ACTA2 in fibroblasts and smooth muscle cells via its ability to interact with the purine-rich strand of a MCAT- containing element in the 5' flanking region of the gene. Represses the transcription of MYOCD, capable of repressing all isoforms of MYOCD but the magnitude of the repressive effects is most notable for the SMC- specific isoforms. Promotes hepatic glucose production by activating the transcription of ADCY6, leading to cAMP accumulation, increased PKA activity, CREB activation, and increased transcription of PCK1 and G6PC genes (By similarity). Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene (PubMed:1448097). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250|UniProtKB:O35295, ECO:0000250|UniProtKB:Q68A21, ECO:0000269|PubMed:1448097}. |
| Q96QT4 | TRPM7 | S103 | 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}. |
| Q96RV3 | PCNX1 | S735 | ochoa | Pecanex-like protein 1 (Pecanex homolog protein 1) | None |
| Q96S53 | TESK2 | S460 | ochoa | Dual specificity testis-specific protein kinase 2 (EC 2.7.12.1) (Testicular protein kinase 2) | Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis. |
| Q96SB4 | SRPK1 | S555 | psp | SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1) | Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. {ECO:0000269|PubMed:10049757, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757, ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240, ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675, ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298, ECO:0000269|PubMed:9237760}. |
| Q96SD1 | DCLRE1C | S503 | 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}. |
| Q96ST3 | SIN3A | S1112 | ochoa | Paired amphipathic helix protein Sin3a (Histone deacetylase complex subunit Sin3a) (Transcriptional corepressor Sin3a) | Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (By similarity). Required for cortical neuron differentiation and callosal axon elongation (By similarity). {ECO:0000250|UniProtKB:Q60520, ECO:0000269|PubMed:12150998}. |
| Q96T49 | PPP1R16B | S333 | psp | Protein phosphatase 1 regulatory inhibitor subunit 16B (Ankyrin repeat domain-containing protein 4) (CAAX box protein TIMAP) (TGF-beta-inhibited membrane-associated protein) (hTIMAP) | Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function (PubMed:18586956). Involved in the regulation of the PI3K/AKT signaling pathway, angiogenesis and endothelial cell proliferation (PubMed:25007873). Regulates angiogenesis and endothelial cell proliferation through the control of ECE1 dephosphorylation, trafficking and activity (By similarity). Protects the endothelial barrier from lipopolysaccharide (LPS)-induced vascular leakage (By similarity). Involved in the regulation of endothelial cell filopodia extension (By similarity). May be a downstream target for TGF-beta1 signaling cascade in endothelial cells (PubMed:16263087, PubMed:18586956). Involved in PKA-mediated moesin dephosphorylation which is important in EC barrier protection against thrombin stimulation (PubMed:18586956). Promotes the interaction of PPP1CA with RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1 (PubMed:16263087). Involved in the dephosphorylation of EEF1A1 (PubMed:26497934). {ECO:0000250|UniProtKB:Q8VHQ3, ECO:0000250|UniProtKB:Q95N27, ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:25007873, ECO:0000269|PubMed:26497934}. |
| Q96T58 | SPEN | S1636 | 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}. |
| Q99081 | TCF12 | S116 | 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}. |
| Q99439 | CNN2 | S217 | ochoa | Calponin-2 (Calponin H2, smooth muscle) (Neutral calponin) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
| Q99613 | EIF3C | S529 | ochoa | Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) | 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_03002, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
| Q99640 | PKMYT1 | S473 | 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}. |
| Q99676 | ZNF184 | S122 | ochoa | Zinc finger protein 184 | May be involved in transcriptional regulation. |
| Q99708 | RBBP8 | S243 | ochoa | DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) | Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117). {ECO:0000250|UniProtKB:Q80YR6, ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462, ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:30601117, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:33836577}. |
| Q99832 | CCT7 | S221 | ochoa | T-complex protein 1 subunit eta (TCP-1-eta) (EC 3.6.1.-) (CCT-eta) (Chaperonin containing T-complex polypeptide 1 subunit 7) (HIV-1 Nef-interacting protein) [Cleaved into: T-complex protein 1 subunit eta, N-terminally processed] | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). {ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| Q9BQI3 | EIF2AK1 | S498 | ochoa | Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-controlled repressor) (HCR) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor) (hHRI) (Hemin-sensitive initiation factor 2-alpha kinase) | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock (PubMed:32132706, PubMed:32132707, PubMed:37327776, PubMed:37550454, PubMed:38340717). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707, PubMed:37327776). Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity (By similarity). This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR (By similarity). Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions (By similarity). In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties (By similarity). It thereby plays an essential protective role for RBC survival in anemias of iron deficiency (By similarity). Iron deficiency also triggers activation by full-length DELE1 (PubMed:37327776). Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (PubMed:32132706, PubMed:32132707). Also acts as an activator of mitophagy in response to mitochondrial damage: catalyzes phosphorylation of eIF-2-alpha (EIF2S1) following activation by S-DELE1, thereby promoting mitochondrial localization of EIF2S1, triggering PRKN-independent mitophagy (PubMed:38340717). {ECO:0000250|UniProtKB:Q9Z2R9, ECO:0000269|PubMed:32132706, ECO:0000269|PubMed:32132707, ECO:0000269|PubMed:32197074, ECO:0000269|PubMed:37550454, ECO:0000269|PubMed:38340717}. |
| Q9BQI7 | PSD2 | S478 | ochoa | PH and SEC7 domain-containing protein 2 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 C) (Exchange factor for ARF6 C) (Pleckstrin homology and SEC7 domain-containing protein 2) | None |
| Q9BQK8 | LPIN3 | S162 | ochoa | Phosphatidate phosphatase LPIN3 (EC 3.1.3.4) (Lipin-3) (Lipin-3-like) | Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis therefore regulates fatty acid metabolism. {ECO:0000250|UniProtKB:Q99PI4}. |
| Q9BRJ6 | C7orf50 | S175 | ochoa | Protein cholesin | Hormone secreted from the intestine in response to cholesterol, where it acts to inhibit cholesterol synthesis in the liver and VLDL secretion,leading to a reduction in circulating cholesterol levels. Acts through binding to its receptor, GPR146. {ECO:0000269|PubMed:38503280}. |
| Q9BRS2 | RIOK1 | S21 | ochoa | 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}. |
| Q9BRT9 | GINS4 | S123 | ochoa | DNA replication complex GINS protein SLD5 (GINS complex subunit 4) [Cleaved into: DNA replication complex GINS protein SLD5, N-terminally processed] | Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks (PubMed:17417653, PubMed:28414293). GINS complex is a 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). {ECO:0000269|PubMed:17417653, ECO:0000269|PubMed:28414293, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232}. |
| Q9BSJ8 | ESYT1 | S1067 | ochoa | Extended synaptotagmin-1 (E-Syt1) (Membrane-bound C2 domain-containing protein) | Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels (PubMed:23791178, PubMed:24183667). Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane (PubMed:24183667). Acts as an inhibitor of ADGRD1 G-protein-coupled receptor activity in absence of cytosolic calcium (PubMed:38758649). Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). {ECO:0000250|UniProtKB:A0FGR8, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24183667, ECO:0000269|PubMed:38758649}. |
| Q9BTF0 | THUMPD2 | S457 | ochoa | U6 snRNA (guanine-N(2))-methyltransferase THUMPD2 (EC 2.1.1.-) (THUMP domain-containing protein 2) | Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine-dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome (PubMed:37283053). This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels (PubMed:37283053). {ECO:0000269|PubMed:37283053}. |
| Q9BU70 | TRMO | S214 | ochoa | tRNA (adenine(37)-N6)-methyltransferase (EC 2.1.1.-) (tRNA methyltransferase O) | S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU) (PubMed:25063302). The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability (By similarity). {ECO:0000250|UniProtKB:P28634, ECO:0000269|PubMed:25063302}. |
| Q9BVJ6 | UTP14A | S445 | ochoa | U3 small nucleolar RNA-associated protein 14 homolog A (Antigen NY-CO-16) (Serologically defined colon cancer antigen 16) | May be required for ribosome biogenesis. {ECO:0000250}. |
| Q9BVV6 | KIAA0586 | S406 | ochoa | Protein TALPID3 | Required for ciliogenesis and sonic hedgehog/SHH signaling. Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation (PubMed:24421332). Involved in regulation of cell intracellular organization. Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles (By similarity). {ECO:0000250|UniProtKB:E9PV87, ECO:0000250|UniProtKB:Q1G7G9, ECO:0000269|PubMed:24421332}. |
| Q9BWH6 | RPAP1 | S277 | ochoa | RNA polymerase II-associated protein 1 | Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Required for interaction of the RNA polymerase II complex with acetylated histone H3. {ECO:0000269|PubMed:17643375}. |
| Q9BX40 | LSM14B | S323 | ochoa | Protein LSM14 homolog B (RNA-associated protein 55B) (hRAP55B) | mRNA-binding protein essential for female fertility, oocyte meiotic maturation and the assembly of MARDO (mitochondria-associated ribonucleoprotein domain), a membraneless compartment that stores maternal mRNAs in oocytes. Ensures the proper accumulation and clearance of mRNAs essential for oocyte meiotic maturation and the normal progression from Meiosis I to Meiosis II in oocytes. Promotes the translation of some oogenesis-related mRNAs. Regulates the expression and/or localization of some key P-body proteins in oocytes. Essential for the assembly of the primordial follicle in the ovary. {ECO:0000250|UniProtKB:Q8CGC4}. |
| Q9BX66 | SORBS1 | S556 | 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}. |
| Q9BXF6 | RAB11FIP5 | S207 | 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}. |
| Q9BXT4 | TDRD1 | S685 | ochoa | Tudor domain-containing protein 1 (Cancer/testis antigen 41.1) (CT41.1) | Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins (By similarity). {ECO:0000250}. |
| Q9BXW9 | FANCD2 | S898 | 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}. |
| Q9BYG5 | PARD6B | S102 | ochoa | Partitioning defective 6 homolog beta (PAR-6 beta) (PAR-6B) | Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. |
| Q9BYJ9 | YTHDF1 | S198 | ochoa | YTH domain-containing family protein 1 (DF1) (Dermatomyositis associated with cancer putative autoantigen 1) (DACA-1) | Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability (PubMed:24284625, PubMed:26318451, PubMed:32492408, PubMed:39900921). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:24284625, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) shares m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:32492408). Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs (By similarity). Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts (By similarity). Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells (By similarity). In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation (By similarity). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31292544, PubMed:31388144, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). {ECO:0000250|UniProtKB:P59326, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:31292544, ECO:0000269|PubMed:31388144, ECO:0000269|PubMed:32451507, ECO:0000269|PubMed:32492408, ECO:0000269|PubMed:39900921}. |
| Q9BZD4 | NUF2 | S247 | ochoa | Kinetochore protein Nuf2 (hNuf2) (hNuf2R) (hsNuf2) (Cell division cycle-associated protein 1) | Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12438418, PubMed:14654001, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:17535814). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592). 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). {ECO:0000269|PubMed:12438418, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:23085020}. |
| Q9BZZ2 | SIGLEC1 | S654 | ochoa | Sialoadhesin (Sialic acid-binding Ig-like lectin 1) (Siglec-1) (CD antigen CD169) | Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response (PubMed:12940982, PubMed:33489013). Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs) (PubMed:28129379). In turn, enhances macrophage-to-T-cell transmission of several viruses including HIV-1 or SARS-CoV-2 (PubMed:28129379, PubMed:34782760). Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid (PubMed:12940982). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination (PubMed:26358190). {ECO:0000250|UniProtKB:Q62230, ECO:0000269|PubMed:12940982, ECO:0000269|PubMed:26358190, ECO:0000269|PubMed:28129379, ECO:0000269|PubMed:33489013, ECO:0000269|PubMed:34782760}.; FUNCTION: (Microbial infection) Facilitates viral cytoplasmic entry into activated dendritic cells via recognition of sialylated gangliosides pesent on viral membrane. {ECO:0000269|PubMed:31160823}. |
| Q9C0C2 | TNKS1BP1 | S1677 | ochoa | 182 kDa tankyrase-1-binding protein | None |
| Q9C0D5 | TANC1 | S243 | 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}. |
| Q9C0K0 | BCL11B | S110 | ochoa | B-cell lymphoma/leukemia 11B (BCL-11B) (B-cell CLL/lymphoma 11B) (COUP-TF-interacting protein 2) (Radiation-induced tumor suppressor gene 1 protein) (hRit1) | Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals. Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of the receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (PubMed:27959755). Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4(+) T-lymphocytes (PubMed:16809611). Tumor-suppressor that represses transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity). May also function in the P53-signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q99PV8, ECO:0000269|PubMed:16809611, ECO:0000269|PubMed:27959755}. |
| Q9GZR2 | REXO4 | S226 | ochoa | RNA exonuclease 4 (EC 3.1.-.-) (Exonuclease XPMC2) (Prevents mitotic catastrophe 2 protein homolog) (hPMC2) | None |
| Q9GZV5 | WWTR1 | S60 | ochoa | 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}. |
| Q9GZY6 | LAT2 | S51 | ochoa | Linker for activation of T-cells family member 2 (Linker for activation of B-cells) (Membrane-associated adapter molecule) (Non-T-cell activation linker) (Williams-Beuren syndrome chromosomal region 15 protein) (Williams-Beuren syndrome chromosomal region 5 protein) | Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2. {ECO:0000269|PubMed:12486104, ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:15010370}. |
| Q9H089 | LSG1 | S93 | ochoa | Large subunit GTPase 1 homolog (hLsg1) (EC 3.6.5.-) | Functions as a GTPase (PubMed:16209721). May act by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm during the 60S ribosomal subunit maturation (PubMed:31148378). {ECO:0000269|PubMed:16209721, ECO:0000269|PubMed:31148378}. |
| Q9H0B6 | KLC2 | S589 | ochoa | Kinesin light chain 2 (KLC 2) | Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends (PubMed:22172677). {ECO:0000269|PubMed:22172677, ECO:0000305|PubMed:22172677}. |
| Q9H0E9 | BRD8 | S579 | 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}. |
| Q9H0K1 | SIK2 | S90 | psp | Serine/threonine-protein kinase SIK2 (EC 2.7.11.1) (Qin-induced kinase) (Salt-inducible kinase 2) (SIK-2) (Serine/threonine-protein kinase SNF1-like kinase 2) | Serine/threonine-protein kinase that plays a role in many biological processes such as fatty acid oxidation, autophagy, immune response or glucose metabolism (PubMed:23322770, PubMed:26983400). Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators (PubMed:15454081). Phosphorylates EP300 and thus inhibits its histone acetyltransferase activity (PubMed:21084751, PubMed:26983400). In turn, regulates the DNA-binding ability of several transcription factors such as PPARA or MLXIPL (PubMed:21084751, PubMed:26983400). Also plays a role in thymic T-cell development (By similarity). {ECO:0000250|UniProtKB:Q8CFH6, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:21084751, ECO:0000269|PubMed:23322770, ECO:0000269|PubMed:26983400}. |
| Q9H165 | BCL11A | S114 | 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}. |
| Q9H2M9 | RAB3GAP2 | S875 | ochoa | Rab3 GTPase-activating protein non-catalytic subunit (RGAP-iso) (Rab3 GTPase-activating protein 150 kDa subunit) (Rab3-GAP p150) (Rab3-GAP150) (Rab3-GAP regulatory subunit) | Regulatory subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18 (PubMed:24891604, PubMed:9733780). As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (By similarity). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (By similarity). The Rab3GAP complex acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604). Recruits and stabilizes RAB18 at the cis-Golgi membrane in human fibroblasts where RAB18 is most likely activated (PubMed:26063829). Also involved in RAB18 recruitment at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604). Required for normal eye and brain development (By similarity). May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity). {ECO:0000250|UniProtKB:Q15042, ECO:0000269|PubMed:24891604, ECO:0000269|PubMed:26063829, ECO:0000269|PubMed:9733780}. |
| Q9H2T7 | RANBP17 | S296 | ochoa | Ran-binding protein 17 | May function as a nuclear transport receptor. {ECO:0000250}. |
| Q9H583 | HEATR1 | S1195 | ochoa | HEAT repeat-containing protein 1 (Protein BAP28) (U3 small nucleolar RNA-associated protein 10 homolog) [Cleaved into: HEAT repeat-containing protein 1, N-terminally processed] | Ribosome biogenesis factor; required for recruitment of Myc to nucleoli (PubMed:38225354). Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I (PubMed:17699751). 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). Involved in neuronal-lineage cell proliferation (PubMed:38225354). {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:38225354}. |
| Q9H5H4 | ZNF768 | S160 | ochoa | Zinc finger protein 768 | Binds to mammalian-wide interspersed repeat (MIRs) sequences in euchromatin and promoter regions of genes at the consensus sequence 5'-GCTGTGTG-[N20]-CCTCTCTG-3', consisting of two anchor regions connected by a linker region; the linker region probably does not contribute to the binding specificity (PubMed:30476274). Required for cell homeostasis (PubMed:34404770). May be involved in transcriptional regulation (Probable). {ECO:0000269|PubMed:30476274, ECO:0000269|PubMed:34404770, ECO:0000305}. |
| Q9H6R7 | WDCP | S485 | ochoa | WD repeat and coiled-coil-containing protein | None |
| Q9H6T3 | RPAP3 | S116 | ochoa|psp | RNA polymerase II-associated protein 3 | Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. {ECO:0000269|PubMed:17643375}. |
| Q9H6U6 | BCAS3 | S154 | 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 | S590 | 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}. |
| Q9H9G7 | AGO3 | S825 | ochoa | Protein argonaute-3 (Argonaute3) (hAgo3) (EC 3.1.26.n2) (Argonaute RISC catalytic component 3) (Eukaryotic translation initiation factor 2C 3) (eIF-2C 3) (eIF2C 3) | Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Proposed to be involved in stabilization of small RNA derivates (siRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent siRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. Possesses RNA slicer activity but only on select RNAs bearing 5'- and 3'-flanking sequences to the region of guide-target complementarity (PubMed:29040713). {ECO:0000255|HAMAP-Rule:MF_03032, ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:23064648, ECO:0000269|PubMed:29040713}. |
| Q9HAB8 | PPCS | S199 | ochoa | Phosphopantothenate--cysteine ligase (EC 6.3.2.51) (Phosphopantothenoylcysteine synthetase) (PPC synthetase) | Catalyzes the second step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine (PubMed:11923312, PubMed:12906824, PubMed:29754768). Has a preference for ATP over CTP as a cosubstrate (PubMed:11923312). {ECO:0000269|PubMed:11923312, ECO:0000269|PubMed:12906824, ECO:0000269|PubMed:29754768}. |
| Q9HAU0 | PLEKHA5 | S860 | 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 |
| Q9HCD6 | TANC2 | S430 | 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}. |
| Q9HCE0 | EPG5 | S1393 | ochoa | Ectopic P granules protein 5 homolog | Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. Plays a key role in innate and adaptive immune response triggered by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides from pathogens, and mediated by the nucleotide-sensing receptor TLR9. It is necessary for the translocation of CpG dinucleotides from early endosomes to late endosomes and lysosomes, where TLR9 is located (PubMed:29130391). {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:23222957, ECO:0000269|PubMed:29130391}. |
| Q9HCK1 | ZDBF2 | S631 | ochoa | DBF4-type zinc finger-containing protein 2 | None |
| Q9HCL2 | GPAM | S604 | ochoa | Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAT-1) (EC 2.3.1.15) | Mitochondrial membrane protein that catalyzes the essential first step of biosynthesis of glycerolipids such as triglycerides, phosphatidic acids and lysophosphatidic acids (PubMed:18238778, PubMed:19075029, PubMed:36522428). Esterifies acyl-group from acyl-coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to produce lysophosphatidic acid (PubMed:18238778). Has a narrow hydrophobic binding cleft that selects for a linear acyl chain (PubMed:36522428). Catalytic activity is higher for substrates with a 16-carbon acyl chain (PubMed:36522428). {ECO:0000269|PubMed:18238778, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:36522428}. |
| Q9NPA3 | MID1IP1 | S75 | ochoa | Mid1-interacting protein 1 (Gastrulation-specific G12-like protein) (Mid1-interacting G12-like protein) (Protein STRAIT11499) (Spot 14-related protein) (S14R) (Spot 14-R) | Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity). {ECO:0000250}. |
| Q9NQ39 | RPS10P5 | S76 | ochoa | Putative ribosomal protein eS10-like (Putative 40S ribosomal protein S10-like) | None |
| Q9NQ84 | GPRC5C | S359 | ochoa | G-protein coupled receptor family C group 5 member C (Retinoic acid-induced gene 3 protein) (RAIG-3) | This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways. {ECO:0000250}. |
| Q9NQW6 | ANLN | S502 | 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}. |
| Q9NR30 | DDX21 | S597 | ochoa | Nucleolar RNA helicase 2 (EC 3.6.4.13) (DEAD box protein 21) (Gu-alpha) (Nucleolar RNA helicase Gu) (Nucleolar RNA helicase II) (RH II/Gu) | RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as a cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins (PubMed:28431233). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305}. |
| Q9NRE2 | TSHZ2 | S980 | ochoa | Teashirt homolog 2 (Ovarian cancer-related protein 10-2) (OVC10-2) (Zinc finger protein 218) | Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential). {ECO:0000305}. |
| Q9NRS6 | SNX15 | S194 | ochoa | Sorting nexin-15 | May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN. {ECO:0000269|PubMed:11085978}. |
| Q9NSC5 | HOMER3 | S256 | ochoa | Homer protein homolog 3 (Homer-3) | Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (PubMed:18218901). {ECO:0000269|PubMed:18218901}. |
| 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}. |
| Q9NVA4 | TMEM184C | S344 | ochoa | Transmembrane protein 184C (Transmembrane protein 34) | Possible tumor suppressor which may play a role in cell growth. {ECO:0000269|PubMed:17072649}. |
| Q9NVI1 | FANCI | S1120 | ochoa | 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}. |
| Q9NVS9 | PNPO | S241 | ochoa | Pyridoxine-5'-phosphate oxidase (EC 1.4.3.5) (Pyridoxamine-phosphate oxidase) | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000269|PubMed:12824491, ECO:0000269|PubMed:15182361, ECO:0000269|PubMed:15772097}. |
| Q9NWH9 | SLTM | S244 | 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}. |
| Q9NWZ3 | IRAK4 | S114 | psp | 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}. |
| Q9NX46 | ADPRS | S67 | ochoa | ADP-ribosylhydrolase ARH3 (ADP-ribose glycohydrolase ARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-) | ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:21498885, PubMed:29907568, PubMed:30045870, PubMed:30401461, PubMed:30830864, PubMed:33186521, PubMed:33769608, PubMed:33894202, PubMed:34019811, PubMed:34321462, PubMed:34479984, PubMed:34625544). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:28650317, PubMed:29234005, PubMed:30045870, PubMed:33186521, PubMed:34019811, PubMed:34625544). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802, PubMed:33186521, PubMed:34625544). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed:16278211, PubMed:33769608). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed:22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed:17075046, PubMed:21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed:21498885). {ECO:0000269|PubMed:16278211, ECO:0000269|PubMed:17075046, ECO:0000269|PubMed:21498885, ECO:0000269|PubMed:22433848, ECO:0000269|PubMed:28650317, ECO:0000269|PubMed:29234005, ECO:0000269|PubMed:29480802, ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0000269|PubMed:30401461, ECO:0000269|PubMed:30830864, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:33769608, ECO:0000269|PubMed:33894202, ECO:0000269|PubMed:34019811, ECO:0000269|PubMed:34321462, ECO:0000269|PubMed:34479984, ECO:0000269|PubMed:34625544}. |
| Q9NX95 | SYBU | S396 | ochoa | Syntabulin (Golgi-localized syntaphilin-related protein) (Syntaxin-1-binding protein) | Part of a kinesin motor-adapter complex that is critical for the anterograde axonal transport of active zone components and contributes to activity-dependent presynaptic assembly during neuronal development. {ECO:0000250, ECO:0000269|PubMed:15459722}. |
| Q9NXH8 | TOR4A | S106 | ochoa | Torsin-4A (Torsin family 4 member A) | None |
| Q9NYB0 | TERF2IP | S179 | 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}. |
| Q9NYL2 | MAP3K20 | S362 | 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}. |
| Q9NYQ7 | CELSR3 | S3058 | ochoa | Cadherin EGF LAG seven-pass G-type receptor 3 (Cadherin family member 11) (Epidermal growth factor-like protein 1) (EGF-like protein 1) (Flamingo homolog 1) (hFmi1) (Multiple epidermal growth factor-like domains protein 2) (Multiple EGF-like domains protein 2) | Receptor that may have an important role in cell/cell signaling during nervous system formation. |
| Q9NZM1 | MYOF | S1915 | ochoa | Myoferlin (Fer-1-like protein 3) | Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}. |
| Q9NZM5 | NOP53 | S93 | ochoa | Ribosome biogenesis protein NOP53 (Glioma tumor suppressor candidate region gene 2 protein) (Protein interacting with carboxyl terminus 1) (PICT-1) (p60) | Nucleolar protein which is involved in the integration of the 5S RNP into the ribosomal large subunit during ribosome biogenesis (PubMed:24120868). In ribosome biogenesis, may also play a role in rRNA transcription (PubMed:27729611). Also functions as a nucleolar sensor that regulates the activation of p53/TP53 in response to ribosome biogenesis perturbation, DNA damage and other stress conditions (PubMed:21741933, PubMed:24120868, PubMed:27829214). DNA damage or perturbation of ribosome biogenesis disrupt the interaction between NOP53 and RPL11 allowing RPL11 transport to the nucleoplasm where it can inhibit MDM2 and allow p53/TP53 activation (PubMed:24120868, PubMed:27829214). It may also positively regulate the function of p53/TP53 in cell cycle arrest and apoptosis through direct interaction, preventing its MDM2-dependent ubiquitin-mediated proteasomal degradation (PubMed:22522597). Originally identified as a tumor suppressor, it may also play a role in cell proliferation and apoptosis by positively regulating the stability of PTEN, thereby antagonizing the PI3K-AKT/PKB signaling pathway (PubMed:15355975, PubMed:16971513, PubMed:27729611). May also inhibit cell proliferation and increase apoptosis through its interaction with NF2 (PubMed:21167305). May negatively regulate NPM1 by regulating its nucleoplasmic localization, oligomerization and ubiquitin-mediated proteasomal degradation (PubMed:25818168). Thereby, may prevent NPM1 interaction with MYC and negatively regulate transcription mediated by the MYC-NPM1 complex (PubMed:25956029). May also regulate cellular aerobic respiration (PubMed:24556985). In the cellular response to viral infection, may play a role in the attenuation of interferon-beta through the inhibition of RIGI (PubMed:27824081). {ECO:0000269|PubMed:15355975, ECO:0000269|PubMed:16971513, ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:21741933, ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24120868, ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}. |
| Q9P0J7 | KCMF1 | S212 | 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}. |
| Q9P0L0 | VAPA | S214 | ochoa | Vesicle-associated membrane protein-associated protein A (VAMP-A) (VAMP-associated protein A) (VAP-A) (33 kDa VAMP-associated protein) (VAP-33) | Endoplasmic reticulum (ER)-anchored protein that mediates the formation of contact sites between the ER and endosomes via interaction with FFAT motif-containing proteins such as STARD3 or WDR44 (PubMed:32344433, PubMed:33124732). STARD3-VAPA interaction enables cholesterol transfer from the ER to endosomes (PubMed:33124732). Via interaction with WDR44 participates in neosynthesized protein export (PubMed:32344433). In addition, recruited to the plasma membrane through OSBPL3 binding (PubMed:25447204). The OSBPL3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:25447204). With OSBPL3, may regulate ER morphology (PubMed:16143324). May play a role in vesicle trafficking (PubMed:11511104, PubMed:19289470). {ECO:0000269|PubMed:11511104, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:19289470, ECO:0000269|PubMed:25447204, ECO:0000269|PubMed:32344433, ECO:0000269|PubMed:33124732}. |
| Q9P244 | LRFN1 | S659 | ochoa | Leucine-rich repeat and fibronectin type III domain-containing protein 1 (Synaptic adhesion-like molecule 2) | Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1 (By similarity). {ECO:0000250}. |
| Q9P273 | TENM3 | S116 | ochoa | Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3) | Involved in neural development by regulating the establishment of proper connectivity within the nervous system. Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion. Required for proper dendrite morphogenesis and axon targeting in the vertebrate visual system, thereby playing a key role in the development of the visual pathway. Regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC). May also be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes. {ECO:0000250|UniProtKB:Q9WTS6}. |
| Q9P2F8 | SIPA1L2 | S194 | ochoa | Signal-induced proliferation-associated 1-like protein 2 (SIPA1-like protein 2) | None |
| Q9P2F8 | SIPA1L2 | S389 | ochoa | Signal-induced proliferation-associated 1-like protein 2 (SIPA1-like protein 2) | None |
| Q9P2Y5 | UVRAG | S571 | ochoa|psp | UV radiation resistance-associated gene protein (p63) | Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:16799551, PubMed:18552835, PubMed:20643123, PubMed:24056303, PubMed:28306502). During autophagy acts as a regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3 (PubMed:16799551, PubMed:20643123, PubMed:24056303, PubMed:28306502). Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 (PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events (PubMed:18552835, PubMed:28306502). Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion (PubMed:24550300). In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (PubMed:24550300). {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:24056303, ECO:0000269|PubMed:28306502, ECO:0000305}.; FUNCTION: Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ) (PubMed:22542840). Required for centrosome stability and proper chromosome segregation (PubMed:22542840). {ECO:0000269|PubMed:22542840}. |
| Q9P2Y5 | UVRAG | S582 | psp | UV radiation resistance-associated gene protein (p63) | Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:16799551, PubMed:18552835, PubMed:20643123, PubMed:24056303, PubMed:28306502). During autophagy acts as a regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3 (PubMed:16799551, PubMed:20643123, PubMed:24056303, PubMed:28306502). Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 (PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events (PubMed:18552835, PubMed:28306502). Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion (PubMed:24550300). In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (PubMed:24550300). {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:24056303, ECO:0000269|PubMed:28306502, ECO:0000305}.; FUNCTION: Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ) (PubMed:22542840). Required for centrosome stability and proper chromosome segregation (PubMed:22542840). {ECO:0000269|PubMed:22542840}. |
| Q9UBN7 | HDAC6 | S146 | psp | Protein deacetylase HDAC6 (EC 3.5.1.-) (E3 ubiquitin-protein ligase HDAC6) (EC 2.3.2.-) (Tubulin-lysine deacetylase HDAC6) (EC 3.5.1.-) | Deacetylates a wide range of non-histone substrates (PubMed:12024216, PubMed:18606987, PubMed:20308065, PubMed:24882211, PubMed:26246421, PubMed:30538141, PubMed:31857589, PubMed:30770470, PubMed:38534334, PubMed:39567688). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed:12024216, PubMed:20308065, PubMed:26246421). Required for cilia disassembly via deacetylation of alpha-tubulin (PubMed:17604723, PubMed:26246421). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141). Deacetylates SQSTM1 (PubMed:31857589). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (PubMed:18606987). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities (PubMed:24882211). Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage (PubMed:30770470). Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity). Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis (PubMed:38534334). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed:26080397). Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region (PubMed:39567688). In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage (PubMed:39567688). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (By similarity). In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome (PubMed:17846173). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy (PubMed:17846173). Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer (PubMed:24413532). {ECO:0000250|UniProtKB:D3ZVD8, ECO:0000250|UniProtKB:Q9Z2V5, ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18606987, ECO:0000269|PubMed:20308065, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:24882211, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:26246421, ECO:0000269|PubMed:30538141, ECO:0000269|PubMed:30770470, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:38534334, ECO:0000269|PubMed:39567688}.; FUNCTION: (Microbial infection) Deacetylates the SARS-CoV-2 N protein which promotes association of the viral N protein with human G3BP1, leading to disruption of cellular stress granule formation and facilitating viral replication. {ECO:0000269|PubMed:39135075}. |
| Q9UBP0 | SPAST | S207 | ochoa | Spastin (EC 5.6.1.1) (Spastic paraplegia 4 protein) | ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:11809724, PubMed:15716377, PubMed:16219033, PubMed:17389232, PubMed:20530212, PubMed:22637577, PubMed:26875866). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Severing activity is not dependent on tubulin acetylation or detyrosination (PubMed:26875866). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (PubMed:19000169, PubMed:21310966, PubMed:26040712). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (PubMed:21310966). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (PubMed:23897888). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (PubMed:23897888). Probably plays a role in axon growth and the formation of axonal branches (PubMed:15716377). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22637577, ECO:0000269|PubMed:23897888, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:26875866}.; FUNCTION: [Isoform 1]: Involved in lipid metabolism by regulating the size and distribution of lipid droplets. {ECO:0000269|PubMed:25875445}. |
| Q9UBU7 | DBF4 | S629 | ochoa | Protein DBF4 homolog A (Activator of S phase kinase) (Chiffon homolog A) (DBF4-type zinc finger-containing protein 1) | Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle. {ECO:0000269|PubMed:10373557, ECO:0000269|PubMed:10523313, ECO:0000269|PubMed:17062569}. |
| Q9UBW5 | BIN2 | S90 | 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}. |
| Q9UBY0 | SLC9A2 | S687 | ochoa | Sodium/hydrogen exchanger 2 (Na(+)/H(+) exchanger 2) (NHE-2) (Solute carrier family 9 member 2) | Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) (PubMed:10444453). Major apical Na(+)/H(+) exchanger in the base of the colonic crypt. Controls in the colonic crypt intracellular pH (pHi) to direct colonic epithelial cell differentiation into the absorptive enterocyte lineage at the expense of the secretory lineage (By similarity). {ECO:0000250|UniProtKB:Q3ZAS0, ECO:0000269|PubMed:10444453}. |
| Q9UBY5 | LPAR3 | S227 | 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. |
| Q9UEG4 | ZNF629 | S745 | ochoa | Zinc finger protein 629 (Zinc finger protein 65) | May be involved in transcriptional regulation. |
| Q9UEY8 | ADD3 | S360 | ochoa | Gamma-adducin (Adducin-like protein 70) | Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping (PubMed:23836506). Binds to calmodulin (Probable). Involved in myogenic reactivity of the renal afferent arteriole (Af-art), renal interlobular arteries and middle cerebral artery (MCA) to increased perfusion pressure. Involved in regulation of potassium channels in the vascular smooth muscle cells (VSMCs) of the Af-art and MCA ex vivo. Involved in regulation of glomerular capillary pressure, glomerular filtration rate (GFR) and glomerular nephrin expression in response to hypertension. Involved in renal blood flow (RBF) autoregulation. Plays a role in podocyte structure and function. Regulates globular monomer actin (G-actin) and filamentous polymer actin (F-actin) ratios in the primary podocytes affecting actin cytoskeleton organization. Regulates expression of synaptopodin, RhoA, Rac1 and CDC42 in the renal cortex and the primary podocytes. Regulates expression of nephrin in the glomeruli and in the primary podocytes, expression of nephrin and podocinin in the renal cortex, and expression of focal adhesion proteins integrin alpha-3 and integrin beta-1 in the glomeruli. Involved in cell migration and cell adhesion of podocytes, and in podocyte foot process effacement. Regulates expression of profibrotics markers MMP2, MMP9, TGF beta-1, tubular tight junction protein E-cadherin, and mesenchymal markers vimentin and alpha-SMA (By similarity). Promotes the growth of neurites (By similarity). {ECO:0000250|UniProtKB:Q62847, ECO:0000250|UniProtKB:Q9QYB5, ECO:0000269|PubMed:23836506, ECO:0000305}. |
| Q9UFH2 | DNAH17 | S699 | ochoa | Dynein axonemal heavy chain 17 (Axonemal beta dynein heavy chain 17) (Axonemal dynein heavy chain-like protein 1) (Ciliary dynein heavy chain 17) (Ciliary dynein heavy chain-like protein 1) (Dynein axonemal light chain 2) | Force generating protein component of the outer dynein arms (ODAs) in the sperm flagellum. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (Probable). Plays a major role in sperm motility, implicated in sperm flagellar assembly and beating (PubMed:31178125). {ECO:0000269|PubMed:31178125, ECO:0000305|PubMed:31178125}. |
| Q9UGU5 | HMGXB4 | S166 | ochoa | HMG domain-containing protein 4 (HMG box-containing protein 4) (High mobility group protein 2-like 1) (Protein HMGBCG) | Negatively regulates Wnt/beta-catenin signaling during development. {ECO:0000250}. |
| Q9UHF7 | TRPS1 | S368 | ochoa | Zinc finger transcription factor Trps1 (Tricho-rhino-phalangeal syndrome type I protein) (Zinc finger protein GC79) | Transcriptional repressor. Binds specifically to GATA sequences and represses expression of GATA-regulated genes at selected sites and stages in vertebrate development. Regulates chondrocyte proliferation and differentiation. Executes multiple functions in proliferating chondrocytes, expanding the region of distal chondrocytes, activating proliferation in columnar cells and supporting the differentiation of columnar into hypertrophic chondrocytes. {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:17391059}. |
| 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}. |
| Q9UHI5 | SLC7A8 | S24 | ochoa | Large neutral amino acids transporter small subunit 2 (L-type amino acid transporter 2) (hLAT2) (Solute carrier family 7 member 8) | Associates with SLC3A2 to form a functional heterodimeric complex that translocates small and large neutral amino acids with broad specificity and a stoichiometry of 1:1. Functions as amino acid antiporter mediating the influx of extracellular essential amino acids mainly in exchange with the efflux of highly concentrated intracellular amino acids (PubMed:10391915, PubMed:11311135, PubMed:11847106, PubMed:12716892, PubMed:15081149, PubMed:15918515, PubMed:29355479, PubMed:33298890, PubMed:34848541). Has relatively symmetrical selectivities but strongly asymmetrical substrate affinities at both the intracellular and extracellular sides of the transporter (PubMed:11847106). This asymmetry allows SLC7A8 to regulate intracellular amino acid pools (mM concentrations) by exchange with external amino acids (uM concentration range), equilibrating the relative concentrations of different amino acids across the plasma membrane instead of mediating their net uptake (PubMed:10391915, PubMed:11847106). May play an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney (PubMed:12716892). Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity (PubMed:12117417). Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane (PubMed:15769744). Imports the thyroid hormone diiodothyronine (T2) and to a smaller extent triiodothyronine (T3) but not rT 3 or thyroxine (T4) (By similarity). Mediates the uptake of L-DOPA (By similarity). May participate in auditory function (By similarity). {ECO:0000250|UniProtKB:Q9QXW9, ECO:0000250|UniProtKB:Q9WVR6, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11847106, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:15081149, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15918515, ECO:0000269|PubMed:29355479, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:34848541}. |
| Q9UHI6 | DDX20 | S560 | ochoa | Probable ATP-dependent RNA helicase DDX20 (EC 3.6.1.15) (EC 3.6.4.13) (Component of gems 3) (DEAD box protein 20) (DEAD box protein DP 103) (Gemin-3) | 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. 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161}. |
| Q9UHK0 | NUFIP1 | S314 | ochoa | FMR1-interacting protein NUFIP1 (Nuclear FMR1-interacting protein 1) (Nuclear FMRP-interacting protein 1) | Binds RNA. {ECO:0000269|PubMed:10556305}. |
| Q9UIF9 | BAZ2A | S361 | 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}. |
| Q9UK32 | RPS6KA6 | S83 | 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}. |
| Q9UKT8 | FBXW2 | S243 | ochoa | F-box/WD repeat-containing protein 2 (F-box and WD-40 domain-containing protein 2) (Protein MD6) | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. |
| Q9UKV3 | ACIN1 | S863 | 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 | S824 | ochoa|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}. |
| Q9UL18 | AGO1 | S822 | ochoa | Protein argonaute-1 (Argonaute1) (hAgo1) (Argonaute RISC catalytic component 1) (Eukaryotic translation initiation factor 2C 1) (eIF-2C 1) (eIF2C 1) (Putative RNA-binding protein Q99) | Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs). {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:18771919}. |
| Q9ULD2 | MTUS1 | S663 | 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}. |
| Q9ULH0 | KIDINS220 | S1555 | 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}. |
| Q9ULI0 | ATAD2B | S1314 | ochoa | ATPase family AAA domain-containing protein 2B | None |
| Q9ULK2 | ATXN7L1 | S38 | ochoa | Ataxin-7-like protein 1 (Ataxin-7-like protein 4) | None |
| Q9ULT0 | TTC7A | S674 | ochoa | Tetratricopeptide repeat protein 7A (TPR repeat protein 7A) | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane (PubMed:23229899, PubMed:24417819). The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In the complex, plays a central role in bridging PI4KA to EFR3B and HYCC1, via direct interactions (By similarity). {ECO:0000250|UniProtKB:Q86TV6, ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:24417819}. |
| Q9ULT8 | HECTD1 | S710 | 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 | S1945 | 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 | S514 | 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}. |
| Q9UNY4 | TTF2 | S236 | ochoa | Transcription termination factor 2 (EC 3.6.4.-) (Lodestar homolog) (RNA polymerase II termination factor) (Transcription release factor 2) (F2) (HuF2) | DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing. {ECO:0000269|PubMed:10455150, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:15125840, ECO:0000269|PubMed:9748214}. |
| Q9UPN3 | MACF1 | S7345 | 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}. |
| Q9UPN9 | TRIM33 | S789 | 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 | S875 | 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}. |
| Q9UPQ3 | AGAP1 | S101 | ochoa | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 (AGAP-1) (Centaurin-gamma-2) (Cnt-g2) (GTP-binding and GTPase-activating protein 1) (GGAP1) | GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system. {ECO:0000269|PubMed:12640130}. |
| Q9UPQ9 | TNRC6B | S1504 | 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}. |
| Q9UQM7 | CAMK2A | S234 | ochoa | Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17) | Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (PubMed:14722083). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (By similarity). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (PubMed:11972023). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (PubMed:35568036). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (By similarity). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:P11798, ECO:0000269|PubMed:11972023, ECO:0000269|PubMed:23805378, ECO:0000269|PubMed:28130356, ECO:0000269|PubMed:29100089}. |
| Q9Y250 | LZTS1 | S209 | 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}. |
| Q9Y267 | SLC22A14 | S198 | ochoa | Solute carrier family 22 member 14 (Organic cation transporter-like 4) (ORCTL-4) | Riboflavin transporter localized at the inner mitochondrial membrane of the spermatozoa midpiece, which is required for male fertility (By similarity). SLC22A14-mediated riboflavin transport is essential for spermatozoa energy generation and motility: riboflavin is the precursor of FMN and FAD, which are coenzymes of many enzymes in the TCA cycle (the citric acid cycle) in mitochondria (By similarity). Required for sperm motility and normal sperm flagellar structure (By similarity). {ECO:0000250|UniProtKB:Q497L9}. |
| Q9Y294 | ASF1A | S175 | 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}. |
| Q9Y2B0 | CNPY2 | S63 | ochoa | Protein canopy homolog 2 (MIR-interacting saposin-like protein) (Putative secreted protein Zsig9) (Transmembrane protein 4) | Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation. |
| Q9Y2B0 | CNPY2 | S115 | ochoa | Protein canopy homolog 2 (MIR-interacting saposin-like protein) (Putative secreted protein Zsig9) (Transmembrane protein 4) | Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation. |
| Q9Y2J4 | AMOTL2 | S667 | 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}. |
| Q9Y3Q8 | TSC22D4 | S310 | ochoa | TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2) | Binds DNA and acts as a transcriptional repressor (PubMed:10488076). Involved in the regulation of systematic glucose homeostasis and insulin sensitivity, via transcriptional repression of downstream insulin signaling targets such as OBP2A/LCN13 (By similarity). Acts as a negative regulator of lipogenic gene expression in hepatocytes and thereby mediates the control of very low-density lipoprotein release (PubMed:23307490). May play a role in neurite elongation and survival (By similarity). {ECO:0000250|UniProtKB:Q9EQN3, ECO:0000269|PubMed:10488076, ECO:0000269|PubMed:23307490}. |
| Q9Y3R0 | GRIP1 | S773 | ochoa | Glutamate receptor-interacting protein 1 (GRIP-1) | May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons (PubMed:10197531). Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity). {ECO:0000250|UniProtKB:P97879, ECO:0000269|PubMed:10197531}. |
| Q9Y448 | KNSTRN | S171 | ochoa | Small kinetochore-associated protein (SKAP) (Kinetochore-localized astrin-binding protein) (Kinastrin) (Kinetochore-localized astrin/SPAG5-binding protein) (TRAF4-associated factor 1) | Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:19667759, PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments (PubMed:21402792). Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division (PubMed:23035123). May be involved in UV-induced apoptosis via its interaction with PRPF19; however, these results need additional evidences (PubMed:24718257). {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123, ECO:0000305|PubMed:24718257}. |
| Q9Y448 | KNSTRN | S232 | ochoa | Small kinetochore-associated protein (SKAP) (Kinetochore-localized astrin-binding protein) (Kinastrin) (Kinetochore-localized astrin/SPAG5-binding protein) (TRAF4-associated factor 1) | Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:19667759, PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments (PubMed:21402792). Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division (PubMed:23035123). May be involved in UV-induced apoptosis via its interaction with PRPF19; however, these results need additional evidences (PubMed:24718257). {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123, ECO:0000305|PubMed:24718257}. |
| Q9Y490 | TLN1 | S620 | 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}. |
| Q9Y490 | TLN1 | S1589 | 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}. |
| Q9Y490 | TLN1 | S1878 | 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}. |
| Q9Y490 | TLN1 | S2040 | 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}. |
| Q9Y490 | TLN1 | S2096 | 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}. |
| 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}. |
| Q9Y4F9 | RIPOR2 | S593 | ochoa | Rho family-interacting cell polarization regulator 2 | Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization (PubMed:17150207, PubMed:23241886, PubMed:24687993, PubMed:24958875, PubMed:25588844, PubMed:27556504). Inhibits chemokine-induced T lymphocyte responses, such as cell adhesion, polarization and migration (PubMed:23241886). Involved also in the regulation of neutrophil polarization, chemotaxis and adhesion (By similarity). Required for normal development of inner and outer hair cell stereocilia within the cochlea of the inner ear (By similarity). Plays a role for maintaining the structural organization of the basal domain of stereocilia (By similarity). Involved in mechanosensory hair cell function (By similarity). Required for normal hearing (PubMed:24958875). {ECO:0000250|UniProtKB:Q80U16, ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:23241886, ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:24958875, ECO:0000269|PubMed:27556504}.; FUNCTION: [Isoform 2]: Acts as an inhibitor of the small GTPase RHOA (PubMed:25588844). Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation (PubMed:17150207). Maintains naive T lymphocytes in a quiescent state (PubMed:27556504). {ECO:0000269|PubMed:17150207, ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27556504}. |
| 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}. |
| Q9Y572 | RIPK3 | S227 | ochoa|psp | Receptor-interacting serine/threonine-protein kinase 3 (EC 2.7.11.1) (RIP-like protein kinase 3) (Receptor-interacting protein 3) (RIP-3) | Serine/threonine-protein kinase that activates necroptosis and apoptosis, two parallel forms of cell death (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32657447). Necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, is triggered by RIPK3 following activation by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32298652). Activated RIPK3 forms a necrosis-inducing complex and mediates phosphorylation of MLKL, promoting MLKL localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:25316792, PubMed:29883609). In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Also regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is independent of MLKL and RIPK3 kinase activity (By similarity). Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). In some cell types, also able to restrict viral replication by promoting cell death-independent responses (By similarity). In response to Zika virus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with ZBP1, promotes a death-independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate (By similarity). Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL (PubMed:19498109). These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (PubMed:19498109). {ECO:0000250|UniProtKB:Q9QZL0, ECO:0000269|PubMed:19498109, ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513, ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:22421439, ECO:0000269|PubMed:25316792, ECO:0000269|PubMed:29883609, ECO:0000269|PubMed:32298652, ECO:0000269|PubMed:32657447}.; FUNCTION: (Microbial infection) In case of herpes simplex virus 1/HHV-1 infection, forms heteromeric amyloid structures with HHV-1 protein RIR1/ICP6 which may inhibit RIPK3-mediated necroptosis, thereby preventing host cell death pathway and allowing viral evasion. {ECO:0000269|PubMed:33348174}. |
| Q9Y5B0 | CTDP1 | S904 | ochoa | RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (TFIIF-associating CTD phosphatase) | Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. {ECO:0000269|PubMed:22692537}. |
| Q9Y5K6 | CD2AP | S469 | 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 | S174 | 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}. |
| Q9Y5S2 | CDC42BPB | S1530 | 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}. |
| Q9Y6D9 | MAD1L1 | S214 | 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}. |
| Q9Y6I3 | EPN1 | S220 | ochoa | Epsin-1 (EH domain-binding mitotic phosphoprotein) (EPS-15-interacting protein 1) | Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis (PubMed:10393179, PubMed:10557078). {ECO:0000250|UniProtKB:O88339, ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:10557078}. |
| Q9Y6K1 | DNMT3A | S393 | psp | DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase HsaIIIA) (DNA MTase HsaIIIA) (M.HsaIIIA) | Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:12138111, PubMed:16357870, PubMed:30478443). DNA methylation is coordinated with methylation of histones (PubMed:12138111, PubMed:16357870, PubMed:30478443). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:12138111, PubMed:16357870, PubMed:30478443). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (By similarity). Plays a role in paternal and maternal imprinting (By similarity). Required for methylation of most imprinted loci in germ cells (By similarity). Acts as a transcriptional corepressor for ZBTB18 (By similarity). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (By similarity). Can actively repress transcription through the recruitment of HDAC activity (By similarity). Also has weak auto-methylation activity on Cys-710 in absence of DNA (By similarity). {ECO:0000250|UniProtKB:O88508, ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:30478443}. |
| R4GMW8 | BIVM-ERCC5 | S882 | ochoa | DNA excision repair protein ERCC-5 | None |
| P17987 | TCP1 | S374 | Sugiyama | T-complex protein 1 subunit alpha (TCP-1-alpha) (EC 3.6.1.-) (CCT-alpha) (Chaperonin containing T-complex polypeptide 1 subunit 1) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| O00444 | PLK4 | S179 | Sugiyama | Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase 18) (Serine/threonine-protein kinase Sak) | Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (PubMed:22020124). Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-372' which is essential for proper organization and integrity of centriolar satellites (PubMed:30804208). {ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942, ECO:0000269|PubMed:21725316, ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:30804208}. |
| P50897 | PPT1 | S262 | Sugiyama | Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.2) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) | Has thioesterase activity against fatty acid thioesters with 14 -18 carbons, including palmitoyl-CoA, S-palmitoyl-N-acetylcysteamine, and palmitoylated proteins (PubMed:12855696, PubMed:26731412, PubMed:8816748). In contrast to PPT2, PPT1 can hydrolyze palmitoylated proteins and palmitoylcysteine (PubMed:12855696). {ECO:0000269|PubMed:12855696, ECO:0000269|PubMed:26731412, ECO:0000269|PubMed:8816748}. |
| Q96RT7 | TUBGCP6 | S392 | SIGNOR | Gamma-tubulin complex component 6 (GCP-6) | Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation (PubMed:11694571, PubMed:38305685, PubMed:38609661, PubMed:39321809). The gTuRC regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments, a critical step in centrosome duplication and spindle formation (PubMed:38305685, PubMed:38609661, PubMed:39321809). {ECO:0000269|PubMed:11694571, ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661, ECO:0000269|PubMed:39321809}. |
| A0A2R8Y4L2 | HNRNPA1L3 | S22 | Sugiyama | Heterogeneous nuclear ribonucleoprotein A1-like 3 (Heterogeneous nuclear ribonucleoprotein A1 pseudogene 48) | None |
| P40227 | CCT6A | S306 | Sugiyama | T-complex protein 1 subunit zeta (TCP-1-zeta) (EC 3.6.1.-) (Acute morphine dependence-related protein 2) (CCT-zeta-1) (Chaperonin containing T-complex polypeptide 1 subunit 6A) (HTR3) (Tcp20) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). {ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| O14893 | GEMIN2 | S131 | Sugiyama | 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}. |
| P50416 | CPT1A | S612 | Sugiyama | Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A) (Succinyltransferase CPT1A) (EC 2.3.1.-) | Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (PubMed:11350182, PubMed:14517221, PubMed:16651524, PubMed:9691089). Also possesses a lysine succinyltransferase activity that can regulate enzymatic activity of substrate proteins such as ENO1 and metabolism independent of its classical carnitine O-palmitoyltransferase activity (PubMed:29425493). Plays an important role in hepatic triglyceride metabolism (By similarity). Also plays a role in inducible regulatory T-cell (iTreg) differentiation once activated by butyryl-CoA that antagonizes malonyl-CoA-mediated CPT1A repression (By similarity). Sustains the IFN-I response by recruiting ZDHCC4 to palmitoylate MAVS at the mitochondria leading to MAVS stabilization and activation (PubMed:38016475). Promotes ROS-induced oxidative stress in liver injury via modulation of NFE2L2 and NLRP3-mediated signaling pathways (By similarity). {ECO:0000250|UniProtKB:P32198, ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221, ECO:0000269|PubMed:16651524, ECO:0000269|PubMed:29425493, ECO:0000269|PubMed:38016475, ECO:0000269|PubMed:9691089}. |
| Q12792 | TWF1 | S55 | Sugiyama | Twinfilin-1 (Protein A6) (Protein tyrosine kinase 9) | Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). {ECO:0000250}. |
| Q13409 | DYNC1I2 | S219 | Sugiyama | Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2) | 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 (PubMed:31079899). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:31079899). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity). {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:31079899}. |
| Q14192 | FHL2 | S238 | Sugiyama | Four and a half LIM domains protein 2 (FHL-2) (LIM domain protein DRAL) (Skeletal muscle LIM-protein 3) (SLIM-3) | May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation. Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes (PubMed:28717008). {ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16652157, ECO:0000269|PubMed:18853468, ECO:0000269|PubMed:28717008}. |
| 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}. |
| Q92796 | DLG3 | S615 | Sugiyama | Disks large homolog 3 (Neuroendocrine-DLG) (Synapse-associated protein 102) (SAP-102) (SAP102) (XLMR) | Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling. |
| O14965 | AURKA | S226 | GPS6|ELM|EPSD|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}. |
| P33993 | MCM7 | S409 | Sugiyama | DNA replication licensing factor MCM7 (EC 3.6.4.12) (CDC47 homolog) (P1.1-MCM3) | 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: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:32453425). Required for S-phase checkpoint activation upon UV-induced damage. {ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:25661590, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000269|PubMed:9305914}. |
| P40925 | MDH1 | S153 | Sugiyama | Malate dehydrogenase, cytoplasmic (EC 1.1.1.37) (Aromatic alpha-keto acid reductase) (KAR) (EC 1.1.1.96) (Cytosolic malate dehydrogenase) | Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH (PubMed:2449162, PubMed:3052244). Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation (PubMed:31538237). Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen species (ROS) (PubMed:34012073). {ECO:0000269|PubMed:2449162, ECO:0000269|PubMed:3052244, ECO:0000269|PubMed:31538237}. |
| P49327 | FASN | S519 | Sugiyama | Fatty acid synthase (EC 2.3.1.85) (Type I fatty acid synthase) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Acyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)] | Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448}.; FUNCTION: (Microbial infection) Fatty acid synthetase activity is required for SARS coronavirus-2/SARS-CoV-2 replication. {ECO:0000269|PubMed:34320401}. |
| Q16600 | ZNF239 | S46 | GPS6 | Zinc finger protein 239 (Zinc finger protein HOK-2) (Zinc finger protein MOK-2) | May be involved in transcriptional regulation. |
| O15111 | CHUK | S249 | Sugiyama | Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK-1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16) | 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:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, 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:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, 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 (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Also participates in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973). {ECO:0000250|UniProtKB:Q60680, ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937, ECO:0000269|PubMed:21765415, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35952808, ECO:0000269|PubMed:9244310, ECO:0000269|PubMed:9252186, ECO:0000269|PubMed:9346484, ECO:0000303|PubMed:18626576}. |
| O15111 | CHUK | S400 | Sugiyama | Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK-1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16) | 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:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, 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:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, 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 (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Also participates in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973). {ECO:0000250|UniProtKB:Q60680, ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937, ECO:0000269|PubMed:21765415, ECO:0000269|PubMed:30217973, ECO:0000269|PubMed:35952808, ECO:0000269|PubMed:9244310, ECO:0000269|PubMed:9252186, ECO:0000269|PubMed:9346484, ECO:0000303|PubMed:18626576}. |
| P52564 | MAP2K6 | S35 | Sugiyama | Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3) | Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13 and MAPK14 and plays an important role in the regulation of cellular responses to cytokines and all kinds of stresses. Especially, MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also phosphorylates and activates PAK6. The p38 MAP kinase signal transduction pathway leads to direct activation of transcription factors. Nuclear targets of p38 MAP kinase include the transcription factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway, MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14 activation, and is therefore required for STAT4 activation and STAT4-regulated gene expression in response to IL-12 stimulation. The pathway is also crucial for IL-6-induced SOCS3 expression and down-regulation of IL-6-mediated gene induction; and for IFNG-dependent gene transcription. Has a role in osteoclast differentiation through NF-kappa-B transactivation by TNFSF11, and in endochondral ossification and since SOX9 is another likely downstream target of the p38 MAPK pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts also as a regulator for melanocytes dendricity, through the modulation of Rho family GTPases. {ECO:0000269|PubMed:10961885, ECO:0000269|PubMed:11727828, ECO:0000269|PubMed:15550393, ECO:0000269|PubMed:20869211, ECO:0000269|PubMed:8622669, ECO:0000269|PubMed:8626699, ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9218798}. |
| O43283 | MAP3K13 | S772 | Sugiyama | Mitogen-activated protein kinase kinase kinase 13 (EC 2.7.11.25) (Leucine zipper-bearing kinase) (Mixed lineage kinase) (MLK) | Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B. {ECO:0000269|PubMed:11726277, ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:9353328}. |
| Q9BXP5 | SRRT | S422 | Sugiyama | Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) | Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity). {ECO:0000250, ECO:0000269|PubMed:19632182}. |
| 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}. |
| P63010 | AP2B1 | Y524 | Sugiyama | AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit) | Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. 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. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. 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. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. 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. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}. |
| Q10567 | AP1B1 | Y524 | Sugiyama | AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit) | Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes (PubMed:31630791). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. {ECO:0000269|PubMed:31630791}. |
| Q13547 | HDAC1 | S88 | Sugiyama | Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein deacylase HDAC1) (EC 3.5.1.-) | Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:16762839, PubMed:17704056, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:16762839, PubMed:17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:16762839, PubMed:17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 (PubMed:12837748, PubMed:16285960, PubMed:16478997, PubMed:17996965, PubMed:19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed:12837748, PubMed:16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed:19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed:19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed:19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed:17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed:17996965). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed:28497810, PubMed:35044827). {ECO:0000250|UniProtKB:O09106, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:28497810, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:35044827}. |
| Q92769 | HDAC2 | S89 | Sugiyama | Histone deacetylase 2 (HD2) (EC 3.5.1.98) (Protein deacylase HDAC2) (EC 3.5.1.-) | Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:28497810). 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). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Component of the SIN3B complex that represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (PubMed:19343227). May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity). Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:35044827). {ECO:0000250|UniProtKB:P70288, ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:28497810, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:29192674, ECO:0000269|PubMed:35044827, ECO:0000269|PubMed:37137925}. |
| P04629 | NTRK1 | S498 | Sugiyama | High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (TRK1-transforming tyrosine kinase protein) (Tropomyosin-related kinase A) (Tyrosine kinase receptor) (Tyrosine kinase receptor A) (Trk-A) (gp140trk) (p140-TrkA) | Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand (PubMed:1281417, PubMed:15488758, PubMed:17196528, PubMed:1849459, PubMed:1850821, PubMed:22649032, PubMed:27445338, PubMed:8325889). Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival (By similarity). Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation (PubMed:1281417). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors. {ECO:0000250|UniProtKB:P35739, ECO:0000250|UniProtKB:Q3UFB7, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:1281417, ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:17196528, ECO:0000269|PubMed:1849459, ECO:0000269|PubMed:1850821, ECO:0000269|PubMed:22649032, ECO:0000269|PubMed:27445338, ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8155326, ECO:0000269|PubMed:8325889}.; FUNCTION: [Isoform TrkA-III]: Resistant to NGF, it constitutively activates AKT1 and NF-kappa-B and is unable to activate the Ras-MAPK signaling cascade. Antagonizes the anti-proliferative NGF-NTRK1 signaling that promotes neuronal precursors differentiation. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. {ECO:0000269|PubMed:15488758}. |
| P28329 | CHAT | S465 | SIGNOR|EPSD | Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6) | Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. {ECO:0000269|PubMed:17144655}. |
| O15357 | INPPL1 | S189 | Sugiyama | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2) | Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:16824732). Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (PubMed:9660833). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (By similarity). Part of a signaling pathway that regulates actin cytoskeleton remodeling (PubMed:11739414, PubMed:12676785). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (PubMed:15668240). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading (PubMed:12235291). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (PubMed:15735664). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (PubMed:17135240). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (PubMed:12690104). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (PubMed:11016922). Involved in EGF signaling pathway (PubMed:11349134). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (PubMed:11349134). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (PubMed:11349134). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (PubMed:23273569). {ECO:0000250|UniProtKB:F1PNY0, ECO:0000250|UniProtKB:Q6P549, ECO:0000250|UniProtKB:Q9WVR3, ECO:0000269|PubMed:11016922, ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12235291, ECO:0000269|PubMed:12676785, ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:15668240, ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:16824732, ECO:0000269|PubMed:17135240, ECO:0000269|PubMed:21624956, ECO:0000269|PubMed:23273569, ECO:0000269|PubMed:9660833}. |
| P31327 | CPS1 | S819 | Sugiyama | Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) | Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. |
| Q96I99 | SUCLG2 | S98 | Sugiyama | Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) | GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-Rule:MF_03221}. |
| Q92626 | PXDN | S918 | Sugiyama | Peroxidasin homolog (EC 1.11.2.-) (Melanoma-associated antigen MG50) (Peroxidasin 1) (hsPxd01) (Vascular peroxidase 1) (p53-responsive gene 2 protein) [Cleaved into: PXDN active fragment] | Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (PubMed:18929642, PubMed:19590037, PubMed:22842973, PubMed:25708780, PubMed:25713063, PubMed:27697841, PubMed:28154175, PubMed:34679700). In turns, directly contributes to the collagen IV network-dependent fibronectin/FN and laminin assembly, which is required for full extracellular matrix (ECM)-mediated signaling (PubMed:19590037, PubMed:32543734, PubMed:34679700). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (PubMed:32543734). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (PubMed:25713063). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1485' and leads to bromine enrichment of the basement membranes (PubMed:32571911). In vitro, can also catalyze the two-electron oxidation of thiocyanate and iodide and these two substrates could effectively compete with bromide and thus inhibit the formation of sulfilimine bonds (PubMed:28154175). Binds laminins (PubMed:32485152). May play a role in the organization of eyeball structure and lens development during eye development (By similarity). {ECO:0000250|UniProtKB:Q3UQ28, ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037, ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:25708780, ECO:0000269|PubMed:25713063, ECO:0000269|PubMed:27697841, ECO:0000269|PubMed:28154175, ECO:0000269|PubMed:32485152, ECO:0000269|PubMed:32543734, ECO:0000269|PubMed:32571911, ECO:0000269|PubMed:34679700}. |
| Q6ZN44 | UNC5A | S532 | SIGNOR | Netrin receptor UNC5A (Protein unc-5 homolog 1) (Protein unc-5 homolog A) | Receptor for netrin required for axon guidance. Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1. Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin. Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. {ECO:0000250|UniProtKB:O08721}. |
| Q9NPI1 | BRD7 | S336 | Sugiyama | 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}. |
| P35916 | FLT4 | S863 | Sugiyama | Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4) | Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'. {ECO:0000269|PubMed:11532940, ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:16452200, ECO:0000269|PubMed:17210781, ECO:0000269|PubMed:19610651, ECO:0000269|PubMed:19779139, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:20445537, ECO:0000269|PubMed:21273538, ECO:0000269|PubMed:7675451, ECO:0000269|PubMed:8700872, ECO:0000269|PubMed:9435229}. |
| P52907 | CAPZA1 | S244 | Sugiyama | F-actin-capping protein subunit alpha-1 (CapZ alpha-1) | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (PubMed:22891260). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250|UniProtKB:A0PFK5, ECO:0000269|PubMed:22891260}. |
| Q6EMK4 | VASN | S322 | Sugiyama | Vasorin (Protein slit-like 2) | May act as an inhibitor of TGF-beta signaling. {ECO:0000269|PubMed:15247411}. |
| P09417 | QDPR | S163 | Sugiyama | Dihydropteridine reductase (EC 1.5.1.34) (HDHPR) (Quinoid dihydropteridine reductase) (Short chain dehydrogenase/reductase family 33C member 1) | Catalyzes the conversion of quinonoid dihydrobiopterin into tetrahydrobiopterin. {ECO:0000269|PubMed:3033643, ECO:0000269|PubMed:8262916}. |
| Q8TEQ6 | GEMIN5 | S1396 | Sugiyama | 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}. |
| P51957 | NEK4 | S379 | 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}. |
| P51957 | NEK4 | S720 | 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}. |
| O60749 | SNX2 | S302 | Sugiyama | Sorting nexin-2 (Transformation-related gene 9 protein) (TRG-9) | Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:16179610). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:17101778). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:20138391, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:23085988, ECO:0000303|PubMed:16179610}. |
| Q9BT78 | COPS4 | S297 | Sugiyama | COP9 signalosome complex subunit 4 (SGN4) (Signalosome subunit 4) (JAB1-containing signalosome subunit 4) | Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:9535219}. |
| Q9Y478 | PRKAB1 | S49 | Sugiyama | 5'-AMP-activated protein kinase subunit beta-1 (AMPK subunit beta-1) (AMPKb) | Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. 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. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). |
| Q13200 | PSMD2 | S467 | Sugiyama | 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000269|PubMed:1317798}.; FUNCTION: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. |
| P10768 | ESD | S189 | Sugiyama | S-formylglutathione hydrolase (FGH) (EC 3.1.2.12) (Esterase D) (Methylumbelliferyl-acetate deacetylase) (EC 3.1.1.56) | Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}. |
| Q9H8Y5 | ANKZF1 | S126 | Sugiyama | tRNA endonuclease ANKZF1 (EC 3.1.-.-) (Ankyrin repeat and zinc finger domain-containing protein 1) (Zinc finger protein 744) | Endonuclease that cleaves polypeptidyl-tRNAs downstream of the ribosome-associated quality control (RQC) pathway to release incompletely synthesized polypeptides for degradation (PubMed:29632312, PubMed:30244831, PubMed:31011209). The RQC pathway disassembles aberrantly stalled translation complexes to recycle or degrade the constituent parts (PubMed:29632312, PubMed:30244831, PubMed:31011209). ANKZF1 acts downstream disassembly of stalled ribosomes and specifically cleaves off the terminal 3'-CCA nucleotides universal to all tRNAs from polypeptidyl-tRNAs, releasing (1) ubiquitinated polypeptides from 60S ribosomal subunit for degradation and (2) cleaved tRNAs (PubMed:31011209). ANKZF1-cleaved tRNAs are then repaired and recycled by ELAC1 and TRNT1 (PubMed:31011209, PubMed:32075755). Also plays a role in the cellular response to hydrogen peroxide and in the maintenance of mitochondrial integrity under conditions of cellular stress (PubMed:28302725). {ECO:0000269|PubMed:28302725, ECO:0000269|PubMed:29632312, ECO:0000269|PubMed:30244831, ECO:0000269|PubMed:31011209, ECO:0000269|PubMed:32075755}. |
| P30101 | PDIA3 | S343 | 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}. |
| P46459 | NSF | S31 | Sugiyama | Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein) (NEM-sensitive fusion protein) (Vesicular-fusion protein NSF) | Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling (By similarity). {ECO:0000250}. |
| Q14697 | GANAB | S45 | Sugiyama | Neutral alpha-glucosidase AB (EC 3.2.1.207) (Alpha-glucosidase 2) (Glucosidase II subunit alpha) | Catalytic 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 PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia (PubMed:27259053). {ECO:0000269|PubMed:10929008, ECO:0000269|PubMed:27259053}. |
| P20073 | ANXA7 | S393 | Sugiyama | Annexin A7 (Annexin VII) (Annexin-7) (Synexin) | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. |
| O60885 | BRD4 | S1223 | Sugiyama | 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}. |
| P31150 | GDI1 | S213 | Sugiyama | Rab GDP dissociation inhibitor alpha (Rab GDI alpha) (Guanosine diphosphate dissociation inhibitor 1) (GDI-1) (Oligophrenin-2) (Protein XAP-4) | Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. {ECO:0000269|PubMed:23815289}. |
| P50395 | GDI2 | S213 | Sugiyama | Rab GDP dissociation inhibitor beta (Rab GDI beta) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) | GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking (PubMed:25860027). Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A (PubMed:25860027). {ECO:0000269|PubMed:25860027}. |
| P00568 | AK1 | S58 | Sugiyama | Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.4) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity) (PubMed:21080915, PubMed:23416111, PubMed:2542324). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity). {ECO:0000250|UniProtKB:P05081, ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111, ECO:0000269|PubMed:2542324}. |
| 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}. |
| Q13873 | BMPR2 | S233 | Sugiyama | Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II) | On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Can also mediate signaling through the activation of the p38MAPK cascade (PubMed:12045205). Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6. Promotes signaling also by binding to activin A/INHBA (PubMed:24018044). {ECO:0000250|UniProtKB:O35607, ECO:0000269|PubMed:12045205, ECO:0000269|PubMed:24018044}. |
| P30305 | CDC25B | S219 | SIGNOR | M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) | Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner (PubMed:17332740). The three isoforms seem to have a different level of activity (PubMed:1836978). {ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. |
| Q15349 | RPS6KA2 | S684 | 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}. |
| Q6L8Q7 | PDE12 | S266 | Sugiyama | 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}. |
| P47755 | CAPZA2 | S244 | Sugiyama | F-actin-capping protein subunit alpha-2 (CapZ alpha-2) | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. |
| P0C0L4 | C4A | S1294 | Sugiyama | Complement C4-A (Acidic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; Complement C4b-A (Complement C4b-alpha' chain); Complement C4d-A; Complement C4 gamma chain] | Precursor of non-enzymatic components of the classical, lectin and GZMK complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. {ECO:0000269|PubMed:12878586, ECO:0000269|PubMed:18204047, ECO:0000269|PubMed:22949645, ECO:0000269|PubMed:2395880, ECO:0000269|PubMed:32769120, ECO:0000269|PubMed:35428691, ECO:0000269|PubMed:39914456, ECO:0000269|PubMed:8538770}.; FUNCTION: [Complement C4b-A]: Non-enzymatic component of C3 and C5 convertases (PubMed:8538770). Generated following cleavage by complement proteases (C1S, MASP2 or GZMK, depending on the complement pathway), it covalently attaches to the surface of pathogens, where it acts as an opsonin that marks the surface of antigens for removal (PubMed:27738201, PubMed:8538770). It then recruits the serine protease complement C2b to form the C3 and C5 convertases, which cleave and activate C3 and C5, respectively, the next components of the complement pathways (PubMed:12878586, PubMed:18204047, PubMed:2387864, PubMed:6906228). Complement C4b-A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while complement C4b-B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens (PubMed:8538770). {ECO:0000269|PubMed:12878586, ECO:0000269|PubMed:18204047, ECO:0000269|PubMed:2387864, ECO:0000269|PubMed:27738201, ECO:0000269|PubMed:6906228, ECO:0000269|PubMed:8538770}.; FUNCTION: [C4a anaphylatoxin]: Putative humoral mediator released following cleavage by complement proteases (C1S, MASP2 or GZMK, depending on the complement pathway) (PubMed:6167582). While it is strongly similar to anaphylatoxins, its role is unclear (PubMed:25659340). Was reported to act as a mediator of local inflammatory process; however these effects were probably due to contamination with C3a and/C5a anaphylatoxins in biological assays (PubMed:25659340). {ECO:0000269|PubMed:6167582, ECO:0000303|PubMed:25659340}. |
| P0C0L5 | C4B | S1294 | Sugiyama | Complement C4-B (Basic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3) [Cleaved into: Complement C4 beta chain; Complement C4-B alpha chain; C4a anaphylatoxin; Complement C4b-B; C4d-B; Complement C4 gamma chain] | Precursor of non-enzymatic components of the classical, lectin and GZMK complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. {ECO:0000269|PubMed:2395880, ECO:0000269|PubMed:8538770}.; FUNCTION: [Complement C4b-B]: Non-enzymatic component of C3 and C5 convertases (By similarity). Generated following cleavage by complement proteases (C1S, MASP2 or GZMK, depending on the complement pathway), it covalently attaches to the surface of pathogens, where it acts as an opsonin that marks the surface of antigens for removal (By similarity). It then recruits the serine protease complement C2b to form the C3 and C5 convertases, which cleave and activate C3 and C5, respectively, the next components of the complement pathways (PubMed:8538770). Complement C4b-B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens, while C4b-A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens (PubMed:8538770). {ECO:0000250|UniProtKB:P0C0L4, ECO:0000269|PubMed:8538770}.; FUNCTION: [C4a anaphylatoxin]: Putative humoral mediator released following cleavage by complement proteases (C1S, MASP2 or GZMK, depending on the complement pathway). While it is strongly similar to anaphylatoxins, its role is unclear. Was reported to act as a mediator of local inflammatory process; however these effects were probably due to contamination with C3a and/C5a anaphylatoxins in biological assays. {ECO:0000250|UniProtKB:P0C0L4}. |
| Q9UHX1 | PUF60 | S461 | 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}. |
| P50990 | CCT8 | S161 | Sugiyama | T-complex protein 1 subunit theta (TCP-1-theta) (EC 3.6.1.-) (CCT-theta) (Chaperonin containing T-complex polypeptide 1 subunit 8) (Renal carcinoma antigen NY-REN-15) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
| P80303 | NUCB2 | S96 | Sugiyama | Nucleobindin-2 (DNA-binding protein NEFA) (Epididymis secretory protein Li 109) (Gastric cancer antigen Zg4) (Prepronesfatin) [Cleaved into: Nesfatin-1] | Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity). {ECO:0000250|UniProtKB:P81117, ECO:0000250|UniProtKB:Q9JI85}.; FUNCTION: [Nesfatin-1]: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance. In intestinal epithelial cells, plays a role in the inhibition of hepatic glucose production via MC4R receptor leading to increased cyclic adenosine monophosphate (cAMP) levels and glucagon-like peptide 1 (GLP-1) secretion (PubMed:39562740). {ECO:0000250|UniProtKB:Q9JI85, ECO:0000269|PubMed:39562740}. |
| Q02818 | NUCB1 | S93 | Sugiyama | Nucleobindin-1 (CALNUC) | Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins) (By similarity). {ECO:0000250|UniProtKB:Q0P569, ECO:0000250|UniProtKB:Q63083}. |
| Q14152 | EIF3A | S227 | 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}. |
| Q9BV86 | NTMT1 | S181 | Sugiyama | N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (N-terminal RCC1 methyltransferase) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed] | Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation (PubMed:24090352). Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1. {ECO:0000269|PubMed:20481588, ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:24090352, ECO:0000269|PubMed:26543159}. |
| Q16832 | DDR2 | S65 | Sugiyama | 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}. |
| O60749 | SNX2 | S264 | Sugiyama | Sorting nexin-2 (Transformation-related gene 9 protein) (TRG-9) | Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:16179610). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:17101778). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:20138391, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:23085988, ECO:0000303|PubMed:16179610}. |
| Q07065 | CKAP4 | S433 | Sugiyama | Cytoskeleton-associated protein 4 (63-kDa cytoskeleton-linking membrane protein) (Climp-63) (p63) | Mediates the anchoring of the endoplasmic reticulum to microtubules. {ECO:0000269|PubMed:15703217}.; FUNCTION: High-affinity epithelial cell surface receptor for the FZD8-related low molecular weight sialoglycopeptide APF/antiproliferative factor. Mediates the APF antiproliferative signaling within cells. {ECO:0000269|PubMed:17030514, ECO:0000269|PubMed:19144824}. |
| Q86TU7 | SETD3 | S505 | Sugiyama | Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3) (hSETD3) | Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73' (PubMed:30526847, PubMed:30626964, PubMed:30785395, PubMed:31388018, PubMed:31993215). Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery (PubMed:30626964). Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin (PubMed:30626964, PubMed:30785395, PubMed:31388018). {ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31993215}. |
| Q8NBP7 | PCSK9 | S666 | GPS6 | Proprotein convertase subtilisin/kexin type 9 (EC 3.4.21.-) (Neural apoptosis-regulated convertase 1) (NARC-1) (Proprotein convertase 9) (PC9) (Subtilisin/kexin-like protease PC9) | Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation (PubMed:17461796, PubMed:18197702, PubMed:18799458, PubMed:22074827). Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway (PubMed:18660751). Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. {ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:18039658, ECO:0000269|PubMed:18197702, ECO:0000269|PubMed:18660751, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22074827, ECO:0000269|PubMed:22493497, ECO:0000269|PubMed:22580899}. |
| Q14204 | DYNC1H1 | S3920 | Sugiyama | Cytoplasmic dynein 1 heavy chain 1 (Cytoplasmic dynein heavy chain 1) (Dynein heavy chain, cytosolic) | Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074). {ECO:0000269|PubMed:27462074}. |
| Q8WUM4 | PDCD6IP | S381 | Sugiyama | Programmed cell death 6-interacting protein (PDCD6-interacting protein) (ALG-2-interacting protein 1) (ALG-2-interacting protein X) (Hp95) | Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes (PubMed:14739459). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:17556548, PubMed:17853893). Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis (PubMed:17556548, PubMed:17853893, PubMed:18641129). May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP (PubMed:22660413). By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier (By similarity). {ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:22660413}.; FUNCTION: (Microbial infection) Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function requires the interaction with CHMP4B. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as enveloped virus budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:18641129}. |
| Q9NYU2 | UGGT1 | S366 | Sugiyama | UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1) (hUGT1) (EC 2.4.1.-) (UDP--Glc:glycoprotein glucosyltransferase) (UDP-glucose ceramide glucosyltransferase-like 1) | Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. {ECO:0000269|PubMed:10694380}. |
| Q9UHV9 | PFDN2 | S22 | Sugiyama | Prefoldin subunit 2 | Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}. |
| Q92630 | DYRK2 | S482 | Sugiyama | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) | Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro). {ECO:0000269|PubMed:11311121, ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:14593110, ECO:0000269|PubMed:15910284, ECO:0000269|PubMed:16511445, ECO:0000269|PubMed:16611631, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:9748265}. |
| Q6UB35 | MTHFD1L | S366 | Sugiyama | Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC 6.3.4.3) (Formyltetrahydrofolate synthetase) | May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism complementing thus the enzymatic activities of MTHFD2. {ECO:0000250, ECO:0000269|PubMed:16171773}. |
| Q7Z3T8 | ZFYVE16 | S360 | Sugiyama | 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}. |
| O60763 | USO1 | S776 | Sugiyama | General vesicular transport factor p115 (Protein USO1 homolog) (Transcytosis-associated protein) (TAP) (Vesicle-docking protein) | General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity. {ECO:0000250|UniProtKB:P41542}. |
| P17980 | PSMC3 | S186 | Sugiyama | 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000269|PubMed:1317798}. |
| Q8N584 | TTC39C | S472 | Sugiyama | Tetratricopeptide repeat protein 39C (TPR repeat protein 39C) | None |
| Q9NWZ3 | IRAK4 | S314 | Sugiyama | 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}. |
| Q9NYY3 | PLK2 | S248 | Sugiyama | Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (hPlk2) (Serine/threonine-protein kinase SNK) (hSNK) (Serum-inducible kinase) | Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. {ECO:0000269|PubMed:15242618, ECO:0000269|PubMed:19001868, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:20531387}. |
| P56192 | MARS1 | S472 | EPSD|PSP | Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) | Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:11714285). Plays a role in the synthesis of ribosomal RNA in the nucleolus (PubMed:10791971). {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:11714285, ECO:0000269|PubMed:33909043}. |
| Q9P2K8 | EIF2AK4 | S1504 | Sugiyama | eIF-2-alpha kinase GCN2 (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 4) (GCN2-like protein) | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (PubMed:25329545, PubMed:32610081). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:32610081). Binds uncharged tRNAs (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442, ECO:0000250|UniProtKB:Q9QZ05, ECO:0000269|PubMed:25329545, ECO:0000269|PubMed:26102367, ECO:0000269|PubMed:32610081}.; FUNCTION: (Microbial infection) Plays a role in modulating the adaptive immune response to yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation (PubMed:24310610). {ECO:0000269|PubMed:24310610}. |
| Q9UBE8 | NLK | S237 | Sugiyama | Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase) (Protein LAK1) | Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination (PubMed:12482967, PubMed:14960582, PubMed:15004007, PubMed:15764709, PubMed:20061393, PubMed:20874444, PubMed:21454679). Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2 (PubMed:15004007, PubMed:15764709). Negative regulator of the canonical Wnt/beta-catenin signaling pathway (PubMed:12482967). Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1 (PubMed:21454679). Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes (PubMed:12482967, PubMed:21454679). Negative regulator of the Notch signaling pathway (PubMed:20118921). Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1 (PubMed:20118921). Negative regulator of the MYB family of transcription factors (PubMed:15082531). Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP (PubMed:15082531). Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself (PubMed:15082531). Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1 (PubMed:15004007, PubMed:15764709). Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members (PubMed:25512613). Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner (PubMed:25512613). Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes (PubMed:26588989). {ECO:0000269|PubMed:12482967, ECO:0000269|PubMed:14960582, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15764709, ECO:0000269|PubMed:20061393, ECO:0000269|PubMed:20118921, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:25512613, ECO:0000269|PubMed:26588989}. |
| Q9UM73 | ALK | S1538 | Sugiyama | ALK tyrosine kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase) (CD antigen CD246) | Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system (PubMed:11121404, PubMed:11387242, PubMed:16317043, PubMed:17274988, PubMed:30061385, PubMed:34646012, PubMed:34819673). Also acts as a key thinness protein involved in the resistance to weight gain: in hypothalamic neurons, controls energy expenditure acting as a negative regulator of white adipose tissue lipolysis and sympathetic tone to fine-tune energy homeostasis (By similarity). Following activation by ALKAL2 ligand at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:30061385, PubMed:33411331, PubMed:34646012, PubMed:34819673). In contrast, ALKAL1 is not a potent physiological ligand for ALK (PubMed:34646012). Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:34819673). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (PubMed:15226403, PubMed:16878150). Induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1 (PubMed:15226403, PubMed:16878150). ALK activation may also be regulated by pleiotrophin (PTN) and midkine (MDK) (PubMed:11278720, PubMed:11809760, PubMed:12107166, PubMed:12122009). PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation (PubMed:11278720, PubMed:11809760, PubMed:12107166). MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction (PubMed:12122009). Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase (PubMed:15226403, PubMed:16878150). Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK (PubMed:15226403, PubMed:16878150). {ECO:0000250|UniProtKB:P97793, ECO:0000269|PubMed:11121404, ECO:0000269|PubMed:11278720, ECO:0000269|PubMed:11387242, ECO:0000269|PubMed:11809760, ECO:0000269|PubMed:12107166, ECO:0000269|PubMed:12122009, ECO:0000269|PubMed:15226403, ECO:0000269|PubMed:16317043, ECO:0000269|PubMed:16878150, ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:30061385, ECO:0000269|PubMed:33411331, ECO:0000269|PubMed:34646012, ECO:0000269|PubMed:34819673}. |
| P12277 | CKB | S147 | Sugiyama | Creatine kinase B-type (EC 2.7.3.2) (Brain creatine kinase) (B-CK) (Creatine kinase B chain) (Creatine phosphokinase B-type) (CPK-B) | Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity). {ECO:0000250|UniProtKB:Q04447, ECO:0000269|PubMed:8186255, ECO:0000305}. |
| P27708 | CAD | S133 | Sugiyama | Multifunctional protein CAD (Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase) [Includes: Glutamine-dependent carbamoyl phosphate synthase (EC 6.3.5.5); Glutamine amidotransferase (GATase) (GLNase) (EC 3.5.1.2); Ammonium-dependent carbamoyl phosphate synthase (CPS) (CPSase) (EC 6.3.4.16); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)] | Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000269|PubMed:24332717}. |
| Q96NW7 | LRRC7 | S1439 | SIGNOR|iPTMNet | Leucine-rich repeat-containing protein 7 (Densin-180) (Densin) (Protein LAP1) | Required for normal synaptic spine architecture and function. Necessary for DISC1 and GRM5 localization to postsynaptic density complexes and for both N-methyl D-aspartate receptor-dependent and metabotropic glutamate receptor-dependent long term depression. {ECO:0000269|PubMed:11729199}. |
| Q9GZT8 | NIF3L1 | S193 | Sugiyama | NIF3-like protein 1 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 1 protein) | May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9EQ80}. |
| A6NES4 | MROH2A | Y1623 | ochoa | Maestro heat-like repeat-containing protein family member 2A (HEAT repeat-containing protein 7B1) | None |
| B4DLN1 | None | S248 | ochoa | Mitochondrial dicarboxylate carrier (Solute carrier family 25 member 10) | Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane. Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity. {ECO:0000256|ARBA:ARBA00057945}. |
| K7EQG2 | None | S90 | ochoa | Uncharacterized protein | None |
| O00244 | ATOX1 | S47 | ochoa | Copper transport protein ATOX1 (Metal transport protein ATX1) | Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense. |
| O15400 | STX7 | S174 | 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. |
| O43432 | EIF4G3 | S1156 | ochoa|psp | Eukaryotic translation initiation factor 4 gamma 3 (eIF-4-gamma 3) (eIF-4G 3) (eIF4G 3) (eIF-4-gamma II) (eIF4GII) | 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:9418880). Functional homolog of EIF4G1 (PubMed:9418880). {ECO:0000269|PubMed:9418880}. |
| O43683 | BUB1 | S618 | ochoa|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}. |
| O60437 | PPL | S949 | ochoa | Periplakin (190 kDa paraneoplastic pemphigus antigen) (195 kDa cornified envelope precursor protein) | Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling. {ECO:0000269|PubMed:9412476}. |
| O60664 | PLIN3 | S383 | 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}. |
| O75396 | SEC22B | S26 | ochoa | Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) | SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}. |
| O95235 | KIF20A | S685 | 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}. |
| P01009 | SERPINA1 | S260 | ochoa | Alpha-1-antitrypsin (Alpha-1 protease inhibitor) (Alpha-1-antiproteinase) (Serpin A1) [Cleaved into: Short peptide from AAT (SPAAT)] | Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.; FUNCTION: [Short peptide from AAT]: Reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). |
| P06733 | ENO1 | S336 | ochoa | Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein) | Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209). {ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133, ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901, ECO:0000269|PubMed:29775581}.; FUNCTION: [Isoform MBP-1]: Binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}. |
| P09543 | CNP | S170 | ochoa | 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) | Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P06623, ECO:0000250|UniProtKB:P16330}. |
| P09874 | PARP1 | S177 | ochoa|psp | Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (DNA ADP-ribosyltransferase PARP1) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1) (Protein poly-ADP-ribosyltransferase PARP1) (EC 2.4.2.-) [Cleaved into: Poly [ADP-ribose] polymerase 1, processed C-terminus (Poly [ADP-ribose] polymerase 1, 89-kDa form); Poly [ADP-ribose] polymerase 1, processed N-terminus (NT-PARP-1) (Poly [ADP-ribose] polymerase 1, 24-kDa form) (Poly [ADP-ribose] polymerase 1, 28-kDa form)] | Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:26626479, PubMed:26626480, PubMed:30104678, PubMed:31796734, PubMed:32028527, PubMed:32241924, PubMed:32358582, PubMed:33186521, PubMed:34465625, PubMed:34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:19764761, PubMed:25043379, PubMed:28190768, PubMed:29954836, PubMed:35393539, PubMed:7852410, PubMed:9315851). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521, PubMed:34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:29954836, PubMed:30257210). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600, PubMed:34465625, PubMed:34874266). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed:33683197, PubMed:34732825, PubMed:34795260). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed:26344098, PubMed:30356214). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed:17396150, PubMed:19764761, PubMed:24906880, PubMed:34049076). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed:27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). 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). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed:15607977, PubMed:17177976, PubMed:19344625, PubMed:27256882, PubMed:32315358, PubMed:32844745, PubMed:35124853, PubMed:35393539, PubMed:35460603). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed:15607977, PubMed:22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed:27256882, PubMed:35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed:27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed:35393539). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed:33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed:32315358, PubMed:32844745, PubMed:35460603). Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed:35460603). Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). {ECO:0000250|UniProtKB:P11103, ECO:0000269|PubMed:15607977, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:19764761, ECO:0000269|PubMed:20388712, ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:26626479, ECO:0000269|PubMed:26626480, ECO:0000269|PubMed:27067600, ECO:0000269|PubMed:27256882, ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:27471034, ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30257210, ECO:0000269|PubMed:30356214, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:32241924, ECO:0000269|PubMed:32315358, ECO:0000269|PubMed:32358582, ECO:0000269|PubMed:32844745, ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:33412112, ECO:0000269|PubMed:33589610, ECO:0000269|PubMed:33683197, ECO:0000269|PubMed:34049076, ECO:0000269|PubMed:34465625, ECO:0000269|PubMed:34625544, ECO:0000269|PubMed:34732825, ECO:0000269|PubMed:34737271, ECO:0000269|PubMed:34795260, ECO:0000269|PubMed:34874266, ECO:0000269|PubMed:35124853, ECO:0000269|PubMed:35393539, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:7852410, ECO:0000269|PubMed:9315851}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed C-terminus]: Promotes AIFM1-mediated apoptosis (PubMed:33168626). This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis (PubMed:33168626). {ECO:0000269|PubMed:33168626}.; FUNCTION: [Poly [ADP-ribose] polymerase 1, processed N-terminus]: This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis. {ECO:0000269|PubMed:35104452}. |
| P10114 | RAP2A | S66 | ochoa | Ras-related protein Rap-2a (EC 3.6.5.2) (RbBP-30) | Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form (PubMed:14966141, PubMed:15342639, PubMed:16246175, PubMed:16540189, PubMed:18930710, PubMed:20159449, PubMed:35293963). In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK (PubMed:14966141, PubMed:15342639, PubMed:18930710, PubMed:20159449). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (PubMed:20159449). More generally, it is part of several signaling cascades and regulates cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading (PubMed:14966141, PubMed:15342639, PubMed:16246175, PubMed:16540189, PubMed:18930710, PubMed:20159449, PubMed:35293963). {ECO:0000269|PubMed:14966141, ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:16540189, ECO:0000269|PubMed:18930710, ECO:0000269|PubMed:20159449, ECO:0000269|PubMed:35293963}. |
| P10412 | H1-4 | S89 | ochoa | Histone H1.4 (Histone H1b) (Histone H1s-4) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P10588 | NR2F6 | S156 | 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}. |
| P11055 | MYH3 | S1200 | ochoa | Myosin-3 (Muscle embryonic myosin heavy chain) (Myosin heavy chain 3) (Myosin heavy chain, fast skeletal muscle, embryonic) (SMHCE) | Muscle contraction. |
| 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}. |
| P12882 | MYH1 | S1203 | ochoa | Myosin-1 (Myosin heavy chain 1) (Myosin heavy chain 2x) (MyHC-2x) (Myosin heavy chain IIx/d) (MyHC-IIx/d) (Myosin heavy chain, skeletal muscle, adult 1) | Required for normal hearing. It plays a role in cochlear amplification of auditory stimuli, likely through the positive regulation of prestin (SLC26A5) activity and outer hair cell (OHC) electromotility. {ECO:0000250|UniProtKB:Q5SX40}. |
| P12883 | MYH7 | S1199 | 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 | S1269 | 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}. |
| P13010 | XRCC5 | S143 | 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 | S1201 | ochoa | Myosin-6 (Myosin heavy chain 6) (Myosin heavy chain, cardiac muscle alpha isoform) (MyHC-alpha) | Muscle contraction. |
| P14625 | HSP90B1 | S725 | ochoa | 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}. |
| P14923 | JUP | S98 | 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}. |
| P16401 | H1-5 | S92 | ochoa | Histone H1.5 (Histone H1a) (Histone H1b) (Histone H1s-3) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16402 | H1-3 | S90 | ochoa | Histone H1.3 (Histone H1c) (Histone H1s-2) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P16403 | H1-2 | S89 | ochoa | Histone H1.2 (Histone H1c) (Histone H1d) (Histone H1s-1) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| P20936 | RASA1 | S831 | ochoa | Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP) | Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1. {ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:8360177}. |
| P21796 | VDAC1 | S241 | ochoa | Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Porin 31HL) (Porin 31HM) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (hVDAC1) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:30061676, PubMed:8420959). The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959). It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959). The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959). Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). May mediate ATP export from cells (PubMed:30061676). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Mediates cytochrome c efflux (PubMed:20230784). {ECO:0000250|UniProtKB:Q60932, ECO:0000269|PubMed:10661876, ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:25296756, ECO:0000269|PubMed:30061676, ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:8420959}.; FUNCTION: Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids. {ECO:0000269|PubMed:38065946}. |
| P23508 | MCC | S715 | ochoa | Colorectal mutant cancer protein (Protein MCC) | Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}. |
| P25098 | GRK2 | S29 | psp | Beta-adrenergic receptor kinase 1 (Beta-ARK-1) (EC 2.7.11.15) (G-protein coupled receptor kinase 2) | Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them (PubMed:19715378). Key regulator of LPAR1 signaling (PubMed:19306925). Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor (PubMed:19306925). Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (PubMed:19306925). Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity (By similarity). Inhibits relaxation of airway smooth muscle in response to blue light (PubMed:30284927). {ECO:0000250|UniProtKB:P21146, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:19715378, ECO:0000269|PubMed:30284927}. |
| P26373 | RPL13 | S106 | ochoa|psp | Large ribosomal subunit protein eL13 (60S ribosomal protein L13) (Breast basic conserved protein 1) | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:31630789, PubMed:32669547). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (Probable). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). As part of the LSU, it is probably required for its formation and the maturation of rRNAs (PubMed:31630789). Plays a role in bone development (PubMed:31630789). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:31630789, ECO:0000269|PubMed:32669547}. |
| P28908 | TNFRSF8 | S429 | ochoa | Tumor necrosis factor receptor superfamily member 8 (CD30L receptor) (Ki-1 antigen) (Lymphocyte activation antigen CD30) (CD antigen CD30) | Receptor for TNFSF8/CD30L (PubMed:8391931). May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B (PubMed:8999898). {ECO:0000269|PubMed:8391931, ECO:0000269|PubMed:8999898}. |
| P29375 | KDM5A | S970 | 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}. |
| P30086 | PEBP1 | S99 | 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}. |
| P30305 | CDC25B | S230 | ochoa|psp | M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) | Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression (PubMed:1836978, PubMed:20360007). Directly dephosphorylates CDK1 and stimulates its kinase activity (PubMed:20360007). Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner (PubMed:17332740). The three isoforms seem to have a different level of activity (PubMed:1836978). {ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:1836978, ECO:0000269|PubMed:20360007}. |
| P33981 | TTK | S80 | ochoa|psp | Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) | Involved in mitotic spindle assembly checkpoint signaling, a process that delays anaphase until chromosomes are bioriented on the spindle, and in the repair of incorrect mitotic kinetochore-spindle microtubule attachments (PubMed:18243099, PubMed:28441529, PubMed:29162720). Phosphorylates MAD1L1 to promote the mitotic spindle assembly checkpoint (PubMed:18243099, PubMed:29162720). Phosphorylates CDCA8/Borealin leading to enhanced AURKB activity at the kinetochore (PubMed:18243099). Phosphorylates SKA3 at 'Ser-34' leading to dissociation of the SKA complex from microtubules and destabilization of microtubule-kinetochore attachments (PubMed:28441529). Phosphorylates KNL1, KNTC1 and autophosphorylates (PubMed:28441529). Phosphorylates MCRS1 which enhances recruitment of KIF2A to the minus end of spindle microtubules and promotes chromosome alignment (PubMed:30785839). {ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:28441529, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:30785839}. |
| P35228 | NOS2 | S56 | ochoa | Nitric oxide synthase, inducible (EC 1.14.13.39) (Hepatocyte NOS) (HEP-NOS) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) | Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7504305, PubMed:7531687, PubMed:7544004, PubMed:7682706). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (PubMed:25417112). Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8 (PubMed:19688109). {ECO:0000250|UniProtKB:P29477, ECO:0000269|PubMed:19688109, ECO:0000269|PubMed:25417112, ECO:0000269|PubMed:7504305, ECO:0000269|PubMed:7531687, ECO:0000269|PubMed:7544004, ECO:0000269|PubMed:7682706}. |
| P35558 | PCK1 | S19 | ochoa | Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-) | Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:24863970, PubMed:26971250, PubMed:28216384, PubMed:30193097). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:24863970, PubMed:26971250, PubMed:28216384, PubMed:30193097). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (PubMed:32322062). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (PubMed:32322062). {ECO:0000250|UniProtKB:Q9Z2V4, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26971250, ECO:0000269|PubMed:28216384, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:32322062}. |
| P36578 | RPL4 | S275 | ochoa | Large ribosomal subunit protein uL4 (60S ribosomal protein L1) (60S ribosomal protein L4) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
| P36897 | TGFBR1 | S189 | psp | TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) | Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis (PubMed:33914044). The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. {ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:33914044, ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9346908}. |
| P37275 | ZEB1 | S529 | 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}. |
| P40238 | MPL | S531 | ochoa | Thrombopoietin receptor (TPO-R) (Myeloproliferative leukemia protein) (Proto-oncogene c-Mpl) (CD antigen CD110) | Receptor for thrombopoietin that regulates hematopoietic stem cell renewal, megakaryocyte differentiation, and platelet formation. Upon activation by THPO, induces rapid tyrosine phosphorylation and activation of JAK2, providing docking sites for many signaling proteins such as STAT5, SHIP/INPP5D, GRB2, SOS1 and PI3K (PubMed:15899890, PubMed:37633268). In turn, These signaling cascades lead to the proliferation, survival, and differentiation of megakaryocytes, ultimately leading to increased platelet production. {ECO:0000269|PubMed:15899890, ECO:0000269|PubMed:37633268}. |
| P43487 | RANBP1 | S60 | ochoa|psp | Ran-specific GTPase-activating protein (Ran-binding protein 1) (RanBP1) | Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (PubMed:17671426). Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (PubMed:7616957, PubMed:7882974). {ECO:0000250|UniProtKB:P34022, ECO:0000269|PubMed:17671426, ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:7616957, ECO:0000269|PubMed:7882974}. |
| P45973 | CBX5 | S132 | ochoa | Chromobox protein homolog 5 (Antigen p25) (Heterochromatin protein 1 homolog alpha) (HP1 alpha) | Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph) (PubMed:19783980). May contribute to the association of heterochromatin with the inner nuclear membrane by interactions with the lamin-B receptor (LBR) (PubMed:19783980). Involved in the formation of kinetochore through interaction with the MIS12 complex subunit NSL1 (PubMed:19783980, PubMed:20231385). Required for the formation of the inner centromere (PubMed:20231385). {ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20231385}. |
| P46939 | UTRN | S830 | ochoa | Utrophin (Dystrophin-related protein 1) (DRP-1) | May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. |
| P51587 | BRCA2 | S70 | ochoa | 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}. |
| P52272 | HNRNPM | S86 | ochoa | Heterogeneous nuclear ribonucleoprotein M (hnRNP M) | Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines. |
| 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. |
| P53621 | COPA | S756 | 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. |
| P53794 | SLC5A3 | S37 | ochoa | Sodium/myo-inositol cotransporter (Na(+)/myo-inositol cotransporter) (Sodium/myo-inositol transporter 1) (SMIT1) (Solute carrier family 5 member 3) | Electrogenic Na(+)-coupled sugar symporter that actively transports myo-inositol and its stereoisomer scyllo-inositol across the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1 (By similarity). Maintains myo-inositol concentration gradient that defines cell volume and fluid balance during osmotic stress, in particular in the fetoplacental unit and central nervous system (By similarity). Forms coregulatory complexes with voltage-gated K(+) ion channels, allosterically altering ion selectivity, voltage dependence and gating kinetics of the channel. In turn, K(+) efflux through the channel forms a local electrical gradient that modulates electrogenic Na(+)-coupled myo-inositol influx through the transporter (PubMed:24595108, PubMed:28793216). Associates with KCNQ1-KCNE2 channel in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability (By similarity) (PubMed:24595108). Associates with KCNQ2-KCNQ3 channel altering ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (PubMed:28793216). Provides myo-inositol precursor for biosynthesis of phosphoinositides such as PI(4,5)P2, thus indirectly affecting the activity of phosphoinositide-dependent ion channels and Ca(2+) signaling upon osmotic stress (PubMed:27217553). {ECO:0000250|UniProtKB:P31637, ECO:0000250|UniProtKB:Q9JKZ2, ECO:0000269|PubMed:24595108, ECO:0000269|PubMed:27217553, ECO:0000269|PubMed:28793216}. |
| P57737 | CORO7 | S613 | ochoa | Coronin-7 (Crn7) (70 kDa WD repeat tumor rejection antigen homolog) | F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology. {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}. |
| P61225 | RAP2B | S66 | ochoa | Ras-related protein Rap-2b (EC 3.6.5.2) | Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. {ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:15143162, ECO:0000269|PubMed:16540189}. |
| P81408 | ENTREP3 | S574 | ochoa | Protein ENTREP3 (Endosomal transmembrane epsin interactor 3) (Protein COTE1) | None |
| P83916 | CBX1 | S128 | ochoa | Chromobox protein homolog 1 (HP1Hsbeta) (Heterochromatin protein 1 homolog beta) (HP1 beta) (Heterochromatin protein p25) (M31) (Modifier 1 protein) (p25beta) | Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane. {ECO:0000250|UniProtKB:P83917}. |
| Q01196 | RUNX1 | S67 | ochoa | Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B 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 (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. 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). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (By similarity). {ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:14970218, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:17431401, ECO:0000305}.; FUNCTION: Isoform AML-1G shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation. {ECO:0000250|UniProtKB:Q03347}.; FUNCTION: Isoform AML-1L interferes with the transactivation activity of RUNX1. {ECO:0000269|PubMed:9199349}. |
| Q01201 | RELB | S50 | ochoa | Transcription factor RelB (I-Rel) | NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function (PubMed:26385063). {ECO:0000269|PubMed:1732739, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:26385063, ECO:0000269|PubMed:7925301, ECO:0000269|PubMed:8441398}. |
| Q02539 | H1-1 | S92 | ochoa | Histone H1.1 (Histone H1a) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
| Q03001 | DST | S5358 | 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. |
| Q07157 | TJP1 | S212 | 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}. |
| Q08378 | GOLGA3 | S140 | 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. |
| Q12888 | TP53BP1 | S999 | 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}. |
| Q12913 | PTPRJ | S1305 | ochoa | Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (Density-enhanced phosphatase 1) (DEP-1) (HPTP eta) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (CD antigen CD148) | Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (PubMed:10821867, PubMed:12062403, PubMed:12370829, PubMed:12475979, PubMed:18348712, PubMed:19494114, PubMed:19922411, PubMed:21262971). Plays a role in cell adhesion, migration, proliferation and differentiation (PubMed:12370829, PubMed:14709717, PubMed:16682945, PubMed:19836242). Has a role in megakaryocytes and platelet formation (PubMed:30591527). Involved in vascular development (By similarity). Regulator of macrophage adhesion and spreading (By similarity). Positively affects cell-matrix adhesion (By similarity). Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation (PubMed:16682945). Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR (PubMed:21091576). Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation (PubMed:18936167). Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation (PubMed:19836242). Enhances the barrier function of epithelial junctions during reassembly (PubMed:19332538). Negatively regulates T-cell receptor (TCR) signaling (PubMed:11259588, PubMed:9531590, PubMed:9780142). Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling (PubMed:11259588, PubMed:12913111). {ECO:0000250|UniProtKB:Q64455, ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403, ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717, ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411, ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:30591527, ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.; FUNCTION: [Isoform 2]: Activates angiogenesis and cell migration (PubMed:28052032). Downregulates the expression of the endothelial adhesion molecules ICAM1 and VCAM1 (PubMed:28052032). {ECO:0000269|PubMed:28052032}. |
| Q13185 | CBX3 | S132 | ochoa | Chromobox protein homolog 3 (HECH) (Heterochromatin protein 1 homolog gamma) (HP1 gamma) (Modifier 2 protein) | Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1. Mediates the recruitment of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (PubMed:28167679). {ECO:0000250|UniProtKB:P23198, ECO:0000269|PubMed:28167679}. |
| Q13416 | ORC2 | S249 | 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}. |
| Q13435 | SF3B2 | S450 | 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}. |
| Q13470 | TNK1 | S582 | 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}. |
| Q13495 | MAMLD1 | S190 | ochoa | Mastermind-like domain-containing protein 1 (F18) (Protein CG1) | Transactivates the HES3 promoter independently of NOTCH proteins. HES3 is a non-canonical NOTCH target gene which lacks binding sites for RBPJ. {ECO:0000269|PubMed:18162467}. |
| Q13501 | SQSTM1 | S233 | 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}. |
| Q13625 | TP53BP2 | S714 | ochoa | Apoptosis-stimulating of p53 protein 2 (Bcl2-binding protein) (Bbp) (Renal carcinoma antigen NY-REN-51) (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2) | Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (PubMed:12524540). Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of NAE1 to conjugate NEDD8 to CUL1, and thereby decreases NAE1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}. |
| Q13761 | RUNX3 | S71 | 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}. |
| Q13813 | SPTAN1 | S1306 | 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. |
| Q13950 | RUNX2 | S118 | ochoa|psp | 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}. |
| Q14012 | CAMK1 | S333 | ochoa | Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha) | Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I. {ECO:0000250, ECO:0000269|PubMed:11114197, ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:14507913, ECO:0000269|PubMed:14754892, ECO:0000269|PubMed:17056143, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:20181577}. |
| Q14161 | GIT2 | S255 | 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}. |
| Q14789 | GOLGB1 | S560 | 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. |
| Q15111 | PLCL1 | S47 | ochoa | Inactive phospholipase C-like protein 1 (PLC-L1) (Phospholipase C-deleted in lung carcinoma) (Phospholipase C-related but catalytically inactive protein) (PRIP) | Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor (By similarity). Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as an inhibitor of PPP1C. {ECO:0000250, ECO:0000269|PubMed:17254016}. |
| Q15147 | PLCB4 | S521 | ochoa | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-4) (Phospholipase C-beta-4) (PLC-beta-4) | Activated phosphatidylinositol-specific phospholipase C enzymes catalyze the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) involved in G-protein coupled receptor signaling pathways. PLCB4 is a direct effector of the endothelin receptor signaling pathway that plays an essential role in lower jaw and middle ear structures development (PubMed:35284927). {ECO:0000250|UniProtKB:Q07722, ECO:0000269|PubMed:35284927}. |
| Q15334 | LLGL1 | S1044 | ochoa | Lethal(2) giant larvae protein homolog 1 (LLGL) (DLG4) (Hugl-1) (Human homolog to the D-lgl gene protein) | Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane. {ECO:0000269|PubMed:15735678, ECO:0000269|PubMed:16170365}. |
| Q15649 | ZNHIT3 | S88 | ochoa | Zinc finger HIT domain-containing protein 3 (HNF-4a coactivator) (Thyroid hormone receptor interactor 3) (Thyroid receptor-interacting protein 3) (TR-interacting protein 3) (TRIP-3) | None |
| Q15678 | PTPN14 | S465 | 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}. |
| Q15691 | MAPRE1 | S40 | psp | Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27225956, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293, ECO:0000269|PubMed:36592928}. |
| Q15750 | TAB1 | S423 | psp | TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 1) (TGF-beta-activated kinase 1-binding protein 1) (TAK1-binding protein 1) | Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751, PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (PubMed:18021073). {ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:11847341, ECO:0000269|PubMed:14592977, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:22307082, ECO:0000269|PubMed:24403530, ECO:0000269|PubMed:25260751, ECO:0000269|PubMed:29229647, ECO:0000269|PubMed:37832545}. |
| Q16825 | PTPN21 | S471 | ochoa | Tyrosine-protein phosphatase non-receptor type 21 (EC 3.1.3.48) (Protein-tyrosine phosphatase D1) | None |
| Q16849 | PTPRN | Y345 | ochoa | Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (Islet cell antigen 512) (ICA 512) (Islet cell autoantigen 3) (PTP IA-2) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)] | Plays a role in vesicle-mediated secretory processes (PubMed:24843546). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity). Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:24843546). Plays a role in insulin secretion in response to glucose stimuli (PubMed:24843546). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (By similarity). In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (By similarity). Required to maintain normal levels of renin expression and renin release (By similarity). Seems to lack intrinsic enzyme activity (By similarity). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (By similarity). {ECO:0000250|UniProtKB:Q60673, ECO:0000269|PubMed:24843546}.; FUNCTION: [ICA512-transmembrane fragment]: ICA512-TMF regulates dynamics and exocytosis of insulin secretory granules (SGs); binding of ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs mobility and exocytosis by tethering them to the actin cytoskeleton depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF dimerizing with ICA512-TMF and displacing SNTB2. {ECO:0000269|PubMed:18824546, ECO:0000269|PubMed:20886068}.; FUNCTION: [ICA512-cleaved cytosolic fragment]: ICA512-CCF translocated to the nucleus promotes expression of insulin and other granule-related genes; the function implicates binding to and regulating activity of STAT5B probably by preventing its dephosphorylation and potentially by inducing its sumoylation by recruiting PIAS4 (PubMed:15596545, PubMed:16622421, PubMed:18178618). Enhances pancreatic beta-cell proliferation by converging with signaling by STAT5B and STAT3 (PubMed:15596545, PubMed:16622421, PubMed:18178618). ICA512-CCF located in the cytoplasm regulates dynamics and exocytosis of insulin secretory granules (SGs) by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs mobility and exocytosis (PubMed:18824546, PubMed:20886068). {ECO:0000269|PubMed:15596545, ECO:0000269|PubMed:16622421, ECO:0000269|PubMed:18178618, ECO:0000269|PubMed:18824546, ECO:0000269|PubMed:20886068}. |
| Q2M1Z3 | ARHGAP31 | S346 | ochoa|psp | 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}. |
| Q4G0N4 | NADK2 | S188 | ochoa|psp | NAD kinase 2, mitochondrial (EC 2.7.1.23) (Mitochondrial NAD kinase) (NAD kinase domain-containing protein 1, mitochondrial) | Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo. {ECO:0000269|PubMed:23212377}. |
| Q4VX76 | SYTL3 | S185 | ochoa | Synaptotagmin-like protein 3 (Exophilin-6) | May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids in the presence of calcium ions (By similarity). {ECO:0000250}. |
| Q5BKX6 | SLC45A4 | S307 | ochoa | Solute carrier family 45 member 4 | Proton-associated sucrose transporter. May be able to transport also glucose and fructose. {ECO:0000250|UniProtKB:Q0P5V9}. |
| Q5CZC0 | FSIP2 | S3898 | ochoa | Fibrous sheath-interacting protein 2 | Plays a role in spermatogenesis. {ECO:0000305|PubMed:30137358}. |
| Q5FWF5 | ESCO1 | S288 | ochoa | N-acetyltransferase ESCO1 (EC 2.3.1.-) (CTF7 homolog 1) (Establishment factor-like protein 1) (EFO1) (EFO1p) (hEFO1) (Establishment of cohesion 1 homolog 1) (ECO1 homolog 1) (ESO1 homolog 1) | Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:15958495, PubMed:18614053). Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3 (PubMed:18614053). {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:18614053, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161}. |
| Q5GLZ8 | HERC4 | S830 | ochoa | Probable E3 ubiquitin-protein ligase HERC4 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 4) (HECT-type E3 ubiquitin transferase HERC4) | Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates. {ECO:0000250|UniProtKB:Q6PAV2}. |
| Q5M775 | SPECC1 | S692 | ochoa | Cytospin-B (Nuclear structure protein 5) (NSP5) (Sperm antigen HCMOGT-1) (Sperm antigen with calponin homology and coiled-coil domains 1) | None |
| Q5T9S5 | CCDC18 | S1355 | ochoa | Coiled-coil domain-containing protein 18 (Sarcoma antigen NY-SAR-24) | None |
| Q5TF21 | MTCL3 | S641 | ochoa | Microtubule cross-linking factor 3 | None |
| Q5VYK3 | ECPAS | S1826 | ochoa | Proteasome adapter and scaffold protein ECM29 (Ecm29 proteasome adapter and scaffold) (Proteasome-associated protein ECM29 homolog) | Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolysis (PubMed:15496406). Promotes proteasome dissociation under oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q6PDI5, ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:20682791}. |
| Q68EM7 | ARHGAP17 | S306 | ochoa | Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17) (RhoGAP interacting with CIP4 homologs protein 1) (RICH-1) | Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1. {ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}. |
| Q6DN90 | IQSEC1 | S361 | ochoa | IQ motif and SEC7 domain-containing protein 1 (ADP-ribosylation factors guanine nucleotide-exchange protein 100) (ADP-ribosylation factors guanine nucleotide-exchange protein 2) (Brefeldin-resistant Arf-GEF 2 protein) (BRAG2) | Guanine nucleotide exchange factor for ARF1 and ARF6 (PubMed:11226253, PubMed:24058294). Guanine nucleotide exchange factor activity is enhanced by lipid binding (PubMed:24058294). Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin (PubMed:16461286). Involved in neuronal development (Probable). In neurons, plays a role in the control of vesicle formation by endocytoc cargo. Upon long term depression, interacts with GRIA2 and mediates the activation of ARF6 to internalize synaptic AMPAR receptors (By similarity). {ECO:0000250|UniProtKB:A0A0G2JUG7, ECO:0000269|PubMed:11226253, ECO:0000269|PubMed:16461286, ECO:0000269|PubMed:24058294, ECO:0000305|PubMed:31607425}. |
| Q6IQ23 | PLEKHA7 | S986 | 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}. |
| Q6NV74 | CRACDL | S912 | ochoa | CRACD-like protein | None |
| Q6NXE6 | ARMC6 | S80 | ochoa | Armadillo repeat-containing protein 6 | None |
| Q6P4Q7 | CNNM4 | S688 | ochoa | Metal transporter CNNM4 (Ancient conserved domain-containing protein 4) (Cyclin-M4) | Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function. {ECO:0000250, ECO:0000269|PubMed:19200525, ECO:0000269|PubMed:19200527}. |
| Q6R327 | RICTOR | S1385 | 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}. |
| Q6ZN28 | MACC1 | S191 | ochoa | Metastasis-associated in colon cancer protein 1 (SH3 domain-containing protein 7a5) | Acts as a transcription activator for MET and as a key regulator of HGF-MET signaling. Promotes cell motility, proliferation and hepatocyte growth factor (HGF)-dependent scattering in vitro and tumor growth and metastasis in vivo. {ECO:0000269|PubMed:19098908}. |
| Q70J99 | UNC13D | S629 | ochoa | Protein unc-13 homolog D (Munc13-4) | Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000269|PubMed:15548590, ECO:0000269|PubMed:17237785}. |
| Q7L8J4 | SH3BP5L | S350 | ochoa | SH3 domain-binding protein 5-like (SH3BP-5-like) | Functions as a guanine nucleotide exchange factor (GEF) for RAB11A. {ECO:0000269|PubMed:30217979}. |
| Q7Z3U7 | MON2 | S205 | ochoa | Protein MON2 homolog (Protein SF21) | Plays a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269|PubMed:30213940}. |
| Q7Z403 | TMC6 | S112 | ochoa | Transmembrane channel-like protein 6 (Epidermodysplasia verruciformis protein 1) (Protein LAK-4) | Acts as a regulatory protein involved in the regulation of numerous cellular processes (PubMed:18158319, PubMed:30068544, PubMed:32917726). Together with its homolog TMC8/EVER2, forms a complex with CIB1 in lymphocytes and keratynocytes where TMC6 and TMC8 stabilize CIB1 and reciprocally (PubMed:30068544, PubMed:32917726). Together with TMC8, also forms a complex with and activates zinc transporter ZNT1 at the ER membrane of keratynocytes, thereby facilitating zinc uptake into the ER (PubMed:18158319). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also plays a role in thermal sensation by inhibiting the M-channel (KCNQ2-KCNQ3 channel) current in primary sensory neurons (By similarity). {ECO:0000250|UniProtKB:Q7TN60, ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:30068544, ECO:0000269|PubMed:32917726}. |
| Q7Z5K2 | WAPL | S257 | ochoa | Wings apart-like protein homolog (Friend of EBNA2 protein) (WAPL cohesin release factor) | Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin (PubMed:26299517). Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203, ECO:0000269|PubMed:26299517}. |
| Q7Z6Z7 | HUWE1 | S2535 | 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 | S468 | 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}. |
| Q86U86 | PBRM1 | S1405 | ochoa | Protein polybromo-1 (hPB1) (BRG1-associated factor 180) (BAF180) (Polybromo-1D) | 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). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
| Q86UD0 | SAPCD2 | S284 | ochoa | Suppressor APC domain-containing protein 2 (Tumor specificity and mitosis phase-dependent expression protein) (TS/MDEP) (p42.3) | Plays a role in planar mitotic spindle orientation in retinal progenitor cells (RPCs) and promotes the production of symmetric terminal divisions (By similarity). Negatively regulates the mitotic apical cortex localization of GPSM2 (PubMed:26766442). Involved also in positive regulation of cell proliferation and tumor cell growth (PubMed:23576022, PubMed:23704824). {ECO:0000250|UniProtKB:Q9D818, ECO:0000269|PubMed:23576022, ECO:0000269|PubMed:23704824, ECO:0000269|PubMed:26766442}. |
| Q86V42 | FAM124A | S402 | ochoa | Protein FAM124A | None |
| Q86VI3 | IQGAP3 | S1429 | ochoa | Ras GTPase-activating-like protein IQGAP3 | None |
| Q86X40 | LRRC28 | S52 | ochoa | Leucine-rich repeat-containing protein 28 | None |
| Q86XZ4 | SPATS2 | S143 | ochoa | Spermatogenesis-associated serine-rich protein 2 (Serine-rich spermatocytes and round spermatid 59 kDa protein) (p59scr) | None |
| Q86YC2 | PALB2 | S285 | ochoa | Partner and localizer of BRCA2 | Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks (PubMed:16793542, PubMed:19369211, PubMed:19423707, PubMed:22941656, PubMed:24141787, PubMed:28319063). Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA) (PubMed:20871615). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51 (PubMed:20871616). Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination (PubMed:19369211). Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair (PubMed:24141787). Essential partner of BRCA2 that promotes the localization and stability of BRCA2 (PubMed:16793542). Also enables its recombinational repair and checkpoint functions of BRCA2 (PubMed:16793542). May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation (PubMed:16793542). Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures (PubMed:20871616). May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (PubMed:24485656). {ECO:0000269|PubMed:16793542, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:19423707, ECO:0000269|PubMed:20871615, ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:22941656, ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:28319063}. |
| Q86YV0 | RASAL3 | S960 | 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}. |
| Q8IVF7 | FMNL3 | S174 | ochoa|psp | Formin-like protein 3 (Formin homology 2 domain-containing protein 3) (WW domain-binding protein 3) (WBP-3) | Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Required for developmental angiogenesis (By similarity). In this process, required for microtubule reorganization and for efficient endothelial cell elongation. In quiescent endothelial cells, triggers rearrangement of the actin cytoskeleton, but does not alter microtubule alignement. {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22275430}. |
| Q8IWB9 | TEX2 | S389 | 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}. |
| Q8IX12 | CCAR1 | S456 | ochoa | Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain) | Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (PubMed:12816952). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}. |
| Q8IXS8 | HYCC2 | S488 | ochoa | Hyccin 2 | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. {ECO:0000305|PubMed:26571211}. |
| Q8IY67 | RAVER1 | S516 | ochoa | Ribonucleoprotein PTB-binding 1 (Protein raver-1) | Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}. |
| Q8N1S5 | SLC39A11 | S179 | ochoa | Zinc transporter ZIP11 (Solute carrier family 39 member 11) (Zrt- and Irt-like protein 11) (ZIP-11) | Zinc importer that regulates cytosolic zinc concentrations either via zinc influx from the extracellular compartment or efflux from intracellular organelles such as Golgi apparatus. May transport copper ions as well. The transport mechanism remains to be elucidated. {ECO:0000250|UniProtKB:Q8BWY7}. |
| Q8N5H3 | FAM89B | S37 | ochoa | Leucine repeat adapter protein 25 | Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation. {ECO:0000250|UniProtKB:Q9QUI1}. |
| Q8N8E3 | CEP112 | S195 | ochoa | Centrosomal protein of 112 kDa (Cep112) (Coiled-coil domain-containing protein 46) | None |
| Q8N9B5 | JMY | S946 | ochoa | Junction-mediating and -regulatory protein | Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions (PubMed:30420355). In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments (PubMed:30420355). Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments (PubMed:30420355). Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the phagophore membrane surfaces to promote actin assembly during autophagy (PubMed:30420355). The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity). {ECO:0000250|UniProtKB:Q9QXM1, ECO:0000269|PubMed:30420355}. |
| Q8NB91 | FANCB | S456 | ochoa | Fanconi anemia group B protein (Protein FACB) (Fanconi anemia-associated polypeptide of 95 kDa) (FAAP95) | DNA repair protein required for FANCD2 ubiquitination. {ECO:0000269|PubMed:15502827}. |
| Q8TE76 | MORC4 | S532 | 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}. |
| Q8TF40 | FNIP1 | S174 | ochoa | Folliculin-interacting protein 1 | Binding partner of the GTPase-activating protein FLCN: involved in the cellular response to amino acid availability by regulating the non-canonical mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3 (PubMed:17028174, PubMed:18663353, PubMed:24081491, PubMed:37079666). Required to promote FLCN recruitment to lysosomes and interaction with Rag GTPases, leading to activation of the non-canonical mTORC1 signaling (PubMed:24081491). In low-amino acid conditions, component of the lysosomal folliculin complex (LFC) on the membrane of lysosomes, which inhibits the GTPase-activating activity of FLCN, thereby inactivating mTORC1 and promoting nuclear translocation of TFEB and TFE3 (By similarity). Upon amino acid restimulation, disassembly of the LFC complex liberates the GTPase-activating activity of FLCN, leading to activation of mTORC1 and subsequent inactivation of TFEB and TFE3 (PubMed:37079666). Together with FLCN, regulates autophagy: following phosphorylation by ULK1, interacts with GABARAP and promotes autophagy (PubMed:25126726). In addition to its role in mTORC1 signaling, also acts as a co-chaperone of HSP90AA1/Hsp90: following gradual phosphorylation by CK2, inhibits the ATPase activity of HSP90AA1/Hsp90, leading to activate both kinase and non-kinase client proteins of HSP90AA1/Hsp90 (PubMed:27353360, PubMed:30699359). Acts as a scaffold to load client protein FLCN onto HSP90AA1/Hsp90 (PubMed:27353360). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Also acts as a core component of the reductive stress response by inhibiting activation of mitochondria in normal conditions: in response to reductive stress, the conserved Cys degron is reduced, leading to recognition and polyubiquitylation by the CRL2(FEM1B) complex, followed by proteasomal (By similarity). Required for B-cell development (PubMed:32905580). {ECO:0000250|UniProtKB:Q68FD7, ECO:0000250|UniProtKB:Q9P278, ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18663353, ECO:0000269|PubMed:24081491, ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:32905580, ECO:0000269|PubMed:37079666}. |
| Q8TF72 | SHROOM3 | S1138 | 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}. |
| Q8WUR7 | C15orf40 | S116 | ochoa | UPF0235 protein C15orf40 | None |
| Q8WUY3 | PRUNE2 | S1723 | ochoa | Protein prune homolog 2 (BNIP2 motif-containing molecule at the C-terminal region 1) | May play an important role in regulating differentiation, survival and aggressiveness of the tumor cells. {ECO:0000269|PubMed:16288218}. |
| Q8WVV4 | POF1B | S83 | 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}. |
| Q8WYQ5 | DGCR8 | S677 | psp | 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}. |
| Q8WYQ5 | DGCR8 | S714 | 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}. |
| Q92621 | NUP205 | S1942 | ochoa | Nuclear pore complex protein Nup205 (205 kDa nucleoporin) (Nucleoporin Nup205) | Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC (PubMed:15229283). In association with TMEM209, may be involved in nuclear transport of various nuclear proteins in addition to MYC (PubMed:22719065). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22719065, ECO:0000269|PubMed:9348540}. |
| Q969K3 | RNF34 | S254 | ochoa | E3 ubiquitin-protein ligase RNF34 (EC 2.3.2.27) (Caspase regulator CARP1) (Caspases-8 and -10-associated RING finger protein 1) (CARP-1) (FYVE-RING finger protein Momo) (Human RING finger homologous to inhibitor of apoptosis protein) (hRFI) (RING finger protein 34) (RING finger protein RIFF) (RING-type E3 ubiquitin transferase RNF34) | E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. 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 (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219). {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:15897238, ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219, ECO:0000269|Ref.13, ECO:0000303|PubMed:18382127}. |
| Q96AC1 | FERMT2 | S332 | ochoa | 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 | S371 | ochoa | 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}. |
| Q96BJ8 | ELMO3 | Y498 | ochoa | Engulfment and cell motility protein 3 | Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). {ECO:0000250}. |
| Q96C57 | CUSTOS | S58 | ochoa | Protein CUSTOS | Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}. |
| Q96DY7 | MTBP | S597 | 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}. |
| Q96H55 | MYO19 | S498 | ochoa | Unconventional myosin-XIX (Myosin head domain-containing protein 1) | Actin-based motor molecule with ATPase activity that localizes to the mitochondrion outer membrane (PubMed:19932026, PubMed:23568824, PubMed:25447992). Motor protein that moves towards the plus-end of actin filaments (By similarity). Required for mitochondrial inheritance during mitosis (PubMed:25447992). May be involved in mitochondrial transport or positioning (PubMed:23568824). {ECO:0000250|UniProtKB:Q5SV80, ECO:0000269|PubMed:19932026, ECO:0000269|PubMed:25447992, ECO:0000305|PubMed:23568824}. |
| Q96JC1 | VPS39 | S439 | ochoa | Vam6/Vps39-like protein (TRAP1-like protein) (hVam6p) | Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2-dependent transcription. Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation. {ECO:0000269|PubMed:12941698}.; FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Acts as a component of the HOPS endosomal tethering complex. This complex is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (PubMed:23351085). Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes (PubMed:11448994, PubMed:23167963, PubMed:23351085). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203, PubMed:37821429). {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:25783203, ECO:0000269|PubMed:33422265, ECO:0000269|PubMed:37821429, ECO:0000305|PubMed:23351085}. |
| Q96SN8 | CDK5RAP2 | S1490 | 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}. |
| Q96T23 | RSF1 | S1226 | 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}. |
| Q99447 | PCYT2 | S336 | ochoa | Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine transferase) | Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway (PubMed:31637422, PubMed:9083101). Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis (PubMed:9083101). {ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101, ECO:0000303|PubMed:9083101}. |
| Q99733 | NAP1L4 | Y55 | ochoa | Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2) (NAP-2) | Acts as a histone chaperone in nucleosome assembly. {ECO:0000269|PubMed:9325046}. |
| Q99759 | MAP3K3 | S311 | ochoa | Mitogen-activated protein kinase kinase kinase 3 (EC 2.7.11.25) (MAPK/ERK kinase kinase 3) (MEK kinase 3) (MEKK 3) | Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. {ECO:0000269|PubMed:12912994, ECO:0000269|PubMed:14661019, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:33729480, ECO:0000269|PubMed:33891857, ECO:0000269|PubMed:9006902}. |
| Q9BQI9 | NRIP2 | S96 | ochoa | Nuclear receptor-interacting protein 2 | Down-regulates transcriptional activation by nuclear receptors such as NR1F2. {ECO:0000250}. |
| Q9BZF1 | OSBPL8 | S19 | 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 | S318 | 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}. |
| Q9H171 | ZBP1 | S27 | ochoa | Z-DNA-binding protein 1 (DNA-dependent activator of IFN-regulatory factors) (DAI) (Tumor stroma and activated macrophage protein DLM-1) | Key innate sensor that recognizes and binds Z-RNA structures, which are produced by a number of viruses, such as herpesvirus, orthomyxovirus or flavivirus, and triggers different forms of cell death (PubMed:32200799). ZBP1 acts as an essential mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, by activating RIPK3, caspase-8 (CASP8), and the NLRP3 inflammasome (By similarity). Key activator of necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, via its ability to bind Z-RNA: once activated upon Z-RNA-binding, ZBP1 interacts and stimulates RIPK3 kinase, which phosphorylates and activates MLKL, triggering execution of programmed necrosis (By similarity). In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: ZBP1 recognizes and binds Z-RNA structures that are produced in infected nuclei by orthomyxoviruses, such as the influenza A virus (IAV), leading to ZBP1 activation, RIPK3 stimulation and subsequent MLKL phosphorylation, triggering disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (PubMed:32200799). ZBP1-dependent cell death in response to IAV infection promotes interleukin-1 alpha (IL1A) induction in an NLRP3-inflammasome-independent manner: IL1A expression is required for the optimal interleukin-1 beta (IL1B) production, and together, these cytokines promote infiltration of inflammatory neutrophils to the lung, leading to the formation of neutrophil extracellular traps (By similarity). In addition to its direct role in driving necroptosis via its ability to sense Z-RNAs, also involved in PANoptosis triggered in response to bacterial infection: component of the AIM2 PANoptosome complex, a multiprotein complex that triggers PANoptosis (By similarity). Also acts as the apical sensor of fungal infection responsible for activating PANoptosis (By similarity). Involved in CASP8-mediated cell death via its interaction with RIPK1 but independently of its ability to sense Z-RNAs (By similarity). In some cell types, also able to restrict viral replication by promoting cell death-independent responses (By similarity). In response to Zika virus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with RIPK3, promotes a death-independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate (By similarity). Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). {ECO:0000250|UniProtKB:Q9QY24, ECO:0000269|PubMed:32200799}.; FUNCTION: (Microbial infection) In case of herpes simplex virus 1/HHV-1 infection, forms hetero-amyloid structures with HHV-1 protein RIR1/ICP6 which may inhibit ZBP1-mediated necroptosis, thereby preventing host cell death pathway and allowing viral evasion. {ECO:0000269|PubMed:33348174}. |
| Q9H2J7 | SLC6A15 | S648 | ochoa | Sodium-dependent neutral amino acid transporter B(0)AT2 (Sodium- and chloride-dependent neurotransmitter transporter NTT73) (Sodium-coupled branched-chain amino-acid transporter 1) (Solute carrier family 6 member 15) (Transporter v7-3) | Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Can also transport low-affinity substrates such as alanine, phenylalanine, glutamine and pipecolic acid. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent. {ECO:0000269|PubMed:16226721}. |
| Q9H2U1 | DHX36 | S167 | ochoa | ATP-dependent DNA/RNA helicase DHX36 (EC 3.6.4.12) (EC 3.6.4.13) (DEAD/H box polypeptide 36) (DEAH-box protein 36) (G4-resolvase-1) (G4R1) (MLE-like protein 1) (RNA helicase associated with AU-rich element protein) | Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (PubMed:16150737, PubMed:18854321, PubMed:20472641, PubMed:21586581). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:14731398, PubMed:18279852, PubMed:21993297, PubMed:22238380, PubMed:25579584). G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-DNA and G4-RNA) (PubMed:16150737, PubMed:18842585, PubMed:20472641, PubMed:21586581, PubMed:24369427, PubMed:26195789). Plays a role in genomic integrity (PubMed:22238380). Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (PubMed:20472641, PubMed:21149580, PubMed:21846770, PubMed:22238380, PubMed:24151078, PubMed:25579584). Plays a role in transcriptional regulation (PubMed:21586581, PubMed:21993297). Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (PubMed:21993297). Plays a role in post-transcriptional regulation (PubMed:27940037). Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (PubMed:27940037). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment (By similarity). Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size (By similarity). Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability (PubMed:24369427, PubMed:26489465). Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression (PubMed:24369427). Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively (PubMed:26489465). Also binds to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (PubMed:14731398, PubMed:18279852). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (PubMed:14731398). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity). Required for early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification (By similarity). {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q8VHK9, ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:18854321, ECO:0000269|PubMed:20472641, ECO:0000269|PubMed:21149580, ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21846770, ECO:0000269|PubMed:21993297, ECO:0000269|PubMed:22238380, ECO:0000269|PubMed:24151078, ECO:0000269|PubMed:24369427, ECO:0000269|PubMed:25579584, ECO:0000269|PubMed:26195789, ECO:0000269|PubMed:26489465, ECO:0000269|PubMed:27940037}. |
| Q9H8V3 | ECT2 | S365 | 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}. |
| Q9H987 | SYNPO2L | S401 | ochoa | Synaptopodin 2-like protein | Actin-associated protein that may play a role in modulating actin-based shape. {ECO:0000250}. |
| Q9H9Q4 | NHEJ1 | S263 | 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}. |
| Q9HAW4 | CLSPN | S1147 | 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}. |
| Q9HBA0 | TRPV4 | S162 | psp | Transient receptor potential cation channel subfamily V member 4 (TrpV4) (Osm-9-like TRP channel 4) (OTRPC4) (Transient receptor potential protein 12) (TRP12) (Vanilloid receptor-like channel 2) (Vanilloid receptor-like protein 2) (VRL-2) (Vanilloid receptor-related osmotically-activated channel) (VR-OAC) | Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:16293632, PubMed:18695040, PubMed:18826956, PubMed:22526352, PubMed:23136043, PubMed:29899501). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:18695040, PubMed:18826956, PubMed:29899501). Also activated by heat, low pH, citrate and phorbol esters (PubMed:16293632, PubMed:18695040, PubMed:18826956, PubMed:20037586, PubMed:21964574, PubMed:25256292). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (PubMed:12724311, PubMed:18826956). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (PubMed:19759329). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (PubMed:19759329). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to pro-inflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). Required for normal development and maintenance of bone and cartilage (PubMed:26249260). In its inactive state, may sequester DDX3X at the plasma membrane. When activated, the interaction between both proteins is affected and DDX3X relocalizes to the nucleus (PubMed:29899501). In neurons of the central nervous system, could play a role in triggering voluntary water intake in response to increased sodium concentration in body fluid (By similarity). {ECO:0000250|UniProtKB:Q9EPK8, ECO:0000269|PubMed:11025659, ECO:0000269|PubMed:12724311, ECO:0000269|PubMed:16293632, ECO:0000269|PubMed:18587396, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:19759329, ECO:0000269|PubMed:20037586, ECO:0000269|PubMed:21964574, ECO:0000269|PubMed:23136043, ECO:0000269|PubMed:25256292, ECO:0000269|PubMed:26249260, ECO:0000269|PubMed:29899501}.; FUNCTION: [Isoform 1]: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by phorbol esters. Has the same channel activity as isoform 1, and is activated by the same stimuli. {ECO:0000269|PubMed:16293632}.; FUNCTION: [Isoform 5]: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by phorbol esters. Has the same channel activity as isoform 1, and is activated by the same stimuli. {ECO:0000269|PubMed:16293632}.; FUNCTION: [Isoform 2]: Lacks channel activity, due to impaired oligomerization and intracellular retention. {ECO:0000269|PubMed:16293632}.; FUNCTION: [Isoform 4]: Lacks channel activity, due to impaired oligomerization and intracellular retention. {ECO:0000269|PubMed:16293632}.; FUNCTION: [Isoform 6]: Lacks channel activity, due to impaired oligomerization and intracellular retention. {ECO:0000269|PubMed:16293632}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication, possibly through its action on DDX3X. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication, possibly through its action on DDX3X. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication, possibly through its action on DDX3X. {ECO:0000269|PubMed:29899501}. |
| Q9HBD1 | RC3H2 | S983 | 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}. |
| Q9HCS7 | XAB2 | S803 | ochoa | Pre-mRNA-splicing factor SYF1 (Protein HCNP) (XPA-binding protein 2) | Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770). Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing (PubMed:10944529, PubMed:17981804). {ECO:0000269|PubMed:10944529, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. |
| Q9NRL3 | STRN4 | S342 | ochoa | Striatin-4 (Zinedin) | Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:32640226). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:32640226). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). Key regulator of the expanded Hippo signaling pathway by interacting and allowing the inhibition of MAP4K kinases by the STRIPAK complex (PubMed:32640226). {ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:32640226, ECO:0000305|PubMed:26876214}. |
| Q9NUQ6 | SPATS2L | S531 | ochoa | SPATS2-like protein (DNA polymerase-transactivated protein 6) (Stress granule and nucleolar protein) (SGNP) | None |
| Q9NWU2 | GID8 | S188 | ochoa | Glucose-induced degradation protein 8 homolog (Two hybrid-associated protein 1 with RanBPM) (Twa1) | 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). Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation (PubMed:28829046). {ECO:0000269|PubMed:28829046, ECO:0000269|PubMed:29911972}. |
| Q9NXF1 | TEX10 | S293 | ochoa | Testis-expressed protein 10 | 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). Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (PubMed:21326211). {ECO:0000269|PubMed:21326211, ECO:0000269|PubMed:22872859}. |
| Q9NZM1 | MYOF | S174 | ochoa | Myoferlin (Fer-1-like protein 3) | Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}. |
| Q9P0J1 | PDP1 | S292 | psp | [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) | Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. {ECO:0000269|PubMed:15554715, ECO:0000305|PubMed:15855260}. |
| Q9P206 | NHSL3 | S215 | ochoa | NHS-like protein 3 | Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269|PubMed:32854746}. |
| Q9P227 | ARHGAP23 | S677 | ochoa | Rho GTPase-activating protein 23 (Rho-type GTPase-activating protein 23) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. |
| Q9P2F8 | SIPA1L2 | S1549 | ochoa | Signal-induced proliferation-associated 1-like protein 2 (SIPA1-like protein 2) | None |
| Q9P2N6 | KANSL3 | S559 | ochoa | KAT8 regulatory NSL complex subunit 3 (NSL complex protein NSL3) (Non-specific lethal 3 homolog) (Serum inhibited-related protein) (Testis development protein PRTD) | 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:33657400). The NSL complex also acts as a regulator of gene expression in mitochondria (PubMed:27768893). Within the NSL complex, KANSL3 is required to promote KAT8 association with mitochondrial DNA (PubMed:27768893). Required for transcription of intraciliary transport genes in both ciliated and non-ciliated cells (By similarity). This is necessary for cilium assembly in ciliated cells and for organization of the microtubule cytoskeleton in non-ciliated cells (By similarity). Also required within the NSL complex to maintain nuclear architecture stability by promoting KAT8-mediated acetylation of lamin LMNA (By similarity). Plays an essential role in spindle assembly during mitosis (PubMed:26243146). Acts as a microtubule minus-end binding protein which stabilizes microtubules and promotes their assembly (PubMed:26243146). Indispensable during early embryonic development where it is required for proper lineage specification and maintenance during peri-implantation development and is essential for implantation (By similarity). {ECO:0000250|UniProtKB:A2RSY1, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:26243146, ECO:0000269|PubMed:27768893, ECO:0000269|PubMed:33657400}. |
| Q9UBX3 | SLC25A10 | S93 | ochoa | Mitochondrial dicarboxylate carrier (DIC) (Solute carrier family 25 member 10) | Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity). {ECO:0000250|UniProtKB:Q9QZD8, ECO:0000269|PubMed:29211846}. |
| Q9UGL1 | KDM5B | S986 | ochoa | Lysine-specific demethylase 5B (EC 1.14.11.67) (Cancer/testis antigen 31) (CT31) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) (Retinoblastoma-binding protein 2 homolog 1) (RBP2-H1) ([histone H3]-trimethyl-L-lysine(4) demethylase 5B) | Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code (PubMed:24952722, PubMed:27214403, PubMed:28262558). Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5 (PubMed:24952722). In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity). {ECO:0000250|UniProtKB:Q80Y84, ECO:0000269|PubMed:12657635, ECO:0000269|PubMed:16645588, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17363312, ECO:0000269|PubMed:24952722, ECO:0000269|PubMed:26645689, ECO:0000269|PubMed:26741168, ECO:0000269|PubMed:27214403, ECO:0000269|PubMed:28262558}. |
| Q9UH62 | ARMCX3 | S288 | ochoa | Armadillo repeat-containing X-linked protein 3 (ARM protein lost in epithelial cancers on chromosome X 3) (Protein ALEX3) | Regulates mitochondrial aggregation and transport in axons in living neurons. May link mitochondria to the TRAK2-kinesin motor complex via its interaction with Miro and TRAK2. Mitochondrial distribution and dynamics is regulated through ARMCX3 protein degradation, which is promoted by PCK and negatively regulated by WNT1. Enhances the SOX10-mediated transactivation of the neuronal acetylcholine receptor subunit alpha-3 and beta-4 subunit gene promoters. {ECO:0000250|UniProtKB:Q8BHS6}. |
| Q9UIF9 | BAZ2A | S1747 | 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}. |
| Q9UIJ7 | AK3 | S37 | ochoa | GTP:AMP phosphotransferase AK3, mitochondrial (EC 2.7.4.10) (Adenylate kinase 3) (Adenylate kinase 3 alpha-like 1) (Adenylate kinase isozyme 3) | Mitochondrial adenylate kinase with a specific GTP:AMP phosphotransferase activity (PubMed:11485571, PubMed:32822537). Could also use ITP as phosphate donor (PubMed:11485571). Its physiological function is to recycle GTP into GDP which is necessary for the TCA cycle in the mitochondrial matrix (Probable). {ECO:0000269|PubMed:11485571, ECO:0000269|PubMed:32822537, ECO:0000305|PubMed:11485571, ECO:0000305|PubMed:35457131}. |
| Q9UKV0 | HDAC9 | S491 | ochoa | Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR) | 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. Represses MEF2-dependent transcription. {ECO:0000269|PubMed:11535832}.; FUNCTION: Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter. |
| Q9UKX2 | MYH2 | S1205 | ochoa | Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. |
| Q9ULC5 | ACSL5 | S605 | ochoa | Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5) | Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:17681178, PubMed:22633490, PubMed:24269233, PubMed:33191500). ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells. {ECO:0000250, ECO:0000269|PubMed:17681178, ECO:0000269|PubMed:18806831, ECO:0000269|PubMed:19459852, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233, ECO:0000269|PubMed:33191500}. |
| Q9ULL1 | PLEKHG1 | S695 | ochoa | Pleckstrin homology domain-containing family G member 1 | None |
| Q9ULL4 | PLXNB3 | S1589 | ochoa | Plexin-B3 | Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}. |
| Q9ULU4 | ZMYND8 | S1117 | 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}. |
| Q9UPV0 | CEP164 | S1085 | 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}. |
| Q9UQC2 | GAB2 | S264 | 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}. |
| Q9Y277 | VDAC3 | S241 | ochoa | Non-selective voltage-gated ion channel VDAC3 (VDAC-3) (hVDAC3) (Outer mitochondrial membrane protein porin 3) | Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:31935282). Forms a high-conducting channel with a stable open state and a voltage-induced closure with a mild preference for anions over cations (PubMed:31935282). Involved in male fertility and sperm mitochondrial sheath formation (By similarity). {ECO:0000250|UniProtKB:Q60931, ECO:0000269|PubMed:31935282}. |
| Q9Y2F5 | ICE1 | S1617 | 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}. |
| Q9Y2I8 | WDR37 | S114 | ochoa | WD repeat-containing protein 37 | Required for normal ER Ca2+ handling in lymphocytes. Together with PACS1, it plays an essential role in stabilizing peripheral lymphocyte populations. {ECO:0000250|UniProtKB:Q8CBE3}. |
| Q9Y2L5 | TRAPPC8 | S273 | 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}. |
| Q9Y3L5 | RAP2C | S66 | ochoa | Ras-related protein Rap-2c (EC 3.6.5.2) | Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription. {ECO:0000269|PubMed:17447155}. |
| Q9Y485 | DMXL1 | S1271 | ochoa | DmX-like protein 1 (X-like 1 protein) | None |
| Q9Y490 | TLN1 | S604 | 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}. |
| Q9Y4B5 | MTCL1 | S630 | 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}. |
| Q9Y5K6 | CD2AP | S582 | 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}. |
| Q9Y5Q9 | GTF3C3 | S495 | ochoa | General transcription factor 3C polypeptide 3 (Transcription factor IIIC 102 kDa subunit) (TFIIIC 102 kDa subunit) (TFIIIC102) (Transcription factor IIIC subunit gamma) (TF3C-gamma) | Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters. |
| Q9Y5S2 | CDC42BPB | S1191 | 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}. |
| Q9Y5T5 | USP16 | S386 | psp | Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-processing protease UBP-M) (Ubiquitin-specific-processing protease 16) | Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator (PubMed:17914355). Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis (PubMed:17914355). In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination (PubMed:17914355). Prefers nucleosomal substrates (PubMed:17914355). Does not deubiquitinate histone H2B (PubMed:17914355). Also deubiquitinates non-histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit (PubMed:32129764). Also mediates deubiquitination of tektin proteins (TEKT1, TEKT2, TEK3, TEKT4 and TEKT5), promoting their stability. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:17914355, ECO:0000269|PubMed:32129764}. |
| P61221 | ABCE1 | S218 | Sugiyama | ATP-binding cassette sub-family E member 1 (EC 3.6.5.-) (2'-5'-oligoadenylate-binding protein) (HuHP68) (RNase L inhibitor) (Ribonuclease 4 inhibitor) (RNS4I) | Nucleoside-triphosphatase (NTPase) involved in ribosome recycling by mediating ribosome disassembly (PubMed:20122402, PubMed:21448132). Able to hydrolyze ATP, GTP, UTP and CTP (PubMed:20122402). Splits ribosomes into free 60S subunits and tRNA- and mRNA-bound 40S subunits (PubMed:20122402, PubMed:21448132). Acts either after canonical termination facilitated by release factors (ETF1/eRF1) or after recognition of stalled and vacant ribosomes by mRNA surveillance factors (PELO/Pelota) (PubMed:20122402, PubMed:21448132). Involved in the No-Go Decay (NGD) pathway: recruited to stalled ribosomes by the Pelota-HBS1L complex, and drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132). Also plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA (PubMed:29861391). As part of the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria damage; this modification generates polyubiquitin signals that recruit autophagy receptors to the mitochondrial outer membrane and initiate mitophagy (PubMed:29861391). RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL (PubMed:9660177). Negative regulator of the anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway (PubMed:11585831, PubMed:9660177, PubMed:9847332). {ECO:0000269|PubMed:11585831, ECO:0000269|PubMed:20122402, ECO:0000269|PubMed:21448132, ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.; FUNCTION: (Microbial infection) May act as a chaperone for post-translational events during HIV-1 capsid assembly. {ECO:0000269|PubMed:9847332}.; FUNCTION: (Microbial infection) Plays a role in the down-regulation of the 2-5A/RNASEL pathway during encephalomyocarditis virus (EMCV) and HIV-1 infections. {ECO:0000269|PubMed:9660177}. |
| P55209 | NAP1L1 | Y66 | Sugiyama | Nucleosome assembly protein 1-like 1 (NAP-1-related protein) (hNRP) | Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity). {ECO:0000250|UniProtKB:P28656, ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:24798879, ECO:0000269|PubMed:26841755, ECO:0000269|PubMed:28369616}.; FUNCTION: (Microbial infection) Positively regulates Epstein-Barr virus reactivation in epithelial cells through the induction of viral BZLF1 expression. {ECO:0000269|PubMed:23691099}.; FUNCTION: (Microbial infection) Together with human herpesvirus 8 protein LANA1, assists the proper assembly of the nucleosome on the replicated viral DNA. {ECO:0000269|PubMed:27599637}. |
| Q13155 | AIMP2 | S51 | Sugiyama | Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) | Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. {ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:19131329}. |
| P08195 | SLC3A2 | S518 | 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}. |
| Q86V81 | ALYREF | S142 | Sugiyama | THO complex subunit 4 (Tho4) (Ally of AML-1 and LEF-1) (Aly/REF export factor) (Transcriptional coactivator Aly/REF) (bZIP-enhancing factor BEF) | Functions as an mRNA export adapter; component of the transcription/export (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). 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). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B (PubMed:17984224). Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex (PubMed:37020021). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:37020021). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224, PubMed:37020021). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway) (PubMed:11675789, PubMed:11707413, PubMed:11979277, PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim (PubMed:19165146). Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (PubMed:28418038). Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation (PubMed:10488337). Involved in transcription elongation and genome stability (PubMed:12438613). {ECO:0000269|PubMed:10488337, ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:11707413, ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:37020021}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. {ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:18974867}. |
| Q13155 | AIMP2 | S48 | Sugiyama | Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) | Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. {ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:19131329}. |
| O60506 | SYNCRIP | Y47 | Sugiyama | Heterogeneous nuclear ribonucleoprotein Q (hnRNP Q) (Glycine- and tyrosine-rich RNA-binding protein) (GRY-RBP) (NS1-associated protein 1) (Synaptotagmin-binding, cytoplasmic RNA-interacting protein) | Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648, ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23071094}. |
| P22415 | USF1 | Y250 | Sugiyama | Upstream stimulatory factor 1 (Class B basic helix-loop-helix protein 11) (bHLHb11) (Major late transcription factor 1) | Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. |
| O14964 | HGS | Y466 | Sugiyama | 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. |
| P35579 | MYH9 | S1376 | Sugiyama | Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000269|PubMed:20944748, ECO:0000269|PubMed:39048823}. |
| Q9NY61 | AATF | S288 | PSP | 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}. |
| O00273 | DFFA | S302 | Sugiyama | DNA fragmentation factor subunit alpha (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) (ICAD) | Inhibitor of the caspase-activated DNase (DFF40). |
| O60664 | PLIN3 | S254 | Sugiyama | 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}. |
| P51812 | RPS6KA3 | S66 | Sugiyama | 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}. |
| Q15349 | RPS6KA2 | S57 | 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}. |
| Q6PHR2 | ULK3 | S300 | GPS6|SIGNOR|EPSD|PSP | Serine/threonine-protein kinase ULK3 (EC 2.7.11.1) (Unc-51-like kinase 3) | Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy. {ECO:0000269|PubMed:19279323, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:20643644}. |
| Q6XUX3 | DSTYK | S603 | Sugiyama | Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (RIP-homologous kinase) (Receptor-interacting serine/threonine-protein kinase 5) (Sugen kinase 496) (SgK496) | Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation (PubMed:23862974, PubMed:28157540). Involved in the regulation of both caspase-dependent apoptosis and caspase-independent cell death (PubMed:15178406). In the skin, it plays a predominant role in suppressing caspase-dependent apoptosis in response to UV stress in a range of dermal cell types (PubMed:28157540). {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974, ECO:0000269|PubMed:28157540}. |
| Q9UPQ9 | TNRC6B | S1086 | Sugiyama | 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}. |
| O43290 | SART1 | S624 | 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}. |
| Q9UIQ6 | LNPEP | S670 | Sugiyama | 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}. |
| Q9P2E9 | RRBP1 | S1233 | Sugiyama | Ribosome-binding protein 1 (180 kDa ribosome receptor homolog) (RRp) (ES/130-related protein) (Ribosome receptor protein) | Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}. |
| Q9UHD2 | TBK1 | S348 | Sugiyama | Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1) | Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755, PubMed:32298923). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653, PubMed:37926288). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, which leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595). Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR (PubMed:29150432, PubMed:31530866). Acts as a positive regulator of the mTORC2 complex by mediating phosphorylation of MTOR, leading to increased phosphorylation and activation of AKT1 (By similarity). Phosphorylates and activates AKT1 (PubMed:21464307). Involved in the regulation of TNF-induced RIPK1-mediated cell death, probably acting via CYLD phosphorylation that in turn controls RIPK1 ubiquitination status (PubMed:34363755). Also participates in the differentiation of T follicular regulatory cells together with the receptor ICOS (PubMed:27135603). {ECO:0000250|UniProtKB:Q9WUN2, ECO:0000269|PubMed:10581243, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11839743, ECO:0000269|PubMed:12692549, ECO:0000269|PubMed:12702806, ECO:0000269|PubMed:14703513, ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15485837, ECO:0000269|PubMed:15489227, ECO:0000269|PubMed:16155125, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21270402, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:22851595, ECO:0000269|PubMed:23453971, ECO:0000269|PubMed:23453972, ECO:0000269|PubMed:23746807, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26611359, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27135603, ECO:0000269|PubMed:29150432, ECO:0000269|PubMed:30842653, ECO:0000269|PubMed:31530866, ECO:0000269|PubMed:31709703, ECO:0000269|PubMed:32298923, ECO:0000269|PubMed:32972995, ECO:0000269|PubMed:34363755, ECO:0000269|PubMed:37926288}. |
| Q08211 | DHX9 | S623 | Sugiyama | 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}. |
Download
| reactome_id | name | p | -log10_p |
|---|---|---|---|
| R-HSA-3371571 | HSF1-dependent transactivation | 1.287139e-08 | 7.890 |
| R-HSA-75153 | Apoptotic execution phase | 8.624435e-08 | 7.064 |
| R-HSA-3371556 | Cellular response to heat stress | 1.696893e-07 | 6.770 |
| R-HSA-1640170 | Cell Cycle | 3.010417e-07 | 6.521 |
| R-HSA-9022692 | Regulation of MECP2 expression and activity | 5.174950e-06 | 5.286 |
| R-HSA-69278 | Cell Cycle, Mitotic | 6.624321e-06 | 5.179 |
| R-HSA-3371568 | Attenuation phase | 8.017008e-06 | 5.096 |
| R-HSA-9856651 | MITF-M-dependent gene expression | 2.937973e-05 | 4.532 |
| R-HSA-2262752 | Cellular responses to stress | 3.657395e-05 | 4.437 |
| R-HSA-8986944 | Transcriptional Regulation by MECP2 | 3.559352e-05 | 4.449 |
| R-HSA-140342 | Apoptosis induced DNA fragmentation | 4.282826e-05 | 4.368 |
| R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 4.937700e-05 | 4.306 |
| R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 6.439897e-05 | 4.191 |
| R-HSA-3371511 | HSF1 activation | 6.433846e-05 | 4.192 |
| R-HSA-8953897 | Cellular responses to stimuli | 7.052703e-05 | 4.152 |
| R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 7.420515e-05 | 4.130 |
| R-HSA-426496 | Post-transcriptional silencing by small RNAs | 1.481216e-04 | 3.829 |
| R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 1.392168e-04 | 3.856 |
| R-HSA-9649948 | Signaling downstream of RAS mutants | 1.392168e-04 | 3.856 |
| R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 1.392168e-04 | 3.856 |
| R-HSA-141424 | Amplification of signal from the kinetochores | 1.452387e-04 | 3.838 |
| R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 1.452387e-04 | 3.838 |
| R-HSA-3700989 | Transcriptional Regulation by TP53 | 1.176286e-04 | 3.929 |
| R-HSA-68877 | Mitotic Prometaphase | 1.213481e-04 | 3.916 |
| R-HSA-6802949 | Signaling by RAS mutants | 1.392168e-04 | 3.856 |
| R-HSA-68886 | M Phase | 1.542661e-04 | 3.812 |
| R-HSA-9700206 | Signaling by ALK in cancer | 1.301186e-04 | 3.886 |
| R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 1.301186e-04 | 3.886 |
| R-HSA-5357801 | Programmed Cell Death | 1.553048e-04 | 3.809 |
| R-HSA-109581 | Apoptosis | 9.353403e-05 | 4.029 |
| R-HSA-9730414 | MITF-M-regulated melanocyte development | 1.331788e-04 | 3.876 |
| R-HSA-9020591 | Interleukin-12 signaling | 1.157474e-04 | 3.936 |
| R-HSA-5673000 | RAF activation | 1.790862e-04 | 3.747 |
| R-HSA-69620 | Cell Cycle Checkpoints | 1.815369e-04 | 3.741 |
| R-HSA-2559584 | Formation of Senescence-Associated Heterochromatin Foci (SAHF) | 2.209125e-04 | 3.656 |
| R-HSA-9764562 | Regulation of CDH1 mRNA translation by microRNAs | 3.106659e-04 | 3.508 |
| R-HSA-6802957 | Oncogenic MAPK signaling | 3.698545e-04 | 3.432 |
| R-HSA-111465 | Apoptotic cleavage of cellular proteins | 4.027154e-04 | 3.395 |
| R-HSA-5633007 | Regulation of TP53 Activity | 4.181733e-04 | 3.379 |
| R-HSA-442742 | CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling | 4.912541e-04 | 3.309 |
| R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 4.912541e-04 | 3.309 |
| R-HSA-8953750 | Transcriptional Regulation by E2F6 | 4.668087e-04 | 3.331 |
| R-HSA-447115 | Interleukin-12 family signaling | 5.251413e-04 | 3.280 |
| R-HSA-9764265 | Regulation of CDH1 Expression and Function | 5.769041e-04 | 3.239 |
| R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 5.769041e-04 | 3.239 |
| R-HSA-9824594 | Regulation of MITF-M-dependent genes involved in apoptosis | 5.537012e-04 | 3.257 |
| R-HSA-68882 | Mitotic Anaphase | 7.174892e-04 | 3.144 |
| R-HSA-8931987 | RUNX1 regulates estrogen receptor mediated transcription | 7.436206e-04 | 3.129 |
| R-HSA-9726840 | SHOC2 M1731 mutant abolishes MRAS complex function | 7.436206e-04 | 3.129 |
| R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 7.477181e-04 | 3.126 |
| R-HSA-9656223 | Signaling by RAF1 mutants | 7.779880e-04 | 3.109 |
| R-HSA-2555396 | Mitotic Metaphase and Anaphase | 7.669808e-04 | 3.115 |
| R-HSA-1500931 | Cell-Cell communication | 8.820670e-04 | 3.054 |
| R-HSA-9759475 | Regulation of CDH11 Expression and Function | 9.059229e-04 | 3.043 |
| R-HSA-69618 | Mitotic Spindle Checkpoint | 9.878803e-04 | 3.005 |
| R-HSA-9768778 | Regulation of NPAS4 mRNA translation | 1.131908e-03 | 2.946 |
| R-HSA-9660537 | Signaling by MRAS-complex mutants | 1.131908e-03 | 2.946 |
| R-HSA-9726842 | Gain-of-function MRAS complexes activate RAF signaling | 1.131908e-03 | 2.946 |
| R-HSA-8943723 | Regulation of PTEN mRNA translation | 1.108826e-03 | 2.955 |
| R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 1.050580e-03 | 2.979 |
| R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 1.257996e-03 | 2.900 |
| R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 1.286651e-03 | 2.891 |
| R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 1.252084e-03 | 2.902 |
| R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 1.555147e-03 | 2.808 |
| R-HSA-9764260 | Regulation of Expression and Function of Type II Classical Cadherins | 1.885526e-03 | 2.725 |
| R-HSA-177243 | Interactions of Rev with host cellular proteins | 1.951227e-03 | 2.710 |
| R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 2.202154e-03 | 2.657 |
| R-HSA-390450 | Folding of actin by CCT/TriC | 2.331812e-03 | 2.632 |
| R-HSA-8948700 | Competing endogenous RNAs (ceRNAs) regulate PTEN translation | 2.345918e-03 | 2.630 |
| R-HSA-2980766 | Nuclear Envelope Breakdown | 2.351656e-03 | 2.629 |
| R-HSA-5683057 | MAPK family signaling cascades | 2.402603e-03 | 2.619 |
| R-HSA-180746 | Nuclear import of Rev protein | 2.622578e-03 | 2.581 |
| R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 2.807556e-03 | 2.552 |
| R-HSA-8951911 | RUNX3 regulates RUNX1-mediated transcription | 2.874845e-03 | 2.541 |
| R-HSA-9617324 | Negative regulation of NMDA receptor-mediated neuronal transmission | 3.126385e-03 | 2.505 |
| R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 3.126385e-03 | 2.505 |
| R-HSA-426486 | Small interfering RNA (siRNA) biogenesis | 3.823135e-03 | 2.418 |
| R-HSA-9759811 | Regulation of CDH11 mRNA translation by microRNAs | 3.193380e-03 | 2.496 |
| R-HSA-9706019 | RHOBTB3 ATPase cycle | 3.193380e-03 | 2.496 |
| R-HSA-6807070 | PTEN Regulation | 3.654119e-03 | 2.437 |
| R-HSA-199920 | CREB phosphorylation | 3.823135e-03 | 2.418 |
| R-HSA-163765 | ChREBP activates metabolic gene expression | 3.193380e-03 | 2.496 |
| R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 3.685793e-03 | 2.433 |
| R-HSA-428540 | Activation of RAC1 | 4.263312e-03 | 2.370 |
| R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 4.769956e-03 | 2.321 |
| R-HSA-399719 | Trafficking of AMPA receptors | 4.841213e-03 | 2.315 |
| R-HSA-2467813 | Separation of Sister Chromatids | 5.127820e-03 | 2.290 |
| R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 5.476015e-03 | 2.262 |
| R-HSA-437239 | Recycling pathway of L1 | 5.793187e-03 | 2.237 |
| R-HSA-9926550 | Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adh... | 5.867866e-03 | 2.232 |
| R-HSA-9018519 | Estrogen-dependent gene expression | 6.105016e-03 | 2.214 |
| R-HSA-9932444 | ATP-dependent chromatin remodelers | 6.511302e-03 | 2.186 |
| R-HSA-9932451 | SWI/SNF chromatin remodelers | 6.511302e-03 | 2.186 |
| R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 6.554607e-03 | 2.183 |
| R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 6.554607e-03 | 2.183 |
| R-HSA-5218920 | VEGFR2 mediated vascular permeability | 7.128107e-03 | 2.147 |
| R-HSA-162582 | Signal Transduction | 7.392484e-03 | 2.131 |
| R-HSA-2559583 | Cellular Senescence | 7.447548e-03 | 2.128 |
| R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 7.566539e-03 | 2.121 |
| R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 7.566539e-03 | 2.121 |
| R-HSA-444257 | RSK activation | 7.659935e-03 | 2.116 |
| R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 7.659935e-03 | 2.116 |
| R-HSA-8934593 | Regulation of RUNX1 Expression and Activity | 7.672345e-03 | 2.115 |
| R-HSA-8941333 | RUNX2 regulates genes involved in differentiation of myeloid cells | 8.763776e-03 | 2.057 |
| R-HSA-4839726 | Chromatin organization | 8.707153e-03 | 2.060 |
| R-HSA-373753 | Nephrin family interactions | 8.632732e-03 | 2.064 |
| R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 8.973898e-03 | 2.047 |
| R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 8.985796e-03 | 2.046 |
| R-HSA-162909 | Host Interactions of HIV factors | 9.134577e-03 | 2.039 |
| R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 9.468309e-03 | 2.024 |
| R-HSA-5693532 | DNA Double-Strand Break Repair | 9.758022e-03 | 2.011 |
| R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 9.937421e-03 | 2.003 |
| R-HSA-9700645 | ALK mutants bind TKIs | 1.028191e-02 | 1.988 |
| R-HSA-418990 | Adherens junctions interactions | 1.008367e-02 | 1.996 |
| R-HSA-211000 | Gene Silencing by RNA | 1.035815e-02 | 1.985 |
| R-HSA-69275 | G2/M Transition | 1.039210e-02 | 1.983 |
| R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 1.095241e-02 | 1.960 |
| R-HSA-1810476 | RIP-mediated NFkB activation via ZBP1 | 1.112397e-02 | 1.954 |
| R-HSA-6804757 | Regulation of TP53 Degradation | 1.131103e-02 | 1.946 |
| R-HSA-445355 | Smooth Muscle Contraction | 1.137558e-02 | 1.944 |
| R-HSA-446728 | Cell junction organization | 1.143888e-02 | 1.942 |
| R-HSA-453274 | Mitotic G2-G2/M phases | 1.156076e-02 | 1.937 |
| R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 1.342389e-02 | 1.872 |
| R-HSA-438066 | Unblocking of NMDA receptors, glutamate binding and activation | 1.222494e-02 | 1.913 |
| R-HSA-442982 | Ras activation upon Ca2+ influx through NMDA receptor | 1.222494e-02 | 1.913 |
| R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 1.281979e-02 | 1.892 |
| R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 1.240819e-02 | 1.906 |
| R-HSA-1606341 | IRF3 mediated activation of type 1 IFN | 1.322988e-02 | 1.878 |
| R-HSA-111932 | CaMK IV-mediated phosphorylation of CREB | 1.342389e-02 | 1.872 |
| R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 1.387730e-02 | 1.858 |
| R-HSA-350054 | Notch-HLH transcription pathway | 1.436652e-02 | 1.843 |
| R-HSA-9839373 | Signaling by TGFBR3 | 1.440243e-02 | 1.842 |
| R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 1.440243e-02 | 1.842 |
| R-HSA-9006936 | Signaling by TGFB family members | 1.459840e-02 | 1.836 |
| R-HSA-5687128 | MAPK6/MAPK4 signaling | 1.470192e-02 | 1.833 |
| R-HSA-380287 | Centrosome maturation | 1.472610e-02 | 1.832 |
| R-HSA-8878171 | Transcriptional regulation by RUNX1 | 1.481613e-02 | 1.829 |
| R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 1.675607e-02 | 1.776 |
| R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 1.586770e-02 | 1.799 |
| R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 1.586770e-02 | 1.799 |
| R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 1.627133e-02 | 1.789 |
| R-HSA-8854518 | AURKA Activation by TPX2 | 1.585536e-02 | 1.800 |
| R-HSA-421270 | Cell-cell junction organization | 1.611469e-02 | 1.793 |
| R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 1.627133e-02 | 1.789 |
| R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 1.735872e-02 | 1.760 |
| R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 1.774837e-02 | 1.751 |
| R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 1.822803e-02 | 1.739 |
| R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 1.822803e-02 | 1.739 |
| R-HSA-8935964 | RUNX1 regulates expression of components of tight junctions | 1.877754e-02 | 1.726 |
| R-HSA-9833576 | CDH11 homotypic and heterotypic interactions | 1.877754e-02 | 1.726 |
| R-HSA-9764302 | Regulation of CDH19 Expression and Function | 1.877754e-02 | 1.726 |
| R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 1.884966e-02 | 1.725 |
| R-HSA-5621575 | CD209 (DC-SIGN) signaling | 1.940594e-02 | 1.712 |
| R-HSA-4839735 | Signaling by AXIN mutants | 2.138812e-02 | 1.670 |
| R-HSA-1855170 | IPs transport between nucleus and cytosol | 2.044040e-02 | 1.690 |
| R-HSA-194441 | Metabolism of non-coding RNA | 2.030694e-02 | 1.692 |
| R-HSA-191859 | snRNP Assembly | 2.030694e-02 | 1.692 |
| R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 1.991912e-02 | 1.701 |
| R-HSA-9006925 | Intracellular signaling by second messengers | 2.191446e-02 | 1.659 |
| R-HSA-2028269 | Signaling by Hippo | 1.961214e-02 | 1.707 |
| R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 2.033016e-02 | 1.692 |
| R-HSA-9768759 | Regulation of NPAS4 gene expression | 1.961214e-02 | 1.707 |
| R-HSA-9833482 | PKR-mediated signaling | 2.195035e-02 | 1.659 |
| R-HSA-8943724 | Regulation of PTEN gene transcription | 2.218746e-02 | 1.654 |
| R-HSA-203927 | MicroRNA (miRNA) biogenesis | 2.232764e-02 | 1.651 |
| R-HSA-9839394 | TGFBR3 expression | 2.232764e-02 | 1.651 |
| R-HSA-9620244 | Long-term potentiation | 2.232764e-02 | 1.651 |
| R-HSA-3214842 | HDMs demethylate histones | 2.232764e-02 | 1.651 |
| R-HSA-5674135 | MAP2K and MAPK activation | 2.263665e-02 | 1.645 |
| R-HSA-168255 | Influenza Infection | 2.296850e-02 | 1.639 |
| R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 2.303982e-02 | 1.638 |
| R-HSA-432142 | Platelet sensitization by LDL | 2.318066e-02 | 1.635 |
| R-HSA-8939256 | RUNX1 regulates transcription of genes involved in WNT signaling | 2.542653e-02 | 1.595 |
| R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 2.553178e-02 | 1.593 |
| R-HSA-5578749 | Transcriptional regulation by small RNAs | 2.606533e-02 | 1.584 |
| R-HSA-8941856 | RUNX3 regulates NOTCH signaling | 2.625638e-02 | 1.581 |
| R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 2.714375e-02 | 1.566 |
| R-HSA-844456 | The NLRP3 inflammasome | 2.714375e-02 | 1.566 |
| R-HSA-68875 | Mitotic Prophase | 2.741215e-02 | 1.562 |
| R-HSA-9909620 | Regulation of PD-L1(CD274) translation | 3.151324e-02 | 1.502 |
| R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 3.151324e-02 | 1.502 |
| R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 3.151324e-02 | 1.502 |
| R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 3.151324e-02 | 1.502 |
| R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 3.151324e-02 | 1.502 |
| R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 3.151324e-02 | 1.502 |
| R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 2.858367e-02 | 1.544 |
| R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 2.858367e-02 | 1.544 |
| R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 2.939461e-02 | 1.532 |
| R-HSA-2426168 | Activation of gene expression by SREBF (SREBP) | 2.858367e-02 | 1.544 |
| R-HSA-6804759 | Regulation of TP53 Activity through Association with Co-factors | 3.173680e-02 | 1.498 |
| R-HSA-6804754 | Regulation of TP53 Expression | 3.193862e-02 | 1.496 |
| R-HSA-1169408 | ISG15 antiviral mechanism | 3.265591e-02 | 1.486 |
| R-HSA-774815 | Nucleosome assembly | 3.360533e-02 | 1.474 |
| R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 3.360533e-02 | 1.474 |
| R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 3.360533e-02 | 1.474 |
| R-HSA-3247509 | Chromatin modifying enzymes | 3.444097e-02 | 1.463 |
| R-HSA-1257604 | PIP3 activates AKT signaling | 3.544648e-02 | 1.450 |
| R-HSA-180910 | Vpr-mediated nuclear import of PICs | 3.570151e-02 | 1.447 |
| R-HSA-438064 | Post NMDA receptor activation events | 3.850979e-02 | 1.414 |
| R-HSA-9764561 | Regulation of CDH1 Function | 3.996274e-02 | 1.398 |
| R-HSA-8939246 | RUNX1 regulates transcription of genes involved in differentiation of myeloid ce... | 4.201213e-02 | 1.377 |
| R-HSA-9828211 | Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation | 4.201213e-02 | 1.377 |
| R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 4.456616e-02 | 1.351 |
| R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 4.608874e-02 | 1.336 |
| R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 4.361964e-02 | 1.360 |
| R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 4.361964e-02 | 1.360 |
| R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 4.737691e-02 | 1.324 |
| R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 4.714573e-02 | 1.327 |
| R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 4.669945e-02 | 1.331 |
| R-HSA-164940 | Nef mediated downregulation of MHC class I complex cell surface expression | 4.201213e-02 | 1.377 |
| R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 4.612488e-02 | 1.336 |
| R-HSA-212676 | Dopamine Neurotransmitter Release Cycle | 4.714573e-02 | 1.327 |
| R-HSA-1280215 | Cytokine Signaling in Immune system | 4.321178e-02 | 1.364 |
| R-HSA-5673001 | RAF/MAP kinase cascade | 4.389486e-02 | 1.358 |
| R-HSA-69481 | G2/M Checkpoints | 4.243349e-02 | 1.372 |
| R-HSA-9705683 | SARS-CoV-2-host interactions | 4.340122e-02 | 1.362 |
| R-HSA-9008059 | Interleukin-37 signaling | 4.134939e-02 | 1.384 |
| R-HSA-9659379 | Sensory processing of sound | 4.317024e-02 | 1.365 |
| R-HSA-187042 | TRKA activation by NGF | 4.771444e-02 | 1.321 |
| R-HSA-9022538 | Loss of MECP2 binding ability to 5mC-DNA | 4.771444e-02 | 1.321 |
| R-HSA-9636249 | Inhibition of nitric oxide production | 4.771444e-02 | 1.321 |
| R-HSA-9766229 | Degradation of CDH1 | 4.771862e-02 | 1.321 |
| R-HSA-202433 | Generation of second messenger molecules | 4.774714e-02 | 1.321 |
| R-HSA-176033 | Interactions of Vpr with host cellular proteins | 4.774714e-02 | 1.321 |
| R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 4.837218e-02 | 1.315 |
| R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 5.033455e-02 | 1.298 |
| R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 5.180010e-02 | 1.286 |
| R-HSA-170984 | ARMS-mediated activation | 5.190250e-02 | 1.285 |
| R-HSA-2025928 | Calcineurin activates NFAT | 5.190250e-02 | 1.285 |
| R-HSA-169893 | Prolonged ERK activation events | 5.191860e-02 | 1.285 |
| R-HSA-8853884 | Transcriptional Regulation by VENTX | 5.227303e-02 | 1.282 |
| R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 5.227303e-02 | 1.282 |
| R-HSA-912526 | Interleukin receptor SHC signaling | 5.321541e-02 | 1.274 |
| R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 5.321541e-02 | 1.274 |
| R-HSA-200425 | Carnitine shuttle | 5.321541e-02 | 1.274 |
| R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 5.321541e-02 | 1.274 |
| R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 5.506536e-02 | 1.259 |
| R-HSA-5684996 | MAPK1/MAPK3 signaling | 5.525054e-02 | 1.258 |
| R-HSA-9669937 | Drug resistance of KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9700649 | Drug resistance of ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9616334 | Defective Base Excision Repair Associated with NEIL1 | 6.690094e-02 | 1.175 |
| R-HSA-9669921 | KIT mutants bind TKIs | 6.690094e-02 | 1.175 |
| R-HSA-9723907 | Loss of Function of TP53 in Cancer | 6.690094e-02 | 1.175 |
| R-HSA-9669926 | Nilotinib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9669917 | Imatinib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9669914 | Dasatinib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-5467333 | APC truncation mutants are not K63 polyubiquitinated | 6.690094e-02 | 1.175 |
| R-HSA-9669936 | Sorafenib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-5467345 | Deletions in the AXIN1 gene destabilize the destruction complex | 6.690094e-02 | 1.175 |
| R-HSA-9717329 | lorlatinib-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9717319 | brigatinib-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9717326 | crizotinib-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9717264 | ASP-3026-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9669924 | Masitinib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9717323 | ceritinib-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9669934 | Sunitinib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9717301 | NVP-TAE684-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9723905 | Loss of function of TP53 in cancer due to loss of tetramerization ability | 6.690094e-02 | 1.175 |
| R-HSA-9717316 | alectinib-resistant ALK mutants | 6.690094e-02 | 1.175 |
| R-HSA-9669929 | Regorafenib-resistant KIT mutants | 6.690094e-02 | 1.175 |
| R-HSA-9705677 | SARS-CoV-2 targets PDZ proteins in cell-cell junction | 6.571213e-02 | 1.182 |
| R-HSA-9707587 | Regulation of HMOX1 expression and activity | 6.571213e-02 | 1.182 |
| R-HSA-9013957 | TLR3-mediated TICAM1-dependent programmed cell death | 6.571213e-02 | 1.182 |
| R-HSA-165181 | Inhibition of TSC complex formation by PKB | 6.571213e-02 | 1.182 |
| R-HSA-2468052 | Establishment of Sister Chromatid Cohesion | 6.280729e-02 | 1.202 |
| R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 5.971788e-02 | 1.224 |
| R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 6.665201e-02 | 1.176 |
| R-HSA-9762292 | Regulation of CDH11 function | 6.280729e-02 | 1.202 |
| R-HSA-5693537 | Resolution of D-Loop Structures | 6.226055e-02 | 1.206 |
| R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 5.654199e-02 | 1.248 |
| R-HSA-6794362 | Protein-protein interactions at synapses | 6.296217e-02 | 1.201 |
| R-HSA-5628897 | TP53 Regulates Metabolic Genes | 6.637550e-02 | 1.178 |
| R-HSA-6784531 | tRNA processing in the nucleus | 5.815083e-02 | 1.235 |
| R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 6.670823e-02 | 1.176 |
| R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 6.113035e-02 | 1.214 |
| R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 5.654199e-02 | 1.248 |
| R-HSA-193670 | p75NTR negatively regulates cell cycle via SC1 | 6.571213e-02 | 1.182 |
| R-HSA-9609736 | Assembly and cell surface presentation of NMDA receptors | 5.705952e-02 | 1.244 |
| R-HSA-194138 | Signaling by VEGF | 6.762525e-02 | 1.170 |
| R-HSA-9768919 | NPAS4 regulates expression of target genes | 6.830822e-02 | 1.166 |
| R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 6.847356e-02 | 1.164 |
| R-HSA-72689 | Formation of a pool of free 40S subunits | 6.955198e-02 | 1.158 |
| R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 6.968741e-02 | 1.157 |
| R-HSA-3134963 | DEx/H-box helicases activate type I IFN and inflammatory cytokines production | 8.556434e-02 | 1.068 |
| R-HSA-8941284 | RUNX2 regulates chondrocyte maturation | 8.556434e-02 | 1.068 |
| R-HSA-9673768 | Signaling by membrane-tethered fusions of PDGFRA or PDGFRB | 8.556434e-02 | 1.068 |
| R-HSA-210990 | PECAM1 interactions | 7.467717e-02 | 1.127 |
| R-HSA-8941332 | RUNX2 regulates genes involved in cell migration | 7.467717e-02 | 1.127 |
| R-HSA-4839744 | Signaling by APC mutants | 7.467717e-02 | 1.127 |
| R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 7.467717e-02 | 1.127 |
| R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 7.467717e-02 | 1.127 |
| R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 7.467717e-02 | 1.127 |
| R-HSA-9824878 | Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 | 8.745620e-02 | 1.058 |
| R-HSA-5339716 | Signaling by GSK3beta mutants | 8.745620e-02 | 1.058 |
| R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 8.494900e-02 | 1.071 |
| R-HSA-72649 | Translation initiation complex formation | 7.013940e-02 | 1.154 |
| R-HSA-72702 | Ribosomal scanning and start codon recognition | 8.064471e-02 | 1.093 |
| R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 8.608423e-02 | 1.065 |
| R-HSA-8878159 | Transcriptional regulation by RUNX3 | 7.728068e-02 | 1.112 |
| R-HSA-72613 | Eukaryotic Translation Initiation | 7.310650e-02 | 1.136 |
| R-HSA-72737 | Cap-dependent Translation Initiation | 7.310650e-02 | 1.136 |
| R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 8.745620e-02 | 1.058 |
| R-HSA-525793 | Myogenesis | 7.401470e-02 | 1.131 |
| R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 7.765367e-02 | 1.110 |
| R-HSA-5693606 | DNA Double Strand Break Response | 8.095615e-02 | 1.092 |
| R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 8.622875e-02 | 1.064 |
| R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 8.745620e-02 | 1.058 |
| R-HSA-3928664 | Ephrin signaling | 7.765367e-02 | 1.110 |
| R-HSA-9663891 | Selective autophagy | 7.900138e-02 | 1.102 |
| R-HSA-174577 | Activation of C3 and C5 | 8.556434e-02 | 1.068 |
| R-HSA-202403 | TCR signaling | 8.698050e-02 | 1.061 |
| R-HSA-187037 | Signaling by NTRK1 (TRKA) | 7.751945e-02 | 1.111 |
| R-HSA-447038 | NrCAM interactions | 8.556434e-02 | 1.068 |
| R-HSA-4839748 | Signaling by AMER1 mutants | 8.745620e-02 | 1.058 |
| R-HSA-181429 | Serotonin Neurotransmitter Release Cycle | 7.765367e-02 | 1.110 |
| R-HSA-73894 | DNA Repair | 8.203330e-02 | 1.086 |
| R-HSA-373760 | L1CAM interactions | 7.310650e-02 | 1.136 |
| R-HSA-9675108 | Nervous system development | 8.680631e-02 | 1.061 |
| R-HSA-9854909 | Regulation of MITF-M dependent genes involved in invasion | 8.556434e-02 | 1.068 |
| R-HSA-418359 | Reduction of cytosolic Ca++ levels | 8.745620e-02 | 1.058 |
| R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 8.718585e-02 | 1.060 |
| R-HSA-2559585 | Oncogene Induced Senescence | 7.468446e-02 | 1.127 |
| R-HSA-9692914 | SARS-CoV-1-host interactions | 7.162074e-02 | 1.145 |
| R-HSA-69205 | G1/S-Specific Transcription | 8.138760e-02 | 1.089 |
| R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 7.401470e-02 | 1.131 |
| R-HSA-446652 | Interleukin-1 family signaling | 8.821197e-02 | 1.054 |
| R-HSA-1632852 | Macroautophagy | 8.840376e-02 | 1.054 |
| R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 9.000396e-02 | 1.046 |
| R-HSA-622312 | Inflammasomes | 9.000396e-02 | 1.046 |
| R-HSA-397014 | Muscle contraction | 9.042934e-02 | 1.044 |
| R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 9.203295e-02 | 1.036 |
| R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 9.256808e-02 | 1.034 |
| R-HSA-449147 | Signaling by Interleukins | 9.303727e-02 | 1.031 |
| R-HSA-1483249 | Inositol phosphate metabolism | 9.537830e-02 | 1.021 |
| R-HSA-8856688 | Golgi-to-ER retrograde transport | 9.601173e-02 | 1.018 |
| R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 9.738452e-02 | 1.012 |
| R-HSA-389356 | Co-stimulation by CD28 | 9.794695e-02 | 1.009 |
| R-HSA-376176 | Signaling by ROBO receptors | 9.796916e-02 | 1.009 |
| R-HSA-157118 | Signaling by NOTCH | 9.945342e-02 | 1.002 |
| R-HSA-2132295 | MHC class II antigen presentation | 1.000881e-01 | 1.000 |
| R-HSA-198323 | AKT phosphorylates targets in the cytosol | 1.010834e-01 | 0.995 |
| R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 1.010834e-01 | 0.995 |
| R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 1.010834e-01 | 0.995 |
| R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 1.010834e-01 | 0.995 |
| R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 1.010834e-01 | 0.995 |
| R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 1.010834e-01 | 0.995 |
| R-HSA-8866427 | VLDLR internalisation and degradation | 1.010834e-01 | 0.995 |
| R-HSA-9005895 | Pervasive developmental disorders | 1.010834e-01 | 0.995 |
| R-HSA-9697154 | Disorders of Nervous System Development | 1.010834e-01 | 0.995 |
| R-HSA-9005891 | Loss of function of MECP2 in Rett syndrome | 1.010834e-01 | 0.995 |
| R-HSA-9931530 | Phosphorylation and nuclear translocation of the CRY:PER:kinase complex | 1.010834e-01 | 0.995 |
| R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 1.026018e-01 | 0.989 |
| R-HSA-114294 | Activation, translocation and oligomerization of BAX | 1.293299e-01 | 0.888 |
| R-HSA-211728 | Regulation of PAK-2p34 activity by PS-GAP/RHG10 | 1.293299e-01 | 0.888 |
| R-HSA-9663199 | Defective DNA double strand break response due to BRCA1 loss of function | 1.293299e-01 | 0.888 |
| R-HSA-9763198 | Impaired BRCA2 binding to SEM1 (DSS1) | 1.293299e-01 | 0.888 |
| R-HSA-6791461 | RPIA deficiency: failed conversion of RU5P to R5P | 1.293299e-01 | 0.888 |
| R-HSA-5659996 | RPIA deficiency: failed conversion of R5P to RU5P | 1.293299e-01 | 0.888 |
| R-HSA-9692912 | SARS-CoV-1 targets PDZ proteins in cell-cell junction | 1.293299e-01 | 0.888 |
| R-HSA-9709275 | Impaired BRCA2 translocation to the nucleus | 1.293299e-01 | 0.888 |
| R-HSA-9699150 | Defective DNA double strand break response due to BARD1 loss of function | 1.293299e-01 | 0.888 |
| R-HSA-5602566 | TICAM1 deficiency - HSE | 1.293299e-01 | 0.888 |
| R-HSA-8941855 | RUNX3 regulates CDKN1A transcription | 1.069429e-01 | 0.971 |
| R-HSA-187706 | Signalling to p38 via RIT and RIN | 1.069429e-01 | 0.971 |
| R-HSA-8951671 | RUNX3 regulates YAP1-mediated transcription | 1.295550e-01 | 0.888 |
| R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 1.154944e-01 | 0.937 |
| R-HSA-177504 | Retrograde neurotrophin signalling | 1.306224e-01 | 0.884 |
| R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 1.369212e-01 | 0.864 |
| R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 1.196748e-01 | 0.922 |
| R-HSA-6794361 | Neurexins and neuroligins | 1.269996e-01 | 0.896 |
| R-HSA-5693538 | Homology Directed Repair | 1.337463e-01 | 0.874 |
| R-HSA-201556 | Signaling by ALK | 1.034257e-01 | 0.985 |
| R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 1.199745e-01 | 0.921 |
| R-HSA-913531 | Interferon Signaling | 1.082731e-01 | 0.965 |
| R-HSA-5674499 | Negative feedback regulation of MAPK pathway | 1.069429e-01 | 0.971 |
| R-HSA-1221632 | Meiotic synapsis | 1.348750e-01 | 0.870 |
| R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 1.185819e-01 | 0.926 |
| R-HSA-8964038 | LDL clearance | 1.318387e-01 | 0.880 |
| R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 1.325903e-01 | 0.877 |
| R-HSA-2032785 | YAP1- and WWTR1 (TAZ)-stimulated gene expression | 1.306224e-01 | 0.884 |
| R-HSA-5675221 | Negative regulation of MAPK pathway | 1.282465e-01 | 0.892 |
| R-HSA-169131 | Inhibition of PKR | 1.293299e-01 | 0.888 |
| R-HSA-434313 | Intracellular metabolism of fatty acids regulates insulin secretion | 1.295550e-01 | 0.888 |
| R-HSA-264642 | Acetylcholine Neurotransmitter Release Cycle | 1.085984e-01 | 0.964 |
| R-HSA-198753 | ERK/MAPK targets | 1.085984e-01 | 0.964 |
| R-HSA-5689880 | Ub-specific processing proteases | 1.251176e-01 | 0.903 |
| R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 1.318387e-01 | 0.880 |
| R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 1.084823e-01 | 0.965 |
| R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 1.267912e-01 | 0.897 |
| R-HSA-166520 | Signaling by NTRKs | 1.201918e-01 | 0.920 |
| R-HSA-111996 | Ca-dependent events | 1.371055e-01 | 0.863 |
| R-HSA-9033500 | TYSND1 cleaves peroxisomal proteins | 1.069429e-01 | 0.971 |
| R-HSA-936837 | Ion transport by P-type ATPases | 1.313828e-01 | 0.881 |
| R-HSA-176187 | Activation of ATR in response to replication stress | 1.369212e-01 | 0.864 |
| R-HSA-210991 | Basigin interactions | 1.085984e-01 | 0.964 |
| R-HSA-389359 | CD28 dependent Vav1 pathway | 1.154944e-01 | 0.937 |
| R-HSA-73762 | RNA Polymerase I Transcription Initiation | 1.371055e-01 | 0.863 |
| R-HSA-381038 | XBP1(S) activates chaperone genes | 1.287725e-01 | 0.890 |
| R-HSA-156902 | Peptide chain elongation | 1.413116e-01 | 0.850 |
| R-HSA-162906 | HIV Infection | 1.426240e-01 | 0.846 |
| R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 1.429844e-01 | 0.845 |
| R-HSA-166166 | MyD88-independent TLR4 cascade | 1.460778e-01 | 0.835 |
| R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 1.460778e-01 | 0.835 |
| R-HSA-418885 | DCC mediated attractive signaling | 1.463996e-01 | 0.834 |
| R-HSA-196299 | Beta-catenin phosphorylation cascade | 1.463996e-01 | 0.834 |
| R-HSA-168927 | TICAM1, RIP1-mediated IKK complex recruitment | 1.463996e-01 | 0.834 |
| R-HSA-3270619 | IRF3-mediated induction of type I IFN | 1.463996e-01 | 0.834 |
| R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 1.463996e-01 | 0.834 |
| R-HSA-9701898 | STAT3 nuclear events downstream of ALK signaling | 1.463996e-01 | 0.834 |
| R-HSA-9823739 | Formation of the anterior neural plate | 1.463996e-01 | 0.834 |
| R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 1.473960e-01 | 0.832 |
| R-HSA-9818027 | NFE2L2 regulating anti-oxidant/detoxification enzymes | 1.473960e-01 | 0.832 |
| R-HSA-73864 | RNA Polymerase I Transcription | 1.475722e-01 | 0.831 |
| R-HSA-9669935 | Signaling by juxtamembrane domain KIT mutants | 1.875855e-01 | 0.727 |
| R-HSA-9680187 | Signaling by extracellular domain mutants of KIT | 1.875855e-01 | 0.727 |
| R-HSA-5674404 | PTEN Loss of Function in Cancer | 1.875855e-01 | 0.727 |
| R-HSA-5603027 | IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (E... | 1.875855e-01 | 0.727 |
| R-HSA-9669933 | Signaling by kinase domain mutants of KIT | 1.875855e-01 | 0.727 |
| R-HSA-5619050 | Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tu... | 1.875855e-01 | 0.727 |
| R-HSA-5602636 | IKBKB deficiency causes SCID | 1.875855e-01 | 0.727 |
| R-HSA-5602571 | TRAF3 deficiency - HSE | 1.875855e-01 | 0.727 |
| R-HSA-5619109 | Defective SLC6A2 causes orthostatic intolerance (OI) | 1.875855e-01 | 0.727 |
| R-HSA-187015 | Activation of TRKA receptors | 1.531405e-01 | 0.815 |
| R-HSA-8948747 | Regulation of PTEN localization | 1.531405e-01 | 0.815 |
| R-HSA-418886 | Netrin mediated repulsion signals | 1.531405e-01 | 0.815 |
| R-HSA-2562578 | TRIF-mediated programmed cell death | 1.531405e-01 | 0.815 |
| R-HSA-9732724 | IFNG signaling activates MAPKs | 1.531405e-01 | 0.815 |
| R-HSA-9632974 | NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis | 1.531405e-01 | 0.815 |
| R-HSA-446107 | Type I hemidesmosome assembly | 1.774680e-01 | 0.751 |
| R-HSA-9613354 | Lipophagy | 2.023331e-01 | 0.694 |
| R-HSA-429947 | Deadenylation of mRNA | 1.569176e-01 | 0.804 |
| R-HSA-416993 | Trafficking of GluR2-containing AMPA receptors | 2.146455e-01 | 0.668 |
| R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 1.581996e-01 | 0.801 |
| R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 1.581996e-01 | 0.801 |
| R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 2.260630e-01 | 0.646 |
| R-HSA-3214815 | HDACs deacetylate histones | 1.513217e-01 | 0.820 |
| R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 2.036671e-01 | 0.691 |
| R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 1.973286e-01 | 0.705 |
| R-HSA-6807878 | COPI-mediated anterograde transport | 2.126631e-01 | 0.672 |
| R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 2.079187e-01 | 0.682 |
| R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 1.695374e-01 | 0.771 |
| R-HSA-6798695 | Neutrophil degranulation | 1.693465e-01 | 0.771 |
| R-HSA-9948299 | Ribosome-associated quality control | 1.935954e-01 | 0.713 |
| R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 1.544606e-01 | 0.811 |
| R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 2.116235e-01 | 0.674 |
| R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 1.796288e-01 | 0.746 |
| R-HSA-156711 | Polo-like kinase mediated events | 2.146455e-01 | 0.668 |
| R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 1.974573e-01 | 0.705 |
| R-HSA-390466 | Chaperonin-mediated protein folding | 2.257088e-01 | 0.646 |
| R-HSA-6804760 | Regulation of TP53 Activity through Methylation | 2.146455e-01 | 0.668 |
| R-HSA-9831926 | Nephron development | 2.146455e-01 | 0.668 |
| R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 1.702926e-01 | 0.769 |
| R-HSA-6803204 | TP53 Regulates Transcription of Genes Involved in Cytochrome C Release | 1.974573e-01 | 0.705 |
| R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 2.043538e-01 | 0.690 |
| R-HSA-373752 | Netrin-1 signaling | 1.556482e-01 | 0.808 |
| R-HSA-1839117 | Signaling by cytosolic FGFR1 fusion mutants | 2.146455e-01 | 0.668 |
| R-HSA-176974 | Unwinding of DNA | 2.023331e-01 | 0.694 |
| R-HSA-187687 | Signalling to ERKs | 1.693150e-01 | 0.771 |
| R-HSA-432720 | Lysosome Vesicle Biogenesis | 1.807247e-01 | 0.743 |
| R-HSA-6804114 | TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest | 1.796288e-01 | 0.746 |
| R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 1.581996e-01 | 0.801 |
| R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 1.961719e-01 | 0.707 |
| R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 1.961719e-01 | 0.707 |
| R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 1.961719e-01 | 0.707 |
| R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 1.961719e-01 | 0.707 |
| R-HSA-6803207 | TP53 Regulates Transcription of Caspase Activators and Caspases | 1.627576e-01 | 0.788 |
| R-HSA-1500620 | Meiosis | 2.007572e-01 | 0.697 |
| R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 1.581996e-01 | 0.801 |
| R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 2.063197e-01 | 0.685 |
| R-HSA-9711097 | Cellular response to starvation | 1.682276e-01 | 0.774 |
| R-HSA-212436 | Generic Transcription Pathway | 2.204862e-01 | 0.657 |
| R-HSA-72764 | Eukaryotic Translation Termination | 2.049352e-01 | 0.688 |
| R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 1.961719e-01 | 0.707 |
| R-HSA-69206 | G1/S Transition | 1.794551e-01 | 0.746 |
| R-HSA-5205647 | Mitophagy | 1.581996e-01 | 0.801 |
| R-HSA-9612973 | Autophagy | 1.579080e-01 | 0.802 |
| R-HSA-9839397 | TGFBR3 regulates FGF2 signaling | 1.875855e-01 | 0.727 |
| R-HSA-9636667 | Manipulation of host energy metabolism | 1.875855e-01 | 0.727 |
| R-HSA-210744 | Regulation of gene expression in late stage (branching morphogenesis) pancreatic... | 1.627576e-01 | 0.788 |
| R-HSA-5576892 | Phase 0 - rapid depolarisation | 2.116235e-01 | 0.674 |
| R-HSA-1912422 | Pre-NOTCH Expression and Processing | 1.640612e-01 | 0.785 |
| R-HSA-9613829 | Chaperone Mediated Autophagy | 2.146455e-01 | 0.668 |
| R-HSA-388841 | Regulation of T cell activation by CD28 family | 1.553155e-01 | 0.809 |
| R-HSA-3858494 | Beta-catenin independent WNT signaling | 1.815943e-01 | 0.741 |
| R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 1.796288e-01 | 0.746 |
| R-HSA-156842 | Eukaryotic Translation Elongation | 1.752782e-01 | 0.756 |
| R-HSA-3295583 | TRP channels | 1.835963e-01 | 0.736 |
| R-HSA-5688426 | Deubiquitination | 1.513854e-01 | 0.820 |
| R-HSA-2559580 | Oxidative Stress Induced Senescence | 1.663398e-01 | 0.779 |
| R-HSA-9675135 | Diseases of DNA repair | 1.752223e-01 | 0.756 |
| R-HSA-4086398 | Ca2+ pathway | 2.036671e-01 | 0.691 |
| R-HSA-139915 | Activation of PUMA and translocation to mitochondria | 1.531405e-01 | 0.815 |
| R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 2.205081e-01 | 0.657 |
| R-HSA-9839389 | TGFBR3 regulates TGF-beta signaling | 1.531405e-01 | 0.815 |
| R-HSA-418889 | Caspase activation via Dependence Receptors in the absence of ligand | 2.023331e-01 | 0.694 |
| R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 2.260630e-01 | 0.646 |
| R-HSA-450294 | MAP kinase activation | 2.057187e-01 | 0.687 |
| R-HSA-112043 | PLC beta mediated events | 2.057187e-01 | 0.687 |
| R-HSA-422475 | Axon guidance | 1.525141e-01 | 0.817 |
| R-HSA-352238 | Breakdown of the nuclear lamina | 1.875855e-01 | 0.727 |
| R-HSA-9635644 | Inhibition of membrane repair | 1.875855e-01 | 0.727 |
| R-HSA-9840373 | Cellular response to mitochondrial stress | 2.023331e-01 | 0.694 |
| R-HSA-388844 | Receptor-type tyrosine-protein phosphatases | 1.627576e-01 | 0.788 |
| R-HSA-9675151 | Disorders of Developmental Biology | 1.796288e-01 | 0.746 |
| R-HSA-168638 | NOD1/2 Signaling Pathway | 1.581996e-01 | 0.801 |
| R-HSA-168325 | Viral Messenger RNA Synthesis | 2.057187e-01 | 0.687 |
| R-HSA-69473 | G2/M DNA damage checkpoint | 2.125441e-01 | 0.673 |
| R-HSA-193648 | NRAGE signals death through JNK | 1.598799e-01 | 0.796 |
| R-HSA-2682334 | EPH-Ephrin signaling | 1.752782e-01 | 0.756 |
| R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 1.949426e-01 | 0.710 |
| R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 1.924412e-01 | 0.716 |
| R-HSA-111933 | Calmodulin induced events | 1.807247e-01 | 0.743 |
| R-HSA-9603505 | NTRK3 as a dependence receptor | 1.875855e-01 | 0.727 |
| R-HSA-425986 | Sodium/Proton exchangers | 1.774680e-01 | 0.751 |
| R-HSA-9012546 | Interleukin-18 signaling | 1.774680e-01 | 0.751 |
| R-HSA-111997 | CaM pathway | 1.807247e-01 | 0.743 |
| R-HSA-418360 | Platelet calcium homeostasis | 2.260630e-01 | 0.646 |
| R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 2.036671e-01 | 0.691 |
| R-HSA-8866910 | TFAP2 (AP-2) family regulates transcription of growth factors and their receptor... | 1.796288e-01 | 0.746 |
| R-HSA-9825895 | Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ... | 1.774680e-01 | 0.751 |
| R-HSA-442729 | CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde | 1.774680e-01 | 0.751 |
| R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 2.023331e-01 | 0.694 |
| R-HSA-373755 | Semaphorin interactions | 2.253189e-01 | 0.647 |
| R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 1.598799e-01 | 0.796 |
| R-HSA-381070 | IRE1alpha activates chaperones | 1.681973e-01 | 0.774 |
| R-HSA-381119 | Unfolded Protein Response (UPR) | 1.997324e-01 | 0.700 |
| R-HSA-5578775 | Ion homeostasis | 1.598799e-01 | 0.796 |
| R-HSA-211736 | Stimulation of the cell death response by PAK-2p34 | 2.419466e-01 | 0.616 |
| R-HSA-8854521 | Interaction between PHLDA1 and AURKA | 2.419466e-01 | 0.616 |
| R-HSA-5579016 | Defective UGT1A4 causes hyperbilirubinemia | 2.419466e-01 | 0.616 |
| R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 2.419466e-01 | 0.616 |
| R-HSA-3645790 | TGFBR2 Kinase Domain Mutants in Cancer | 2.419466e-01 | 0.616 |
| R-HSA-5619104 | Defective SLC12A1 causes Bartter syndrome 1 (BS1) | 2.419466e-01 | 0.616 |
| R-HSA-3828062 | Glycogen storage disease type 0 (muscle GYS1) | 2.419466e-01 | 0.616 |
| R-HSA-3814836 | Glycogen storage disease type XV (GYG1) | 2.419466e-01 | 0.616 |
| R-HSA-4755609 | Defective DHDDS causes RP59 | 2.419466e-01 | 0.616 |
| R-HSA-5357609 | Glycogen storage disease type II (GAA) | 2.419466e-01 | 0.616 |
| R-HSA-167021 | PLC-gamma1 signalling | 2.926732e-01 | 0.534 |
| R-HSA-5368598 | Negative regulation of TCF-dependent signaling by DVL-interacting proteins | 2.926732e-01 | 0.534 |
| R-HSA-198745 | Signalling to STAT3 | 2.926732e-01 | 0.534 |
| R-HSA-5660862 | Defective SLC7A7 causes lysinuric protein intolerance (LPI) | 2.926732e-01 | 0.534 |
| R-HSA-5603037 | IRAK4 deficiency (TLR5) | 2.926732e-01 | 0.534 |
| R-HSA-8952158 | RUNX3 regulates BCL2L11 (BIM) transcription | 3.400083e-01 | 0.469 |
| R-HSA-1306955 | GRB7 events in ERBB2 signaling | 3.400083e-01 | 0.469 |
| R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 3.400083e-01 | 0.469 |
| R-HSA-69200 | Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 ... | 3.400083e-01 | 0.469 |
| R-HSA-9014325 | TICAM1,TRAF6-dependent induction of TAK1 complex | 2.275551e-01 | 0.643 |
| R-HSA-2151209 | Activation of PPARGC1A (PGC-1alpha) by phosphorylation | 2.275551e-01 | 0.643 |
| R-HSA-8876493 | InlA-mediated entry of Listeria monocytogenes into host cells | 2.529752e-01 | 0.597 |
| R-HSA-8939247 | RUNX1 regulates transcription of genes involved in interleukin signaling | 3.841782e-01 | 0.415 |
| R-HSA-8939245 | RUNX1 regulates transcription of genes involved in BCR signaling | 3.841782e-01 | 0.415 |
| R-HSA-111463 | SMAC (DIABLO) binds to IAPs | 3.841782e-01 | 0.415 |
| R-HSA-111464 | SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes | 3.841782e-01 | 0.415 |
| R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 3.841782e-01 | 0.415 |
| R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 3.841782e-01 | 0.415 |
| R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 2.326628e-01 | 0.633 |
| R-HSA-8951936 | RUNX3 regulates p14-ARF | 3.038702e-01 | 0.517 |
| R-HSA-111469 | SMAC, XIAP-regulated apoptotic response | 4.253946e-01 | 0.371 |
| R-HSA-187024 | NGF-independant TRKA activation | 4.253946e-01 | 0.371 |
| R-HSA-164525 | Plus-strand DNA synthesis | 4.253946e-01 | 0.371 |
| R-HSA-182218 | Nef Mediated CD8 Down-regulation | 4.253946e-01 | 0.371 |
| R-HSA-8849470 | PTK6 Regulates Cell Cycle | 4.253946e-01 | 0.371 |
| R-HSA-111459 | Activation of caspases through apoptosome-mediated cleavage | 4.253946e-01 | 0.371 |
| R-HSA-8985586 | SLIT2:ROBO1 increases RHOA activity | 4.253946e-01 | 0.371 |
| R-HSA-176417 | Phosphorylation of Emi1 | 4.253946e-01 | 0.371 |
| R-HSA-9022537 | Loss of MECP2 binding ability to the NCoR/SMRT complex | 4.253946e-01 | 0.371 |
| R-HSA-8877330 | RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) | 3.291181e-01 | 0.483 |
| R-HSA-9933947 | Formation of the non-canonical BAF (ncBAF) complex | 3.291181e-01 | 0.483 |
| R-HSA-1433559 | Regulation of KIT signaling | 3.541065e-01 | 0.451 |
| R-HSA-937072 | TRAF6-mediated induction of TAK1 complex within TLR4 complex | 3.787572e-01 | 0.422 |
| R-HSA-6785631 | ERBB2 Regulates Cell Motility | 3.787572e-01 | 0.422 |
| R-HSA-1362300 | Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL... | 4.030035e-01 | 0.395 |
| R-HSA-174411 | Polymerase switching on the C-strand of the telomere | 3.629449e-01 | 0.440 |
| R-HSA-212300 | PRC2 methylates histones and DNA | 3.476970e-01 | 0.459 |
| R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 2.768318e-01 | 0.558 |
| R-HSA-8957275 | Post-translational protein phosphorylation | 2.284656e-01 | 0.641 |
| R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 4.000513e-01 | 0.398 |
| R-HSA-171306 | Packaging Of Telomere Ends | 4.000513e-01 | 0.398 |
| R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 4.500675e-01 | 0.347 |
| R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 2.982351e-01 | 0.525 |
| R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 2.881889e-01 | 0.540 |
| R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 2.455859e-01 | 0.610 |
| R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 2.455859e-01 | 0.610 |
| R-HSA-192823 | Viral mRNA Translation | 2.697778e-01 | 0.569 |
| R-HSA-9615710 | Late endosomal microautophagy | 4.365287e-01 | 0.360 |
| R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 4.365287e-01 | 0.360 |
| R-HSA-8941858 | Regulation of RUNX3 expression and activity | 4.096423e-01 | 0.388 |
| R-HSA-72163 | mRNA Splicing - Major Pathway | 2.289702e-01 | 0.640 |
| R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 3.384917e-01 | 0.470 |
| R-HSA-8948751 | Regulation of PTEN stability and activity | 4.148696e-01 | 0.382 |
| R-HSA-72172 | mRNA Splicing | 2.947854e-01 | 0.530 |
| R-HSA-8878166 | Transcriptional regulation by RUNX2 | 3.186826e-01 | 0.497 |
| R-HSA-5693607 | Processing of DNA double-strand break ends | 2.783532e-01 | 0.555 |
| R-HSA-9646399 | Aggrephagy | 2.289364e-01 | 0.640 |
| R-HSA-9013508 | NOTCH3 Intracellular Domain Regulates Transcription | 4.544554e-01 | 0.343 |
| R-HSA-8941326 | RUNX2 regulates bone development | 3.476970e-01 | 0.459 |
| R-HSA-73886 | Chromosome Maintenance | 3.356002e-01 | 0.474 |
| R-HSA-9013695 | NOTCH4 Intracellular Domain Regulates Transcription | 2.694121e-01 | 0.570 |
| R-HSA-68962 | Activation of the pre-replicative complex | 2.407439e-01 | 0.618 |
| R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 4.345221e-01 | 0.362 |
| R-HSA-5213460 | RIPK1-mediated regulated necrosis | 3.787470e-01 | 0.422 |
| R-HSA-1170546 | Prolactin receptor signaling | 3.541065e-01 | 0.451 |
| R-HSA-6803211 | TP53 Regulates Transcription of Death Receptors and Ligands | 3.541065e-01 | 0.451 |
| R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 3.321735e-01 | 0.479 |
| R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 4.544554e-01 | 0.343 |
| R-HSA-170968 | Frs2-mediated activation | 3.291181e-01 | 0.483 |
| R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 3.158430e-01 | 0.501 |
| R-HSA-8983432 | Interleukin-15 signaling | 3.038702e-01 | 0.517 |
| R-HSA-9842860 | Regulation of endogenous retroelements | 2.613283e-01 | 0.583 |
| R-HSA-5675482 | Regulation of necroptotic cell death | 2.859220e-01 | 0.544 |
| R-HSA-69541 | Stabilization of p53 | 3.942253e-01 | 0.404 |
| R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 4.249769e-01 | 0.372 |
| R-HSA-8866911 | TFAP2 (AP-2) family regulates transcription of cell cycle factors | 3.400083e-01 | 0.469 |
| R-HSA-191650 | Regulation of gap junction activity | 3.400083e-01 | 0.469 |
| R-HSA-68884 | Mitotic Telophase/Cytokinesis | 2.784541e-01 | 0.555 |
| R-HSA-418890 | Role of second messengers in netrin-1 signaling | 3.038702e-01 | 0.517 |
| R-HSA-174430 | Telomere C-strand synthesis initiation | 3.787572e-01 | 0.422 |
| R-HSA-982772 | Growth hormone receptor signaling | 3.254938e-01 | 0.487 |
| R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 3.476970e-01 | 0.459 |
| R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 4.179650e-01 | 0.379 |
| R-HSA-451927 | Interleukin-2 family signaling | 2.289364e-01 | 0.640 |
| R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 2.982351e-01 | 0.525 |
| R-HSA-6783310 | Fanconi Anemia Pathway | 3.068549e-01 | 0.513 |
| R-HSA-9754189 | Germ layer formation at gastrulation | 2.326628e-01 | 0.633 |
| R-HSA-9758274 | Regulation of NF-kappa B signaling | 4.030035e-01 | 0.395 |
| R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 3.607482e-01 | 0.443 |
| R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 3.607482e-01 | 0.443 |
| R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 3.252885e-01 | 0.488 |
| R-HSA-9851151 | MDK and PTN in ALK signaling | 3.400083e-01 | 0.469 |
| R-HSA-9609523 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane | 2.509377e-01 | 0.600 |
| R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 2.735223e-01 | 0.563 |
| R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 4.148696e-01 | 0.382 |
| R-HSA-199977 | ER to Golgi Anterograde Transport | 3.582331e-01 | 0.446 |
| R-HSA-428359 | Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RN... | 2.275551e-01 | 0.643 |
| R-HSA-9832991 | Formation of the posterior neural plate | 2.529752e-01 | 0.597 |
| R-HSA-165158 | Activation of AKT2 | 3.841782e-01 | 0.415 |
| R-HSA-9933387 | RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression | 2.407439e-01 | 0.618 |
| R-HSA-430039 | mRNA decay by 5' to 3' exoribonuclease | 4.267892e-01 | 0.370 |
| R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 3.321735e-01 | 0.479 |
| R-HSA-9007101 | Rab regulation of trafficking | 4.219394e-01 | 0.375 |
| R-HSA-1358803 | Downregulation of ERBB2:ERBB3 signaling | 3.038702e-01 | 0.517 |
| R-HSA-4791275 | Signaling by WNT in cancer | 2.707041e-01 | 0.568 |
| R-HSA-1482801 | Acyl chain remodelling of PS | 3.629449e-01 | 0.440 |
| R-HSA-8964043 | Plasma lipoprotein clearance | 3.942253e-01 | 0.404 |
| R-HSA-73857 | RNA Polymerase II Transcription | 3.901999e-01 | 0.409 |
| R-HSA-74160 | Gene expression (Transcription) | 3.640784e-01 | 0.439 |
| R-HSA-199991 | Membrane Trafficking | 2.608087e-01 | 0.584 |
| R-HSA-9692913 | SARS-CoV-1-mediated effects on programmed cell death | 3.400083e-01 | 0.469 |
| R-HSA-69895 | Transcriptional activation of cell cycle inhibitor p21 | 3.400083e-01 | 0.469 |
| R-HSA-69560 | Transcriptional activation of p53 responsive genes | 3.400083e-01 | 0.469 |
| R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 3.841782e-01 | 0.415 |
| R-HSA-110362 | POLB-Dependent Long Patch Base Excision Repair | 2.784541e-01 | 0.555 |
| R-HSA-5250992 | Toxicity of botulinum toxin type E (botE) | 4.253946e-01 | 0.371 |
| R-HSA-975163 | IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation | 3.541065e-01 | 0.451 |
| R-HSA-77595 | Processing of Intronless Pre-mRNAs | 4.267892e-01 | 0.370 |
| R-HSA-429914 | Deadenylation-dependent mRNA decay | 3.208836e-01 | 0.494 |
| R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 2.606448e-01 | 0.584 |
| R-HSA-165159 | MTOR signalling | 2.672593e-01 | 0.573 |
| R-HSA-199992 | trans-Golgi Network Vesicle Budding | 3.199744e-01 | 0.495 |
| R-HSA-1266695 | Interleukin-7 signaling | 3.629449e-01 | 0.440 |
| R-HSA-69615 | G1/S DNA Damage Checkpoints | 3.692997e-01 | 0.433 |
| R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 3.660907e-01 | 0.436 |
| R-HSA-391251 | Protein folding | 2.787211e-01 | 0.555 |
| R-HSA-162587 | HIV Life Cycle | 3.303904e-01 | 0.481 |
| R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 4.000513e-01 | 0.398 |
| R-HSA-453279 | Mitotic G1 phase and G1/S transition | 3.504035e-01 | 0.455 |
| R-HSA-5218859 | Regulated Necrosis | 2.768318e-01 | 0.558 |
| R-HSA-9020702 | Interleukin-1 signaling | 3.731884e-01 | 0.428 |
| R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 3.309732e-01 | 0.480 |
| R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 2.725835e-01 | 0.565 |
| R-HSA-6804116 | TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest | 4.030035e-01 | 0.395 |
| R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 3.199744e-01 | 0.495 |
| R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 3.443329e-01 | 0.463 |
| R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 3.443329e-01 | 0.463 |
| R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 3.443329e-01 | 0.463 |
| R-HSA-195721 | Signaling by WNT | 2.882050e-01 | 0.540 |
| R-HSA-8985801 | Regulation of cortical dendrite branching | 2.419466e-01 | 0.616 |
| R-HSA-3642278 | Loss of Function of TGFBR2 in Cancer | 2.419466e-01 | 0.616 |
| R-HSA-3249367 | STAT6-mediated induction of chemokines | 2.926732e-01 | 0.534 |
| R-HSA-844623 | The IPAF inflammasome | 2.926732e-01 | 0.534 |
| R-HSA-8875513 | MET interacts with TNS proteins | 2.926732e-01 | 0.534 |
| R-HSA-211163 | AKT-mediated inactivation of FOXO1A | 3.400083e-01 | 0.469 |
| R-HSA-5140745 | WNT5A-dependent internalization of FZD2, FZD5 and ROR2 | 2.275551e-01 | 0.643 |
| R-HSA-877312 | Regulation of IFNG signaling | 3.038702e-01 | 0.517 |
| R-HSA-111457 | Release of apoptotic factors from the mitochondria | 4.253946e-01 | 0.371 |
| R-HSA-6791465 | Pentose phosphate pathway disease | 4.253946e-01 | 0.371 |
| R-HSA-5603029 | IkBA variant leads to EDA-ID | 4.253946e-01 | 0.371 |
| R-HSA-109703 | PKB-mediated events | 4.253946e-01 | 0.371 |
| R-HSA-165160 | PDE3B signalling | 4.253946e-01 | 0.371 |
| R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 4.253946e-01 | 0.371 |
| R-HSA-68689 | CDC6 association with the ORC:origin complex | 4.253946e-01 | 0.371 |
| R-HSA-9816359 | Maternal to zygotic transition (MZT) | 3.526858e-01 | 0.453 |
| R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 3.475582e-01 | 0.459 |
| R-HSA-389948 | Co-inhibition by PD-1 | 3.511436e-01 | 0.455 |
| R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 3.220481e-01 | 0.492 |
| R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 3.670899e-01 | 0.435 |
| R-HSA-9707616 | Heme signaling | 3.571419e-01 | 0.447 |
| R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 3.202471e-01 | 0.495 |
| R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 3.202471e-01 | 0.495 |
| R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 3.944675e-01 | 0.404 |
| R-HSA-8876384 | Listeria monocytogenes entry into host cells | 2.880306e-01 | 0.541 |
| R-HSA-162599 | Late Phase of HIV Life Cycle | 3.194343e-01 | 0.496 |
| R-HSA-9860931 | Response of endothelial cells to shear stress | 2.783108e-01 | 0.555 |
| R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 3.337052e-01 | 0.477 |
| R-HSA-168256 | Immune System | 3.697299e-01 | 0.432 |
| R-HSA-69242 | S Phase | 3.660907e-01 | 0.436 |
| R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 2.803421e-01 | 0.552 |
| R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 3.632297e-01 | 0.440 |
| R-HSA-1980143 | Signaling by NOTCH1 | 3.641426e-01 | 0.439 |
| R-HSA-9707564 | Cytoprotection by HMOX1 | 4.420621e-01 | 0.355 |
| R-HSA-111448 | Activation of NOXA and translocation to mitochondria | 3.400083e-01 | 0.469 |
| R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 2.529752e-01 | 0.597 |
| R-HSA-8949215 | Mitochondrial calcium ion transport | 2.880306e-01 | 0.541 |
| R-HSA-5099900 | WNT5A-dependent internalization of FZD4 | 4.030035e-01 | 0.395 |
| R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 4.541841e-01 | 0.343 |
| R-HSA-9855142 | Cellular responses to mechanical stimuli | 2.613089e-01 | 0.583 |
| R-HSA-8953854 | Metabolism of RNA | 2.816198e-01 | 0.550 |
| R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 3.460121e-01 | 0.461 |
| R-HSA-6811555 | PI5P Regulates TP53 Acetylation | 3.291181e-01 | 0.483 |
| R-HSA-9861718 | Regulation of pyruvate metabolism | 3.202471e-01 | 0.495 |
| R-HSA-3214841 | PKMTs methylate histone lysines | 4.249769e-01 | 0.372 |
| R-HSA-112315 | Transmission across Chemical Synapses | 4.254909e-01 | 0.371 |
| R-HSA-162592 | Integration of provirus | 2.784541e-01 | 0.555 |
| R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 2.289364e-01 | 0.640 |
| R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 2.289364e-01 | 0.640 |
| R-HSA-983189 | Kinesins | 3.329212e-01 | 0.478 |
| R-HSA-418346 | Platelet homeostasis | 3.043597e-01 | 0.517 |
| R-HSA-8939211 | ESR-mediated signaling | 2.517342e-01 | 0.599 |
| R-HSA-448424 | Interleukin-17 signaling | 2.982351e-01 | 0.525 |
| R-HSA-376172 | DSCAM interactions | 2.419466e-01 | 0.616 |
| R-HSA-8981607 | Intracellular oxygen transport | 2.926732e-01 | 0.534 |
| R-HSA-429593 | Inositol transporters | 3.841782e-01 | 0.415 |
| R-HSA-9026403 | Biosynthesis of DPAn-3-derived 13-series resolvins | 3.841782e-01 | 0.415 |
| R-HSA-195399 | VEGF binds to VEGFR leading to receptor dimerization | 4.253946e-01 | 0.371 |
| R-HSA-5607763 | CLEC7A (Dectin-1) induces NFAT activation | 3.541065e-01 | 0.451 |
| R-HSA-181430 | Norepinephrine Neurotransmitter Release Cycle | 3.442428e-01 | 0.463 |
| R-HSA-1614517 | Sulfide oxidation to sulfate | 4.500675e-01 | 0.347 |
| R-HSA-75105 | Fatty acyl-CoA biosynthesis | 2.982351e-01 | 0.525 |
| R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 3.194343e-01 | 0.496 |
| R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 2.935470e-01 | 0.532 |
| R-HSA-1474165 | Reproduction | 3.152523e-01 | 0.501 |
| R-HSA-1834941 | STING mediated induction of host immune responses | 2.326628e-01 | 0.633 |
| R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 3.199744e-01 | 0.495 |
| R-HSA-9006931 | Signaling by Nuclear Receptors | 2.721693e-01 | 0.565 |
| R-HSA-73854 | RNA Polymerase I Promoter Clearance | 2.307279e-01 | 0.637 |
| R-HSA-112040 | G-protein mediated events | 2.662812e-01 | 0.575 |
| R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 4.087164e-01 | 0.389 |
| R-HSA-110328 | Recognition and association of DNA glycosylase with site containing an affected ... | 3.166851e-01 | 0.499 |
| R-HSA-2408557 | Selenocysteine synthesis | 2.529674e-01 | 0.597 |
| R-HSA-73887 | Death Receptor Signaling | 3.083401e-01 | 0.511 |
| R-HSA-9605308 | Diseases of Base Excision Repair | 4.253946e-01 | 0.371 |
| R-HSA-114452 | Activation of BH3-only proteins | 4.544554e-01 | 0.343 |
| R-HSA-5339562 | Uptake and actions of bacterial toxins | 4.013749e-01 | 0.396 |
| R-HSA-352230 | Amino acid transport across the plasma membrane | 3.208836e-01 | 0.494 |
| R-HSA-9607240 | FLT3 Signaling | 4.249769e-01 | 0.372 |
| R-HSA-844615 | The AIM2 inflammasome | 2.419466e-01 | 0.616 |
| R-HSA-9022702 | MECP2 regulates transcription of neuronal ligands | 2.275551e-01 | 0.643 |
| R-HSA-9927353 | Co-inhibition by BTLA | 3.841782e-01 | 0.415 |
| R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 3.038702e-01 | 0.517 |
| R-HSA-427652 | Sodium-coupled phosphate cotransporters | 4.253946e-01 | 0.371 |
| R-HSA-194313 | VEGF ligand-receptor interactions | 4.253946e-01 | 0.371 |
| R-HSA-9029558 | NR1H2 & NR1H3 regulate gene expression linked to lipogenesis | 3.291181e-01 | 0.483 |
| R-HSA-1855204 | Synthesis of IP3 and IP4 in the cytosol | 2.859220e-01 | 0.544 |
| R-HSA-9945266 | Differentiation of T cells | 4.030035e-01 | 0.395 |
| R-HSA-9942503 | Differentiation of naive CD+ T cells to T helper 1 cells (Th1 cells) | 4.030035e-01 | 0.395 |
| R-HSA-210500 | Glutamate Neurotransmitter Release Cycle | 3.815601e-01 | 0.418 |
| R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 3.089117e-01 | 0.510 |
| R-HSA-9958863 | SLC-mediated transport of amino acids | 4.179650e-01 | 0.379 |
| R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 3.815601e-01 | 0.418 |
| R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 2.392041e-01 | 0.621 |
| R-HSA-196780 | Biotin transport and metabolism | 3.787572e-01 | 0.422 |
| R-HSA-3214858 | RMTs methylate histone arginines | 2.935470e-01 | 0.532 |
| R-HSA-9662834 | CD163 mediating an anti-inflammatory response | 2.529752e-01 | 0.597 |
| R-HSA-881907 | Gastrin-CREB signalling pathway via PKC and MAPK | 2.326628e-01 | 0.633 |
| R-HSA-193704 | p75 NTR receptor-mediated signalling | 2.365312e-01 | 0.626 |
| R-HSA-9645723 | Diseases of programmed cell death | 3.589913e-01 | 0.445 |
| R-HSA-1489509 | DAG and IP3 signaling | 3.068549e-01 | 0.513 |
| R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 2.672593e-01 | 0.573 |
| R-HSA-5250971 | Toxicity of botulinum toxin type C (botC) | 3.841782e-01 | 0.415 |
| R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 2.784541e-01 | 0.555 |
| R-HSA-8983711 | OAS antiviral response | 3.038702e-01 | 0.517 |
| R-HSA-9758919 | Epithelial-Mesenchymal Transition (EMT) during gastrulation | 4.253946e-01 | 0.371 |
| R-HSA-2660826 | Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant | 4.253946e-01 | 0.371 |
| R-HSA-2660825 | Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant | 4.253946e-01 | 0.371 |
| R-HSA-391160 | Signal regulatory protein family interactions | 3.541065e-01 | 0.451 |
| R-HSA-9958790 | SLC-mediated transport of inorganic anions | 3.787470e-01 | 0.422 |
| R-HSA-2408522 | Selenoamino acid metabolism | 3.830404e-01 | 0.417 |
| R-HSA-9637687 | Suppression of phagosomal maturation | 3.815601e-01 | 0.418 |
| R-HSA-70326 | Glucose metabolism | 4.219394e-01 | 0.375 |
| R-HSA-70171 | Glycolysis | 3.635397e-01 | 0.439 |
| R-HSA-9860276 | SLC15A4:TASL-dependent IRF5 activation | 4.253946e-01 | 0.371 |
| R-HSA-9706369 | Negative regulation of FLT3 | 4.030035e-01 | 0.395 |
| R-HSA-8979227 | Triglyceride metabolism | 3.208836e-01 | 0.494 |
| R-HSA-5620971 | Pyroptosis | 4.183845e-01 | 0.378 |
| R-HSA-5210891 | Uptake and function of anthrax toxins | 4.500675e-01 | 0.347 |
| R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 3.977349e-01 | 0.400 |
| R-HSA-9694516 | SARS-CoV-2 Infection | 3.383067e-01 | 0.471 |
| R-HSA-9679506 | SARS-CoV Infections | 2.743629e-01 | 0.562 |
| R-HSA-1912420 | Pre-NOTCH Processing in Golgi | 2.326628e-01 | 0.633 |
| R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 4.000513e-01 | 0.398 |
| R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 2.543178e-01 | 0.595 |
| R-HSA-163560 | Triglyceride catabolism | 3.476970e-01 | 0.459 |
| R-HSA-9678108 | SARS-CoV-1 Infection | 2.749944e-01 | 0.561 |
| R-HSA-9827857 | Specification of primordial germ cells | 4.500675e-01 | 0.347 |
| R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 3.291181e-01 | 0.483 |
| R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 3.853244e-01 | 0.414 |
| R-HSA-9828806 | Maturation of hRSV A proteins | 4.000513e-01 | 0.398 |
| R-HSA-109606 | Intrinsic Pathway for Apoptosis | 4.550059e-01 | 0.342 |
| R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 4.550059e-01 | 0.342 |
| R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 4.553205e-01 | 0.342 |
| R-HSA-379716 | Cytosolic tRNA aminoacylation | 4.553205e-01 | 0.342 |
| R-HSA-73928 | Depyrimidination | 4.553205e-01 | 0.342 |
| R-HSA-110329 | Cleavage of the damaged pyrimidine | 4.553205e-01 | 0.342 |
| R-HSA-8869496 | TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif... | 4.638547e-01 | 0.334 |
| R-HSA-8866423 | VLDL assembly | 4.638547e-01 | 0.334 |
| R-HSA-8964026 | Chylomicron clearance | 4.638547e-01 | 0.334 |
| R-HSA-9645135 | STAT5 Activation | 4.638547e-01 | 0.334 |
| R-HSA-5263617 | Metabolism of ingested MeSeO2H into MeSeH | 4.638547e-01 | 0.334 |
| R-HSA-162585 | Uncoating of the HIV Virion | 4.638547e-01 | 0.334 |
| R-HSA-113507 | E2F-enabled inhibition of pre-replication complex formation | 4.638547e-01 | 0.334 |
| R-HSA-5250981 | Toxicity of botulinum toxin type F (botF) | 4.638547e-01 | 0.334 |
| R-HSA-5250955 | Toxicity of botulinum toxin type D (botD) | 4.638547e-01 | 0.334 |
| R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 4.638547e-01 | 0.334 |
| R-HSA-2980767 | Activation of NIMA Kinases NEK9, NEK6, NEK7 | 4.638547e-01 | 0.334 |
| R-HSA-69478 | G2/M DNA replication checkpoint | 4.638547e-01 | 0.334 |
| R-HSA-447043 | Neurofascin interactions | 4.638547e-01 | 0.334 |
| R-HSA-389542 | NADPH regeneration | 4.638547e-01 | 0.334 |
| R-HSA-164944 | Nef and signal transduction | 4.638547e-01 | 0.334 |
| R-HSA-453276 | Regulation of mitotic cell cycle | 4.661479e-01 | 0.331 |
| R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 4.661479e-01 | 0.331 |
| R-HSA-427413 | NoRC negatively regulates rRNA expression | 4.661479e-01 | 0.331 |
| R-HSA-9710421 | Defective pyroptosis | 4.702934e-01 | 0.328 |
| R-HSA-9637690 | Response of Mtb to phagocytosis | 4.702934e-01 | 0.328 |
| R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 4.721392e-01 | 0.326 |
| R-HSA-5694530 | Cargo concentration in the ER | 4.721392e-01 | 0.326 |
| R-HSA-186763 | Downstream signal transduction | 4.721392e-01 | 0.326 |
| R-HSA-983712 | Ion channel transport | 4.723954e-01 | 0.326 |
| R-HSA-111471 | Apoptotic factor-mediated response | 4.727996e-01 | 0.325 |
| R-HSA-8849932 | Synaptic adhesion-like molecules | 4.727996e-01 | 0.325 |
| R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 4.750842e-01 | 0.323 |
| R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 4.780413e-01 | 0.321 |
| R-HSA-168898 | Toll-like Receptor Cascades | 4.870559e-01 | 0.312 |
| R-HSA-1538133 | G0 and Early G1 | 4.895570e-01 | 0.310 |
| R-HSA-110330 | Recognition and association of DNA glycosylase with site containing an affected ... | 4.895570e-01 | 0.310 |
| R-HSA-69052 | Switching of origins to a post-replicative state | 4.898550e-01 | 0.310 |
| R-HSA-3214847 | HATs acetylate histones | 4.926764e-01 | 0.307 |
| R-HSA-449836 | Other interleukin signaling | 4.949546e-01 | 0.305 |
| R-HSA-9679191 | Potential therapeutics for SARS | 4.961998e-01 | 0.304 |
| R-HSA-2892245 | POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation | 4.997427e-01 | 0.301 |
| R-HSA-8949275 | RUNX3 Regulates Immune Response and Cell Migration | 4.997427e-01 | 0.301 |
| R-HSA-428890 | Role of ABL in ROBO-SLIT signaling | 4.997427e-01 | 0.301 |
| R-HSA-8964046 | VLDL clearance | 4.997427e-01 | 0.301 |
| R-HSA-2470946 | Cohesin Loading onto Chromatin | 4.997427e-01 | 0.301 |
| R-HSA-72731 | Recycling of eIF2:GDP | 4.997427e-01 | 0.301 |
| R-HSA-8964041 | LDL remodeling | 4.997427e-01 | 0.301 |
| R-HSA-167590 | Nef Mediated CD4 Down-regulation | 4.997427e-01 | 0.301 |
| R-HSA-8951430 | RUNX3 regulates WNT signaling | 4.997427e-01 | 0.301 |
| R-HSA-5576890 | Phase 3 - rapid repolarisation | 4.997427e-01 | 0.301 |
| R-HSA-9686347 | Microbial modulation of RIPK1-mediated regulated necrosis | 4.997427e-01 | 0.301 |
| R-HSA-3371599 | Defective HLCS causes multiple carboxylase deficiency | 4.997427e-01 | 0.301 |
| R-HSA-4411364 | Binding of TCF/LEF:CTNNB1 to target gene promoters | 4.997427e-01 | 0.301 |
| R-HSA-426117 | Cation-coupled Chloride cotransporters | 4.997427e-01 | 0.301 |
| R-HSA-447041 | CHL1 interactions | 4.997427e-01 | 0.301 |
| R-HSA-5336415 | Uptake and function of diphtheria toxin | 4.997427e-01 | 0.301 |
| R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 4.997601e-01 | 0.301 |
| R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 4.997601e-01 | 0.301 |
| R-HSA-9013694 | Signaling by NOTCH4 | 5.015807e-01 | 0.300 |
| R-HSA-9755511 | KEAP1-NFE2L2 pathway | 5.043500e-01 | 0.297 |
| R-HSA-1839124 | FGFR1 mutant receptor activation | 5.066885e-01 | 0.295 |
| R-HSA-212165 | Epigenetic regulation of gene expression | 5.074201e-01 | 0.295 |
| R-HSA-5633008 | TP53 Regulates Transcription of Cell Death Genes | 5.132101e-01 | 0.290 |
| R-HSA-112316 | Neuronal System | 5.140913e-01 | 0.289 |
| R-HSA-72165 | mRNA Splicing - Minor Pathway | 5.142249e-01 | 0.289 |
| R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 5.165078e-01 | 0.287 |
| R-HSA-389513 | Co-inhibition by CTLA4 | 5.165078e-01 | 0.287 |
| R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 5.165078e-01 | 0.287 |
| R-HSA-6807004 | Negative regulation of MET activity | 5.165078e-01 | 0.287 |
| R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 5.165078e-01 | 0.287 |
| R-HSA-9823730 | Formation of definitive endoderm | 5.165078e-01 | 0.287 |
| R-HSA-8939902 | Regulation of RUNX2 expression and activity | 5.199762e-01 | 0.284 |
| R-HSA-114608 | Platelet degranulation | 5.213937e-01 | 0.283 |
| R-HSA-9768727 | Regulation of CDH1 posttranslational processing and trafficking to plasma membra... | 5.235154e-01 | 0.281 |
| R-HSA-390522 | Striated Muscle Contraction | 5.235154e-01 | 0.281 |
| R-HSA-5696394 | DNA Damage Recognition in GG-NER | 5.235154e-01 | 0.281 |
| R-HSA-189483 | Heme degradation | 5.235154e-01 | 0.281 |
| R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 5.325819e-01 | 0.274 |
| R-HSA-162589 | Reverse Transcription of HIV RNA | 5.332304e-01 | 0.273 |
| R-HSA-164516 | Minus-strand DNA synthesis | 5.332304e-01 | 0.273 |
| R-HSA-111995 | phospho-PLA2 pathway | 5.332304e-01 | 0.273 |
| R-HSA-196025 | Formation of annular gap junctions | 5.332304e-01 | 0.273 |
| R-HSA-3785653 | Myoclonic epilepsy of Lafora | 5.332304e-01 | 0.273 |
| R-HSA-8939242 | RUNX1 regulates transcription of genes involved in differentiation of keratinocy... | 5.332304e-01 | 0.273 |
| R-HSA-8985947 | Interleukin-9 signaling | 5.332304e-01 | 0.273 |
| R-HSA-190370 | FGFR1b ligand binding and activation | 5.332304e-01 | 0.273 |
| R-HSA-9839383 | TGFBR3 PTM regulation | 5.332304e-01 | 0.273 |
| R-HSA-179409 | APC-Cdc20 mediated degradation of Nek2A | 5.374405e-01 | 0.270 |
| R-HSA-162594 | Early Phase of HIV Life Cycle | 5.374405e-01 | 0.270 |
| R-HSA-167044 | Signalling to RAS | 5.374405e-01 | 0.270 |
| R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 5.374405e-01 | 0.270 |
| R-HSA-9927426 | Developmental Lineage of Mammary Gland Alveolar Cells | 5.400221e-01 | 0.268 |
| R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 5.400221e-01 | 0.268 |
| R-HSA-901042 | Calnexin/calreticulin cycle | 5.400221e-01 | 0.268 |
| R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 5.400221e-01 | 0.268 |
| R-HSA-111885 | Opioid Signalling | 5.423189e-01 | 0.266 |
| R-HSA-9031628 | NGF-stimulated transcription | 5.425541e-01 | 0.266 |
| R-HSA-4086400 | PCP/CE pathway | 5.474455e-01 | 0.262 |
| R-HSA-416482 | G alpha (12/13) signalling events | 5.474455e-01 | 0.262 |
| R-HSA-5621481 | C-type lectin receptors (CLRs) | 5.546766e-01 | 0.256 |
| R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 5.561947e-01 | 0.255 |
| R-HSA-169911 | Regulation of Apoptosis | 5.561947e-01 | 0.255 |
| R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 5.561947e-01 | 0.255 |
| R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 5.561947e-01 | 0.255 |
| R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 5.577392e-01 | 0.254 |
| R-HSA-9671555 | Signaling by PDGFR in disease | 5.577392e-01 | 0.254 |
| R-HSA-1280218 | Adaptive Immune System | 5.593215e-01 | 0.252 |
| R-HSA-1266738 | Developmental Biology | 5.597670e-01 | 0.252 |
| R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 5.632416e-01 | 0.249 |
| R-HSA-5649702 | APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement P... | 5.644784e-01 | 0.248 |
| R-HSA-9020958 | Interleukin-21 signaling | 5.644784e-01 | 0.248 |
| R-HSA-201688 | WNT mediated activation of DVL | 5.644784e-01 | 0.248 |
| R-HSA-198693 | AKT phosphorylates targets in the nucleus | 5.644784e-01 | 0.248 |
| R-HSA-190873 | Gap junction degradation | 5.644784e-01 | 0.248 |
| R-HSA-448706 | Interleukin-1 processing | 5.644784e-01 | 0.248 |
| R-HSA-2465910 | MASTL Facilitates Mitotic Progression | 5.644784e-01 | 0.248 |
| R-HSA-5250968 | Toxicity of botulinum toxin type A (botA) | 5.644784e-01 | 0.248 |
| R-HSA-9619229 | Activation of RAC1 downstream of NMDARs | 5.644784e-01 | 0.248 |
| R-HSA-937042 | IRAK2 mediated activation of TAK1 complex | 5.644784e-01 | 0.248 |
| R-HSA-9013700 | NOTCH4 Activation and Transmission of Signal to the Nucleus | 5.644784e-01 | 0.248 |
| R-HSA-428542 | Regulation of commissural axon pathfinding by SLIT and ROBO | 5.644784e-01 | 0.248 |
| R-HSA-112411 | MAPK1 (ERK2) activation | 5.644784e-01 | 0.248 |
| R-HSA-1433617 | Regulation of signaling by NODAL | 5.644784e-01 | 0.248 |
| R-HSA-450520 | HuR (ELAVL1) binds and stabilizes mRNA | 5.644784e-01 | 0.248 |
| R-HSA-430116 | GP1b-IX-V activation signalling | 5.644784e-01 | 0.248 |
| R-HSA-9762293 | Regulation of CDH11 gene transcription | 5.644784e-01 | 0.248 |
| R-HSA-3323169 | Defects in biotin (Btn) metabolism | 5.644784e-01 | 0.248 |
| R-HSA-8851680 | Butyrophilin (BTN) family interactions | 5.644784e-01 | 0.248 |
| R-HSA-9843745 | Adipogenesis | 5.648622e-01 | 0.248 |
| R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 5.696572e-01 | 0.244 |
| R-HSA-5658442 | Regulation of RAS by GAPs | 5.700105e-01 | 0.244 |
| R-HSA-114604 | GPVI-mediated activation cascade | 5.720215e-01 | 0.243 |
| R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 5.722121e-01 | 0.242 |
| R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 5.722121e-01 | 0.242 |
| R-HSA-9909396 | Circadian clock | 5.733632e-01 | 0.242 |
| R-HSA-72312 | rRNA processing | 5.759102e-01 | 0.240 |
| R-HSA-6803529 | FGFR2 alternative splicing | 5.773950e-01 | 0.239 |
| R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 5.773950e-01 | 0.239 |
| R-HSA-912694 | Regulation of IFNA/IFNB signaling | 5.773950e-01 | 0.239 |
| R-HSA-6803205 | TP53 regulates transcription of several additional cell death genes whose specif... | 5.773950e-01 | 0.239 |
| R-HSA-166208 | mTORC1-mediated signalling | 5.773950e-01 | 0.239 |
| R-HSA-168799 | Neurotoxicity of clostridium toxins | 5.773950e-01 | 0.239 |
| R-HSA-9857377 | Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autopha... | 5.773950e-01 | 0.239 |
| R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 5.814123e-01 | 0.236 |
| R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 5.817927e-01 | 0.235 |
| R-HSA-912446 | Meiotic recombination | 5.833883e-01 | 0.234 |
| R-HSA-5617833 | Cilium Assembly | 5.855586e-01 | 0.232 |
| R-HSA-4641257 | Degradation of AXIN | 5.874928e-01 | 0.231 |
| R-HSA-4641258 | Degradation of DVL | 5.874928e-01 | 0.231 |
| R-HSA-110331 | Cleavage of the damaged purine | 5.874928e-01 | 0.231 |
| R-HSA-5689896 | Ovarian tumor domain proteases | 5.874928e-01 | 0.231 |
| R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 5.899060e-01 | 0.229 |
| R-HSA-173107 | Binding and entry of HIV virion | 5.936362e-01 | 0.226 |
| R-HSA-164843 | 2-LTR circle formation | 5.936362e-01 | 0.226 |
| R-HSA-451308 | Activation of Ca-permeable Kainate Receptor | 5.936362e-01 | 0.226 |
| R-HSA-198203 | PI3K/AKT activation | 5.936362e-01 | 0.226 |
| R-HSA-5689877 | Josephin domain DUBs | 5.936362e-01 | 0.226 |
| R-HSA-6803544 | Ion influx/efflux at host-pathogen interface | 5.936362e-01 | 0.226 |
| R-HSA-9020956 | Interleukin-27 signaling | 5.936362e-01 | 0.226 |
| R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 5.936362e-01 | 0.226 |
| R-HSA-9664873 | Pexophagy | 5.936362e-01 | 0.226 |
| R-HSA-9683686 | Maturation of spike protein | 5.936362e-01 | 0.226 |
| R-HSA-110056 | MAPK3 (ERK1) activation | 5.936362e-01 | 0.226 |
| R-HSA-1300642 | Sperm Motility And Taxes | 5.936362e-01 | 0.226 |
| R-HSA-9627069 | Regulation of the apoptosome activity | 5.936362e-01 | 0.226 |
| R-HSA-111458 | Formation of apoptosome | 5.936362e-01 | 0.226 |
| R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 5.964030e-01 | 0.224 |
| R-HSA-1855167 | Synthesis of pyrophosphates in the cytosol | 5.964030e-01 | 0.224 |
| R-HSA-9018682 | Biosynthesis of maresins | 5.964030e-01 | 0.224 |
| R-HSA-3000170 | Syndecan interactions | 5.964030e-01 | 0.224 |
| R-HSA-400451 | Free fatty acids regulate insulin secretion | 5.964030e-01 | 0.224 |
| R-HSA-68949 | Orc1 removal from chromatin | 5.965223e-01 | 0.224 |
| R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 5.986230e-01 | 0.223 |
| R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 5.986230e-01 | 0.223 |
| R-HSA-69002 | DNA Replication Pre-Initiation | 5.991670e-01 | 0.222 |
| R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 5.996336e-01 | 0.222 |
| R-HSA-452723 | Transcriptional regulation of pluripotent stem cells | 6.026004e-01 | 0.220 |
| R-HSA-73927 | Depurination | 6.026004e-01 | 0.220 |
| R-HSA-9639288 | Amino acids regulate mTORC1 | 6.094060e-01 | 0.215 |
| R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 6.094060e-01 | 0.215 |
| R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 6.094060e-01 | 0.215 |
| R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 6.094060e-01 | 0.215 |
| R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 6.099274e-01 | 0.215 |
| R-HSA-163685 | Integration of energy metabolism | 6.147406e-01 | 0.211 |
| R-HSA-9821993 | Replacement of protamines by nucleosomes in the male pronucleus | 6.147619e-01 | 0.211 |
| R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 6.147619e-01 | 0.211 |
| R-HSA-8863678 | Neurodegenerative Diseases | 6.147619e-01 | 0.211 |
| R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 6.147619e-01 | 0.211 |
| R-HSA-9711123 | Cellular response to chemical stress | 6.151276e-01 | 0.211 |
| R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 6.161697e-01 | 0.210 |
| R-HSA-9931509 | Expression of BMAL (ARNTL), CLOCK, and NPAS2 | 6.173380e-01 | 0.209 |
| R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 6.173380e-01 | 0.209 |
| R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 6.173380e-01 | 0.209 |
| R-HSA-8963888 | Chylomicron assembly | 6.208435e-01 | 0.207 |
| R-HSA-112308 | Presynaptic depolarization and calcium channel opening | 6.208435e-01 | 0.207 |
| R-HSA-9020558 | Interleukin-2 signaling | 6.208435e-01 | 0.207 |
| R-HSA-451306 | Ionotropic activity of kainate receptors | 6.208435e-01 | 0.207 |
| R-HSA-192814 | vRNA Synthesis | 6.208435e-01 | 0.207 |
| R-HSA-210747 | Regulation of gene expression in early pancreatic precursor cells | 6.208435e-01 | 0.207 |
| R-HSA-425381 | Bicarbonate transporters | 6.208435e-01 | 0.207 |
| R-HSA-9645460 | Alpha-protein kinase 1 signaling pathway | 6.208435e-01 | 0.207 |
| R-HSA-427601 | Inorganic anion exchange by SLC26 transporters | 6.208435e-01 | 0.207 |
| R-HSA-5682910 | LGI-ADAM interactions | 6.208435e-01 | 0.207 |
| R-HSA-9026290 | Biosynthesis of DPAn-3-derived maresins | 6.208435e-01 | 0.207 |
| R-HSA-9614399 | Regulation of localization of FOXO transcription factors | 6.208435e-01 | 0.207 |
| R-HSA-933543 | NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 | 6.208435e-01 | 0.207 |
| R-HSA-75205 | Dissolution of Fibrin Clot | 6.208435e-01 | 0.207 |
| R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 6.220336e-01 | 0.206 |
| R-HSA-73929 | Base-Excision Repair, AP Site Formation | 6.220336e-01 | 0.206 |
| R-HSA-9609690 | HCMV Early Events | 6.271281e-01 | 0.203 |
| R-HSA-69202 | Cyclin E associated events during G1/S transition | 6.273706e-01 | 0.202 |
| R-HSA-204005 | COPII-mediated vesicle transport | 6.273706e-01 | 0.202 |
| R-HSA-9670095 | Inhibition of DNA recombination at telomere | 6.317007e-01 | 0.199 |
| R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 6.317007e-01 | 0.199 |
| R-HSA-5260271 | Diseases of Immune System | 6.317007e-01 | 0.199 |
| R-HSA-420029 | Tight junction interactions | 6.324733e-01 | 0.199 |
| R-HSA-70221 | Glycogen breakdown (glycogenolysis) | 6.324733e-01 | 0.199 |
| R-HSA-400685 | Sema4D in semaphorin signaling | 6.324733e-01 | 0.199 |
| R-HSA-9012852 | Signaling by NOTCH3 | 6.344004e-01 | 0.198 |
| R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 6.344004e-01 | 0.198 |
| R-HSA-5632684 | Hedgehog 'on' state | 6.383718e-01 | 0.195 |
| R-HSA-9821002 | Chromatin modifications during the maternal to zygotic transition (MZT) | 6.456850e-01 | 0.190 |
| R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 6.456850e-01 | 0.190 |
| R-HSA-3000497 | Scavenging by Class H Receptors | 6.462307e-01 | 0.190 |
| R-HSA-2514853 | Condensation of Prometaphase Chromosomes | 6.462307e-01 | 0.190 |
| R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 6.462307e-01 | 0.190 |
| R-HSA-75896 | Plasmalogen biosynthesis | 6.462307e-01 | 0.190 |
| R-HSA-209560 | NF-kB is activated and signals survival | 6.462307e-01 | 0.190 |
| R-HSA-168330 | Viral RNP Complexes in the Host Cell Nucleus | 6.462307e-01 | 0.190 |
| R-HSA-111461 | Cytochrome c-mediated apoptotic response | 6.462307e-01 | 0.190 |
| R-HSA-1236977 | Endosomal/Vacuolar pathway | 6.462307e-01 | 0.190 |
| R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 6.465024e-01 | 0.189 |
| R-HSA-75893 | TNF signaling | 6.465024e-01 | 0.189 |
| R-HSA-9703465 | Signaling by FLT3 fusion proteins | 6.495416e-01 | 0.187 |
| R-HSA-5689901 | Metalloprotease DUBs | 6.495416e-01 | 0.187 |
| R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 6.495416e-01 | 0.187 |
| R-HSA-70635 | Urea cycle | 6.495416e-01 | 0.187 |
| R-HSA-70268 | Pyruvate metabolism | 6.526820e-01 | 0.185 |
| R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 6.592887e-01 | 0.181 |
| R-HSA-6811438 | Intra-Golgi traffic | 6.592887e-01 | 0.181 |
| R-HSA-5655302 | Signaling by FGFR1 in disease | 6.592887e-01 | 0.181 |
| R-HSA-442660 | SLC-mediated transport of neurotransmitters | 6.592887e-01 | 0.181 |
| R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 6.597620e-01 | 0.181 |
| R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 6.659736e-01 | 0.177 |
| R-HSA-445095 | Interaction between L1 and Ankyrins | 6.659736e-01 | 0.177 |
| R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 6.659736e-01 | 0.177 |
| R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 6.659736e-01 | 0.177 |
| R-HSA-202427 | Phosphorylation of CD3 and TCR zeta chains | 6.659736e-01 | 0.177 |
| R-HSA-201451 | Signaling by BMP | 6.659736e-01 | 0.177 |
| R-HSA-75109 | Triglyceride biosynthesis | 6.659736e-01 | 0.177 |
| R-HSA-3928663 | EPHA-mediated growth cone collapse | 6.659736e-01 | 0.177 |
| R-HSA-1483213 | Synthesis of PE | 6.659736e-01 | 0.177 |
| R-HSA-193807 | Synthesis of bile acids and bile salts via 27-hydroxycholesterol | 6.659736e-01 | 0.177 |
| R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 6.659736e-01 | 0.177 |
| R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 6.661371e-01 | 0.176 |
| R-HSA-201722 | Formation of the beta-catenin:TCF transactivating complex | 6.699002e-01 | 0.174 |
| R-HSA-2197563 | NOTCH2 intracellular domain regulates transcription | 6.699195e-01 | 0.174 |
| R-HSA-9820865 | Z-decay: degradation of maternal mRNAs by zygotically expressed factors | 6.699195e-01 | 0.174 |
| R-HSA-3000484 | Scavenging by Class F Receptors | 6.699195e-01 | 0.174 |
| R-HSA-8984722 | Interleukin-35 Signalling | 6.699195e-01 | 0.174 |
| R-HSA-2691232 | Constitutive Signaling by NOTCH1 HD Domain Mutants | 6.699195e-01 | 0.174 |
| R-HSA-2691230 | Signaling by NOTCH1 HD Domain Mutants in Cancer | 6.699195e-01 | 0.174 |
| R-HSA-380615 | Serotonin clearance from the synaptic cleft | 6.699195e-01 | 0.174 |
| R-HSA-209543 | p75NTR recruits signalling complexes | 6.699195e-01 | 0.174 |
| R-HSA-9026286 | Biosynthesis of DPAn-3-derived protectins and resolvins | 6.699195e-01 | 0.174 |
| R-HSA-4641265 | Repression of WNT target genes | 6.699195e-01 | 0.174 |
| R-HSA-1679131 | Trafficking and processing of endosomal TLR | 6.699195e-01 | 0.174 |
| R-HSA-937039 | IRAK1 recruits IKK complex | 6.699195e-01 | 0.174 |
| R-HSA-975144 | IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation | 6.699195e-01 | 0.174 |
| R-HSA-1247673 | Erythrocytes take up oxygen and release carbon dioxide | 6.699195e-01 | 0.174 |
| R-HSA-877300 | Interferon gamma signaling | 6.802545e-01 | 0.167 |
| R-HSA-112310 | Neurotransmitter release cycle | 6.811427e-01 | 0.167 |
| R-HSA-202424 | Downstream TCR signaling | 6.811427e-01 | 0.167 |
| R-HSA-73884 | Base Excision Repair | 6.811427e-01 | 0.167 |
| R-HSA-9033241 | Peroxisomal protein import | 6.811916e-01 | 0.167 |
| R-HSA-186712 | Regulation of beta-cell development | 6.811916e-01 | 0.167 |
| R-HSA-167287 | HIV elongation arrest and recovery | 6.817778e-01 | 0.166 |
| R-HSA-167290 | Pausing and recovery of HIV elongation | 6.817778e-01 | 0.166 |
| R-HSA-171319 | Telomere Extension By Telomerase | 6.817778e-01 | 0.166 |
| R-HSA-9757110 | Prednisone ADME | 6.817778e-01 | 0.166 |
| R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 6.829287e-01 | 0.166 |
| R-HSA-1433557 | Signaling by SCF-KIT | 6.853518e-01 | 0.164 |
| R-HSA-8854214 | TBC/RABGAPs | 6.853518e-01 | 0.164 |
| R-HSA-75876 | Synthesis of very long-chain fatty acyl-CoAs | 6.853518e-01 | 0.164 |
| R-HSA-5576891 | Cardiac conduction | 6.880051e-01 | 0.162 |
| R-HSA-5689603 | UCH proteinases | 6.902784e-01 | 0.161 |
| R-HSA-8963901 | Chylomicron remodeling | 6.920234e-01 | 0.160 |
| R-HSA-9661069 | Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) | 6.920234e-01 | 0.160 |
| R-HSA-6788467 | IL-6-type cytokine receptor ligand interactions | 6.920234e-01 | 0.160 |
| R-HSA-1059683 | Interleukin-6 signaling | 6.920234e-01 | 0.160 |
| R-HSA-8949664 | Processing of SMDT1 | 6.920234e-01 | 0.160 |
| R-HSA-9659787 | Aberrant regulation of mitotic G1/S transition in cancer due to RB1 defects | 6.920234e-01 | 0.160 |
| R-HSA-75892 | Platelet Adhesion to exposed collagen | 6.920234e-01 | 0.160 |
| R-HSA-190373 | FGFR1c ligand binding and activation | 6.920234e-01 | 0.160 |
| R-HSA-162658 | Golgi Cisternae Pericentriolar Stack Reorganization | 6.920234e-01 | 0.160 |
| R-HSA-9682706 | Replication of the SARS-CoV-1 genome | 6.920234e-01 | 0.160 |
| R-HSA-379724 | tRNA Aminoacylation | 6.922098e-01 | 0.160 |
| R-HSA-5334118 | DNA methylation | 6.969647e-01 | 0.157 |
| R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 6.969647e-01 | 0.157 |
| R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 6.978125e-01 | 0.156 |
| R-HSA-3928662 | EPHB-mediated forward signaling | 6.978125e-01 | 0.156 |
| R-HSA-9907900 | Proteasome assembly | 6.978125e-01 | 0.156 |
| R-HSA-4608870 | Asymmetric localization of PCP proteins | 7.098950e-01 | 0.149 |
| R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 7.098950e-01 | 0.149 |
| R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 7.098950e-01 | 0.149 |
| R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 7.115461e-01 | 0.148 |
| R-HSA-8863795 | Downregulation of ERBB2 signaling | 7.115461e-01 | 0.148 |
| R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 7.115461e-01 | 0.148 |
| R-HSA-8847993 | ERBB2 Activates PTK6 Signaling | 7.126484e-01 | 0.147 |
| R-HSA-1855191 | Synthesis of IPs in the nucleus | 7.126484e-01 | 0.147 |
| R-HSA-1483115 | Hydrolysis of LPC | 7.126484e-01 | 0.147 |
| R-HSA-9023661 | Biosynthesis of E-series 18(R)-resolvins | 7.126484e-01 | 0.147 |
| R-HSA-205043 | NRIF signals cell death from the nucleus | 7.126484e-01 | 0.147 |
| R-HSA-5684264 | MAP3K8 (TPL2)-dependent MAPK1/3 activation | 7.126484e-01 | 0.147 |
| R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 7.126484e-01 | 0.147 |
| R-HSA-173599 | Formation of the active cofactor, UDP-glucuronate | 7.126484e-01 | 0.147 |
| R-HSA-5578768 | Physiological factors | 7.126484e-01 | 0.147 |
| R-HSA-9856872 | Malate-aspartate shuttle | 7.126484e-01 | 0.147 |
| R-HSA-1482798 | Acyl chain remodeling of CL | 7.126484e-01 | 0.147 |
| R-HSA-9679514 | SARS-CoV-1 Genome Replication and Transcription | 7.126484e-01 | 0.147 |
| R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 7.134248e-01 | 0.147 |
| R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 7.134248e-01 | 0.147 |
| R-HSA-375165 | NCAM signaling for neurite out-growth | 7.134248e-01 | 0.147 |
| R-HSA-9824446 | Viral Infection Pathways | 7.155296e-01 | 0.145 |
| R-HSA-69239 | Synthesis of DNA | 7.159786e-01 | 0.145 |
| R-HSA-68867 | Assembly of the pre-replicative complex | 7.166600e-01 | 0.145 |
| R-HSA-9758941 | Gastrulation | 7.186806e-01 | 0.143 |
| R-HSA-9925561 | Developmental Lineage of Pancreatic Acinar Cells | 7.188754e-01 | 0.143 |
| R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 7.216024e-01 | 0.142 |
| R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 7.216024e-01 | 0.142 |
| R-HSA-5357905 | Regulation of TNFR1 signaling | 7.216024e-01 | 0.142 |
| R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 7.236222e-01 | 0.140 |
| R-HSA-162588 | Budding and maturation of HIV virion | 7.255349e-01 | 0.139 |
| R-HSA-2129379 | Molecules associated with elastic fibres | 7.255349e-01 | 0.139 |
| R-HSA-182971 | EGFR downregulation | 7.255349e-01 | 0.139 |
| R-HSA-9833109 | Evasion by RSV of host interferon responses | 7.255349e-01 | 0.139 |
| R-HSA-1852241 | Organelle biogenesis and maintenance | 7.302623e-01 | 0.137 |
| R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 7.318933e-01 | 0.136 |
| R-HSA-9857492 | Protein lipoylation | 7.318933e-01 | 0.136 |
| R-HSA-193639 | p75NTR signals via NF-kB | 7.318933e-01 | 0.136 |
| R-HSA-1502540 | Signaling by Activin | 7.318933e-01 | 0.136 |
| R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 7.318933e-01 | 0.136 |
| R-HSA-171007 | p38MAPK events | 7.318933e-01 | 0.136 |
| R-HSA-419408 | Lysosphingolipid and LPA receptors | 7.318933e-01 | 0.136 |
| R-HSA-111447 | Activation of BAD and translocation to mitochondria | 7.318933e-01 | 0.136 |
| R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 7.318933e-01 | 0.136 |
| R-HSA-1295596 | Spry regulation of FGF signaling | 7.318933e-01 | 0.136 |
| R-HSA-450385 | Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA | 7.318933e-01 | 0.136 |
| R-HSA-8875360 | InlB-mediated entry of Listeria monocytogenes into host cell | 7.318933e-01 | 0.136 |
| R-HSA-416700 | Other semaphorin interactions | 7.318933e-01 | 0.136 |
| R-HSA-446353 | Cell-extracellular matrix interactions | 7.318933e-01 | 0.136 |
| R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 7.329383e-01 | 0.135 |
| R-HSA-1483191 | Synthesis of PC | 7.329383e-01 | 0.135 |
| R-HSA-5619102 | SLC transporter disorders | 7.330765e-01 | 0.135 |
| R-HSA-168249 | Innate Immune System | 7.379444e-01 | 0.132 |
| R-HSA-9675126 | Diseases of mitotic cell cycle | 7.389450e-01 | 0.131 |
| R-HSA-9937080 | Developmental Lineage of Multipotent Pancreatic Progenitor Cells | 7.389450e-01 | 0.131 |
| R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 7.389450e-01 | 0.131 |
| R-HSA-69190 | DNA strand elongation | 7.389450e-01 | 0.131 |
| R-HSA-201681 | TCF dependent signaling in response to WNT | 7.404433e-01 | 0.131 |
| R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 7.415603e-01 | 0.130 |
| R-HSA-70263 | Gluconeogenesis | 7.439071e-01 | 0.128 |
| R-HSA-69306 | DNA Replication | 7.447586e-01 | 0.128 |
| R-HSA-9609507 | Protein localization | 7.447586e-01 | 0.128 |
| R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 7.455409e-01 | 0.128 |
| R-HSA-354194 | GRB2:SOS provides linkage to MAPK signaling for Integrins | 7.498503e-01 | 0.125 |
| R-HSA-168275 | Entry of Influenza Virion into Host Cell via Endocytosis | 7.498503e-01 | 0.125 |
| R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 7.498503e-01 | 0.125 |
| R-HSA-9664420 | Killing mechanisms | 7.498503e-01 | 0.125 |
| R-HSA-9673324 | WNT5:FZD7-mediated leishmania damping | 7.498503e-01 | 0.125 |
| R-HSA-5635838 | Activation of SMO | 7.498503e-01 | 0.125 |
| R-HSA-9754706 | Atorvastatin ADME | 7.498503e-01 | 0.125 |
| R-HSA-450604 | KSRP (KHSRP) binds and destabilizes mRNA | 7.498503e-01 | 0.125 |
| R-HSA-399955 | SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion | 7.498503e-01 | 0.125 |
| R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 7.498503e-01 | 0.125 |
| R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 7.517912e-01 | 0.124 |
| R-HSA-68616 | Assembly of the ORC complex at the origin of replication | 7.517912e-01 | 0.124 |
| R-HSA-397795 | G-protein beta:gamma signalling | 7.517912e-01 | 0.124 |
| R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 7.540022e-01 | 0.123 |
| R-HSA-532668 | N-glycan trimming in the ER and Calnexin/Calreticulin cycle | 7.545136e-01 | 0.122 |
| R-HSA-1989781 | PPARA activates gene expression | 7.571659e-01 | 0.121 |
| R-HSA-948021 | Transport to the Golgi and subsequent modification | 7.584617e-01 | 0.120 |
| R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 7.622515e-01 | 0.118 |
| R-HSA-1482788 | Acyl chain remodelling of PC | 7.640889e-01 | 0.117 |
| R-HSA-180534 | Vpu mediated degradation of CD4 | 7.640889e-01 | 0.117 |
| R-HSA-199220 | Vitamin B5 (pantothenate) metabolism | 7.640889e-01 | 0.117 |
| R-HSA-5223345 | Miscellaneous transport and binding events | 7.640889e-01 | 0.117 |
| R-HSA-2892247 | POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation | 7.666057e-01 | 0.115 |
| R-HSA-8964616 | G beta:gamma signalling through CDC42 | 7.666057e-01 | 0.115 |
| R-HSA-141430 | Inactivation of APC/C via direct inhibition of the APC/C complex | 7.666057e-01 | 0.115 |
| R-HSA-3000471 | Scavenging by Class B Receptors | 7.666057e-01 | 0.115 |
| R-HSA-6783984 | Glycine degradation | 7.666057e-01 | 0.115 |
| R-HSA-141405 | Inhibition of the proteolytic activity of APC/C required for the onset of anapha... | 7.666057e-01 | 0.115 |
| R-HSA-975110 | TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling | 7.666057e-01 | 0.115 |
| R-HSA-918233 | TRAF3-dependent IRF activation pathway | 7.666057e-01 | 0.115 |
| R-HSA-9027307 | Biosynthesis of maresin-like SPMs | 7.666057e-01 | 0.115 |
| R-HSA-964975 | Vitamin B6 activation to pyridoxal phosphate | 7.666057e-01 | 0.115 |
| R-HSA-9702518 | STAT5 activation downstream of FLT3 ITD mutants | 7.666057e-01 | 0.115 |
| R-HSA-432047 | Passive transport by Aquaporins | 7.666057e-01 | 0.115 |
| R-HSA-5661270 | Formation of xylulose-5-phosphate | 7.666057e-01 | 0.115 |
| R-HSA-196783 | Coenzyme A biosynthesis | 7.666057e-01 | 0.115 |
| R-HSA-9614085 | FOXO-mediated transcription | 7.720114e-01 | 0.112 |
| R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 7.746625e-01 | 0.111 |
| R-HSA-1169091 | Activation of NF-kappaB in B cells | 7.746625e-01 | 0.111 |
| R-HSA-5696400 | Dual Incision in GG-NER | 7.758539e-01 | 0.110 |
| R-HSA-1980145 | Signaling by NOTCH2 | 7.758539e-01 | 0.110 |
| R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 7.758539e-01 | 0.110 |
| R-HSA-5365859 | RA biosynthesis pathway | 7.758539e-01 | 0.110 |
| R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 7.781203e-01 | 0.109 |
| R-HSA-8951664 | Neddylation | 7.797386e-01 | 0.108 |
| R-HSA-372708 | p130Cas linkage to MAPK signaling for integrins | 7.822397e-01 | 0.107 |
| R-HSA-176407 | Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase | 7.822397e-01 | 0.107 |
| R-HSA-3229121 | Glycogen storage diseases | 7.822397e-01 | 0.107 |
| R-HSA-9020265 | Biosynthesis of aspirin-triggered D-series resolvins | 7.822397e-01 | 0.107 |
| R-HSA-1963642 | PI3K events in ERBB2 signaling | 7.822397e-01 | 0.107 |
| R-HSA-139853 | Elevation of cytosolic Ca2+ levels | 7.822397e-01 | 0.107 |
| R-HSA-9909505 | Modulation of host responses by IFN-stimulated genes | 7.822397e-01 | 0.107 |
| R-HSA-209905 | Catecholamine biosynthesis | 7.822397e-01 | 0.107 |
| R-HSA-2408550 | Metabolism of ingested H2SeO4 and H2SeO3 into H2Se | 7.822397e-01 | 0.107 |
| R-HSA-9694686 | Replication of the SARS-CoV-2 genome | 7.822397e-01 | 0.107 |
| R-HSA-72187 | mRNA 3'-end processing | 7.842172e-01 | 0.106 |
| R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 7.842172e-01 | 0.106 |
| R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 7.842172e-01 | 0.106 |
| R-HSA-199418 | Negative regulation of the PI3K/AKT network | 7.845889e-01 | 0.105 |
| R-HSA-5653656 | Vesicle-mediated transport | 7.860011e-01 | 0.105 |
| R-HSA-1482839 | Acyl chain remodelling of PE | 7.871024e-01 | 0.104 |
| R-HSA-381042 | PERK regulates gene expression | 7.871024e-01 | 0.104 |
| R-HSA-193775 | Synthesis of bile acids and bile salts via 24-hydroxycholesterol | 7.871024e-01 | 0.104 |
| R-HSA-909733 | Interferon alpha/beta signaling | 7.880700e-01 | 0.103 |
| R-HSA-1483255 | PI Metabolism | 7.931071e-01 | 0.101 |
| R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 7.955866e-01 | 0.099 |
| R-HSA-2142700 | Biosynthesis of Lipoxins (LX) | 7.968273e-01 | 0.099 |
| R-HSA-190242 | FGFR1 ligand binding and activation | 7.968273e-01 | 0.099 |
| R-HSA-428643 | Organic anion transport by SLC5/17/25 transporters | 7.968273e-01 | 0.099 |
| R-HSA-9679504 | Translation of Replicase and Assembly of the Replication Transcription Complex | 7.968273e-01 | 0.099 |
| R-HSA-9682385 | FLT3 signaling in disease | 7.978506e-01 | 0.098 |
| R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 7.978506e-01 | 0.098 |
| R-HSA-1592230 | Mitochondrial biogenesis | 8.006958e-01 | 0.097 |
| R-HSA-156588 | Glucuronidation | 8.023208e-01 | 0.096 |
| R-HSA-76002 | Platelet activation, signaling and aggregation | 8.035622e-01 | 0.095 |
| R-HSA-1236974 | ER-Phagosome pathway | 8.073933e-01 | 0.093 |
| R-HSA-1296072 | Voltage gated Potassium channels | 8.081152e-01 | 0.093 |
| R-HSA-933541 | TRAF6 mediated IRF7 activation | 8.081152e-01 | 0.093 |
| R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 8.081152e-01 | 0.093 |
| R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 8.081152e-01 | 0.093 |
| R-HSA-549127 | SLC-mediated transport of organic cations | 8.081152e-01 | 0.093 |
| R-HSA-167242 | Abortive elongation of HIV-1 transcript in the absence of Tat | 8.104385e-01 | 0.091 |
| R-HSA-500753 | Pyrimidine biosynthesis | 8.104385e-01 | 0.091 |
| R-HSA-9834899 | Specification of the neural plate border | 8.104385e-01 | 0.091 |
| R-HSA-2142688 | Synthesis of 5-eicosatetraenoic acids | 8.104385e-01 | 0.091 |
| R-HSA-113510 | E2F mediated regulation of DNA replication | 8.104385e-01 | 0.091 |
| R-HSA-1480926 | O2/CO2 exchange in erythrocytes | 8.104385e-01 | 0.091 |
| R-HSA-392517 | Rap1 signalling | 8.104385e-01 | 0.091 |
| R-HSA-1237044 | Erythrocytes take up carbon dioxide and release oxygen | 8.104385e-01 | 0.091 |
| R-HSA-9856532 | Mechanical load activates signaling by PIEZO1 and integrins in osteocytes | 8.104385e-01 | 0.091 |
| R-HSA-2243919 | Crosslinking of collagen fibrils | 8.104385e-01 | 0.091 |
| R-HSA-9694631 | Maturation of nucleoprotein | 8.104385e-01 | 0.091 |
| R-HSA-9694682 | SARS-CoV-2 Genome Replication and Transcription | 8.104385e-01 | 0.091 |
| R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 8.126729e-01 | 0.090 |
| R-HSA-5619507 | Activation of HOX genes during differentiation | 8.126729e-01 | 0.090 |
| R-HSA-1566948 | Elastic fibre formation | 8.179127e-01 | 0.087 |
| R-HSA-5696398 | Nucleotide Excision Repair | 8.188629e-01 | 0.087 |
| R-HSA-177929 | Signaling by EGFR | 8.191313e-01 | 0.087 |
| R-HSA-3299685 | Detoxification of Reactive Oxygen Species | 8.191313e-01 | 0.087 |
| R-HSA-5620916 | VxPx cargo-targeting to cilium | 8.231386e-01 | 0.085 |
| R-HSA-3322077 | Glycogen synthesis | 8.231386e-01 | 0.085 |
| R-HSA-1181150 | Signaling by NODAL | 8.231386e-01 | 0.085 |
| R-HSA-8848584 | Wax and plasmalogen biosynthesis | 8.231386e-01 | 0.085 |
| R-HSA-71288 | Creatine metabolism | 8.231386e-01 | 0.085 |
| R-HSA-1482922 | Acyl chain remodelling of PI | 8.231386e-01 | 0.085 |
| R-HSA-196108 | Pregnenolone biosynthesis | 8.231386e-01 | 0.085 |
| R-HSA-445144 | Signal transduction by L1 | 8.231386e-01 | 0.085 |
| R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 8.254749e-01 | 0.083 |
| R-HSA-3000171 | Non-integrin membrane-ECM interactions | 8.254749e-01 | 0.083 |
| R-HSA-1483166 | Synthesis of PA | 8.270705e-01 | 0.082 |
| R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 8.272596e-01 | 0.082 |
| R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 8.272596e-01 | 0.082 |
| R-HSA-6782135 | Dual incision in TC-NER | 8.347093e-01 | 0.078 |
| R-HSA-2979096 | NOTCH2 Activation and Transmission of Signal to the Nucleus | 8.349886e-01 | 0.078 |
| R-HSA-450321 | JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ... | 8.349886e-01 | 0.078 |
| R-HSA-9018896 | Biosynthesis of E-series 18(S)-resolvins | 8.349886e-01 | 0.078 |
| R-HSA-8964208 | Phenylalanine metabolism | 8.349886e-01 | 0.078 |
| R-HSA-9931295 | PD-L1(CD274) glycosylation and translocation to plasma membrane | 8.349886e-01 | 0.078 |
| R-HSA-2161541 | Abacavir metabolism | 8.349886e-01 | 0.078 |
| R-HSA-422085 | Synthesis, secretion, and deacylation of Ghrelin | 8.349886e-01 | 0.078 |
| R-HSA-9819196 | Zygotic genome activation (ZGA) | 8.349886e-01 | 0.078 |
| R-HSA-1482925 | Acyl chain remodelling of PG | 8.349886e-01 | 0.078 |
| R-HSA-9636383 | Prevention of phagosomal-lysosomal fusion | 8.349886e-01 | 0.078 |
| R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 8.361722e-01 | 0.078 |
| R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 8.361722e-01 | 0.078 |
| R-HSA-167169 | HIV Transcription Elongation | 8.361722e-01 | 0.078 |
| R-HSA-5696395 | Formation of Incision Complex in GG-NER | 8.361722e-01 | 0.078 |
| R-HSA-8982491 | Glycogen metabolism | 8.361722e-01 | 0.078 |
| R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 8.361722e-01 | 0.078 |
| R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 8.364652e-01 | 0.078 |
| R-HSA-1236975 | Antigen processing-Cross presentation | 8.364652e-01 | 0.078 |
| R-HSA-2672351 | Stimuli-sensing channels | 8.364652e-01 | 0.078 |
| R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 8.404910e-01 | 0.075 |
| R-HSA-72306 | tRNA processing | 8.413874e-01 | 0.075 |
| R-HSA-180786 | Extension of Telomeres | 8.420558e-01 | 0.075 |
| R-HSA-2022090 | Assembly of collagen fibrils and other multimeric structures | 8.420558e-01 | 0.075 |
| R-HSA-5625886 | Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene... | 8.446668e-01 | 0.073 |
| R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 8.446668e-01 | 0.073 |
| R-HSA-5362768 | Hh mutants are degraded by ERAD | 8.446668e-01 | 0.073 |
| R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 8.460452e-01 | 0.073 |
| R-HSA-5603041 | IRAK4 deficiency (TLR2/4) | 8.460452e-01 | 0.073 |
| R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 8.460452e-01 | 0.073 |
| R-HSA-175474 | Assembly Of The HIV Virion | 8.460452e-01 | 0.073 |
| R-HSA-9034015 | Signaling by NTRK3 (TRKC) | 8.460452e-01 | 0.073 |
| R-HSA-1227986 | Signaling by ERBB2 | 8.491177e-01 | 0.071 |
| R-HSA-3000480 | Scavenging by Class A Receptors | 8.527593e-01 | 0.069 |
| R-HSA-9932298 | Degradation of CRY and PER proteins | 8.527593e-01 | 0.069 |
| R-HSA-5610780 | Degradation of GLI1 by the proteasome | 8.527593e-01 | 0.069 |
| R-HSA-5610783 | Degradation of GLI2 by the proteasome | 8.527593e-01 | 0.069 |
| R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 8.527593e-01 | 0.069 |
| R-HSA-73856 | RNA Polymerase II Transcription Termination | 8.559032e-01 | 0.068 |
| R-HSA-9793380 | Formation of paraxial mesoderm | 8.559032e-01 | 0.068 |
| R-HSA-9669938 | Signaling by KIT in disease | 8.563617e-01 | 0.067 |
| R-HSA-9670439 | Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m... | 8.563617e-01 | 0.067 |
| R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 8.563617e-01 | 0.067 |
| R-HSA-9018676 | Biosynthesis of D-series resolvins | 8.563617e-01 | 0.067 |
| R-HSA-3238698 | WNT ligand biogenesis and trafficking | 8.563617e-01 | 0.067 |
| R-HSA-9013507 | NOTCH3 Activation and Transmission of Signal to the Nucleus | 8.563617e-01 | 0.067 |
| R-HSA-112409 | RAF-independent MAPK1/3 activation | 8.563617e-01 | 0.067 |
| R-HSA-9694676 | Translation of Replicase and Assembly of the Replication Transcription Complex | 8.563617e-01 | 0.067 |
| R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 8.620136e-01 | 0.064 |
| R-HSA-1268020 | Mitochondrial protein import | 8.624203e-01 | 0.064 |
| R-HSA-186797 | Signaling by PDGF | 8.624203e-01 | 0.064 |
| R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 8.634391e-01 | 0.064 |
| R-HSA-8854691 | Interleukin-20 family signaling | 8.659874e-01 | 0.062 |
| R-HSA-392451 | G beta:gamma signalling through PI3Kgamma | 8.659874e-01 | 0.062 |
| R-HSA-9634638 | Estrogen-dependent nuclear events downstream of ESR-membrane signaling | 8.659874e-01 | 0.062 |
| R-HSA-879518 | Organic anion transport by SLCO transporters | 8.659874e-01 | 0.062 |
| R-HSA-5387390 | Hh mutants abrogate ligand secretion | 8.678008e-01 | 0.062 |
| R-HSA-8848021 | Signaling by PTK6 | 8.686769e-01 | 0.061 |
| R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 8.686769e-01 | 0.061 |
| R-HSA-422356 | Regulation of insulin secretion | 8.722107e-01 | 0.059 |
| R-HSA-109582 | Hemostasis | 8.727011e-01 | 0.059 |
| R-HSA-211999 | CYP2E1 reactions | 8.749686e-01 | 0.058 |
| R-HSA-202430 | Translocation of ZAP-70 to Immunological synapse | 8.749686e-01 | 0.058 |
| R-HSA-6783589 | Interleukin-6 family signaling | 8.749686e-01 | 0.058 |
| R-HSA-8963898 | Plasma lipoprotein assembly | 8.749686e-01 | 0.058 |
| R-HSA-933542 | TRAF6 mediated NF-kB activation | 8.749686e-01 | 0.058 |
| R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 8.749686e-01 | 0.058 |
| R-HSA-9703648 | Signaling by FLT3 ITD and TKD mutants | 8.749686e-01 | 0.058 |
| R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 8.749686e-01 | 0.058 |
| R-HSA-446199 | Synthesis of dolichyl-phosphate | 8.749686e-01 | 0.058 |
| R-HSA-5669034 | TNFs bind their physiological receptors | 8.749686e-01 | 0.058 |
| R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 8.796148e-01 | 0.056 |
| R-HSA-1234174 | Cellular response to hypoxia | 8.804407e-01 | 0.055 |
| R-HSA-76009 | Platelet Aggregation (Plug Formation) | 8.814185e-01 | 0.055 |
| R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 8.814185e-01 | 0.055 |
| R-HSA-1614558 | Degradation of cysteine and homocysteine | 8.814185e-01 | 0.055 |
| R-HSA-9824272 | Somitogenesis | 8.814185e-01 | 0.055 |
| R-HSA-1296059 | G protein gated Potassium channels | 8.833484e-01 | 0.054 |
| R-HSA-997272 | Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits | 8.833484e-01 | 0.054 |
| R-HSA-1296041 | Activation of G protein gated Potassium channels | 8.833484e-01 | 0.054 |
| R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 8.833484e-01 | 0.054 |
| R-HSA-389887 | Beta-oxidation of pristanoyl-CoA | 8.833484e-01 | 0.054 |
| R-HSA-9027604 | Biosynthesis of electrophilic ω-3 PUFA oxo-derivatives | 8.833484e-01 | 0.054 |
| R-HSA-1187000 | Fertilization | 8.833484e-01 | 0.054 |
| R-HSA-5218921 | VEGFR2 mediated cell proliferation | 8.833484e-01 | 0.054 |
| R-HSA-2122948 | Activated NOTCH1 Transmits Signal to the Nucleus | 8.911670e-01 | 0.050 |
| R-HSA-2161522 | Abacavir ADME | 8.911670e-01 | 0.050 |
| R-HSA-1660514 | Synthesis of PIPs at the Golgi membrane | 8.911670e-01 | 0.050 |
| R-HSA-9830369 | Kidney development | 8.912574e-01 | 0.050 |
| R-HSA-193368 | Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol | 8.912574e-01 | 0.050 |
| R-HSA-9609646 | HCMV Infection | 8.914999e-01 | 0.050 |
| R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 8.937288e-01 | 0.049 |
| R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 8.937288e-01 | 0.049 |
| R-HSA-73863 | RNA Polymerase I Transcription Termination | 8.984620e-01 | 0.047 |
| R-HSA-73728 | RNA Polymerase I Promoter Opening | 8.984620e-01 | 0.047 |
| R-HSA-8949613 | Cristae formation | 8.984620e-01 | 0.047 |
| R-HSA-9025094 | Biosynthesis of DPAn-3 SPMs | 8.984620e-01 | 0.047 |
| R-HSA-83936 | Transport of nucleosides and free purine and pyrimidine bases across the plasma ... | 8.984620e-01 | 0.047 |
| R-HSA-8866652 | Synthesis of active ubiquitin: roles of E1 and E2 enzymes | 8.984620e-01 | 0.047 |
| R-HSA-901032 | ER Quality Control Compartment (ERQC) | 8.984620e-01 | 0.047 |
| R-HSA-264876 | Insulin processing | 8.984620e-01 | 0.047 |
| R-HSA-425410 | Metal ion SLC transporters | 8.994284e-01 | 0.046 |
| R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 9.012202e-01 | 0.045 |
| R-HSA-157858 | Gap junction trafficking and regulation | 9.048418e-01 | 0.043 |
| R-HSA-113418 | Formation of the Early Elongation Complex | 9.052685e-01 | 0.043 |
| R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 9.052685e-01 | 0.043 |
| R-HSA-167158 | Formation of the HIV-1 Early Elongation Complex | 9.052685e-01 | 0.043 |
| R-HSA-77387 | Insulin receptor recycling | 9.052685e-01 | 0.043 |
| R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 9.052685e-01 | 0.043 |
| R-HSA-5654732 | Negative regulation of FGFR3 signaling | 9.052685e-01 | 0.043 |
| R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 9.052685e-01 | 0.043 |
| R-HSA-73614 | Pyrimidine salvage | 9.052685e-01 | 0.043 |
| R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 9.076623e-01 | 0.042 |
| R-HSA-8957322 | Metabolism of steroids | 9.095231e-01 | 0.041 |
| R-HSA-109704 | PI3K Cascade | 9.099819e-01 | 0.041 |
| R-HSA-975634 | Retinoid metabolism and transport | 9.102942e-01 | 0.041 |
| R-HSA-189445 | Metabolism of porphyrins | 9.102942e-01 | 0.041 |
| R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 9.116191e-01 | 0.040 |
| R-HSA-917729 | Endosomal Sorting Complex Required For Transport (ESCRT) | 9.116191e-01 | 0.040 |
| R-HSA-9018679 | Biosynthesis of EPA-derived SPMs | 9.116191e-01 | 0.040 |
| R-HSA-204174 | Regulation of pyruvate dehydrogenase (PDH) complex | 9.116191e-01 | 0.040 |
| R-HSA-5654733 | Negative regulation of FGFR4 signaling | 9.116191e-01 | 0.040 |
| R-HSA-392154 | Nitric oxide stimulates guanylate cyclase | 9.116191e-01 | 0.040 |
| R-HSA-180024 | DARPP-32 events | 9.116191e-01 | 0.040 |
| R-HSA-210745 | Regulation of gene expression in beta cells | 9.116191e-01 | 0.040 |
| R-HSA-1592389 | Activation of Matrix Metalloproteinases | 9.116191e-01 | 0.040 |
| R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 9.145553e-01 | 0.039 |
| R-HSA-5358346 | Hedgehog ligand biogenesis | 9.148609e-01 | 0.039 |
| R-HSA-2424491 | DAP12 signaling | 9.175443e-01 | 0.037 |
| R-HSA-1250196 | SHC1 events in ERBB2 signaling | 9.175443e-01 | 0.037 |
| R-HSA-76046 | RNA Polymerase III Transcription Initiation | 9.175443e-01 | 0.037 |
| R-HSA-1227990 | Signaling by ERBB2 in Cancer | 9.175443e-01 | 0.037 |
| R-HSA-112311 | Neurotransmitter clearance | 9.175443e-01 | 0.037 |
| R-HSA-9749641 | Aspirin ADME | 9.186314e-01 | 0.037 |
| R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 9.194799e-01 | 0.036 |
| R-HSA-112382 | Formation of RNA Pol II elongation complex | 9.194908e-01 | 0.036 |
| R-HSA-73772 | RNA Polymerase I Promoter Escape | 9.194908e-01 | 0.036 |
| R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 9.213064e-01 | 0.036 |
| R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 9.213064e-01 | 0.036 |
| R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 9.213064e-01 | 0.036 |
| R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 9.220905e-01 | 0.035 |
| R-HSA-1226099 | Signaling by FGFR in disease | 9.225293e-01 | 0.035 |
| R-HSA-1222556 | ROS and RNS production in phagocytes | 9.225293e-01 | 0.035 |
| R-HSA-9913351 | Formation of the dystrophin-glycoprotein complex (DGC) | 9.230726e-01 | 0.035 |
| R-HSA-9018683 | Biosynthesis of DPA-derived SPMs | 9.230726e-01 | 0.035 |
| R-HSA-162710 | Synthesis of glycosylphosphatidylinositol (GPI) | 9.230726e-01 | 0.035 |
| R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 9.230726e-01 | 0.035 |
| R-HSA-75955 | RNA Polymerase II Transcription Elongation | 9.238829e-01 | 0.034 |
| R-HSA-8956320 | Nucleotide biosynthesis | 9.238829e-01 | 0.034 |
| R-HSA-9734767 | Developmental Cell Lineages | 9.239084e-01 | 0.034 |
| R-HSA-917937 | Iron uptake and transport | 9.262556e-01 | 0.033 |
| R-HSA-5619115 | Disorders of transmembrane transporters | 9.265374e-01 | 0.033 |
| R-HSA-1296065 | Inwardly rectifying K+ channels | 9.282305e-01 | 0.032 |
| R-HSA-8856828 | Clathrin-mediated endocytosis | 9.282528e-01 | 0.032 |
| R-HSA-9837999 | Mitochondrial protein degradation | 9.287659e-01 | 0.032 |
| R-HSA-354192 | Integrin signaling | 9.330429e-01 | 0.030 |
| R-HSA-9930044 | Nuclear RNA decay | 9.330429e-01 | 0.030 |
| R-HSA-9668328 | Sealing of the nuclear envelope (NE) by ESCRT-III | 9.330429e-01 | 0.030 |
| R-HSA-5654726 | Negative regulation of FGFR1 signaling | 9.330429e-01 | 0.030 |
| R-HSA-5609975 | Diseases associated with glycosylation precursor biosynthesis | 9.330429e-01 | 0.030 |
| R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 9.357415e-01 | 0.029 |
| R-HSA-5654736 | Signaling by FGFR1 | 9.357415e-01 | 0.029 |
| R-HSA-6783783 | Interleukin-10 signaling | 9.364691e-01 | 0.029 |
| R-HSA-191273 | Cholesterol biosynthesis | 9.364691e-01 | 0.029 |
| R-HSA-216083 | Integrin cell surface interactions | 9.364691e-01 | 0.029 |
| R-HSA-8964539 | Glutamate and glutamine metabolism | 9.375329e-01 | 0.028 |
| R-HSA-114508 | Effects of PIP2 hydrolysis | 9.375329e-01 | 0.028 |
| R-HSA-112399 | IRS-mediated signalling | 9.392892e-01 | 0.027 |
| R-HSA-157579 | Telomere Maintenance | 9.405894e-01 | 0.027 |
| R-HSA-9843970 | Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex | 9.417221e-01 | 0.026 |
| R-HSA-983170 | Antigen Presentation: Folding, assembly and peptide loading of class I MHC | 9.417221e-01 | 0.026 |
| R-HSA-5654727 | Negative regulation of FGFR2 signaling | 9.417221e-01 | 0.026 |
| R-HSA-5686938 | Regulation of TLR by endogenous ligand | 9.417221e-01 | 0.026 |
| R-HSA-1368108 | BMAL1:CLOCK,NPAS2 activates circadian expression | 9.417221e-01 | 0.026 |
| R-HSA-392518 | Signal amplification | 9.417221e-01 | 0.026 |
| R-HSA-5654738 | Signaling by FGFR2 | 9.425346e-01 | 0.026 |
| R-HSA-6806834 | Signaling by MET | 9.425346e-01 | 0.026 |
| R-HSA-9772572 | Early SARS-CoV-2 Infection Events | 9.426504e-01 | 0.026 |
| R-HSA-190236 | Signaling by FGFR | 9.432517e-01 | 0.025 |
| R-HSA-6806667 | Metabolism of fat-soluble vitamins | 9.453618e-01 | 0.024 |
| R-HSA-917977 | Transferrin endocytosis and recycling | 9.456306e-01 | 0.024 |
| R-HSA-3296482 | Defects in vitamin and cofactor metabolism | 9.456306e-01 | 0.024 |
| R-HSA-72766 | Translation | 9.477638e-01 | 0.023 |
| R-HSA-156590 | Glutathione conjugation | 9.488489e-01 | 0.023 |
| R-HSA-5362517 | Signaling by Retinoic Acid | 9.488489e-01 | 0.023 |
| R-HSA-351202 | Metabolism of polyamines | 9.488489e-01 | 0.023 |
| R-HSA-74158 | RNA Polymerase III Transcription | 9.492771e-01 | 0.023 |
| R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 9.492771e-01 | 0.023 |
| R-HSA-8853659 | RET signaling | 9.492771e-01 | 0.023 |
| R-HSA-9845576 | Glycosphingolipid transport | 9.492771e-01 | 0.023 |
| R-HSA-1483257 | Phospholipid metabolism | 9.500444e-01 | 0.022 |
| R-HSA-2428928 | IRS-related events triggered by IGF1R | 9.517033e-01 | 0.021 |
| R-HSA-427359 | SIRT1 negatively regulates rRNA expression | 9.526793e-01 | 0.021 |
| R-HSA-390247 | Beta-oxidation of very long chain fatty acids | 9.526793e-01 | 0.021 |
| R-HSA-419037 | NCAM1 interactions | 9.526793e-01 | 0.021 |
| R-HSA-8963691 | Phenylalanine and tyrosine metabolism | 9.526793e-01 | 0.021 |
| R-HSA-2142789 | Ubiquinol biosynthesis | 9.526793e-01 | 0.021 |
| R-HSA-196757 | Metabolism of folate and pterines | 9.526793e-01 | 0.021 |
| R-HSA-9616222 | Transcriptional regulation of granulopoiesis | 9.544051e-01 | 0.020 |
| R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 9.549277e-01 | 0.020 |
| R-HSA-2046106 | alpha-linolenic acid (ALA) metabolism | 9.558535e-01 | 0.020 |
| R-HSA-8875878 | MET promotes cell motility | 9.558535e-01 | 0.020 |
| R-HSA-9610379 | HCMV Late Events | 9.578784e-01 | 0.019 |
| R-HSA-71336 | Pentose phosphate pathway | 9.588149e-01 | 0.018 |
| R-HSA-2428924 | IGF1R signaling cascade | 9.593813e-01 | 0.018 |
| R-HSA-74751 | Insulin receptor signalling cascade | 9.593813e-01 | 0.018 |
| R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 9.599804e-01 | 0.018 |
| R-HSA-9854311 | Maturation of TCA enzymes and regulation of TCA cycle | 9.615778e-01 | 0.017 |
| R-HSA-1251985 | Nuclear signaling by ERBB4 | 9.615778e-01 | 0.017 |
| R-HSA-71240 | Tryptophan catabolism | 9.615778e-01 | 0.017 |
| R-HSA-2404192 | Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) | 9.616699e-01 | 0.017 |
| R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 9.617917e-01 | 0.017 |
| R-HSA-9694548 | Maturation of spike protein | 9.641556e-01 | 0.016 |
| R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 9.641556e-01 | 0.016 |
| R-HSA-9683701 | Translation of Structural Proteins | 9.665605e-01 | 0.015 |
| R-HSA-167172 | Transcription of the HIV genome | 9.678163e-01 | 0.014 |
| R-HSA-425407 | SLC-mediated transmembrane transport | 9.683077e-01 | 0.014 |
| R-HSA-991365 | Activation of GABAB receptors | 9.688043e-01 | 0.014 |
| R-HSA-977444 | GABA B receptor activation | 9.688043e-01 | 0.014 |
| R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.700098e-01 | 0.013 |
| R-HSA-5654743 | Signaling by FGFR4 | 9.708976e-01 | 0.013 |
| R-HSA-2871796 | FCERI mediated MAPK activation | 9.720554e-01 | 0.012 |
| R-HSA-74752 | Signaling by Insulin receptor | 9.720748e-01 | 0.012 |
| R-HSA-2172127 | DAP12 interactions | 9.728505e-01 | 0.012 |
| R-HSA-2142691 | Synthesis of Leukotrienes (LT) and Eoxins (EX) | 9.728505e-01 | 0.012 |
| R-HSA-190828 | Gap junction trafficking | 9.728505e-01 | 0.012 |
| R-HSA-5683826 | Surfactant metabolism | 9.728505e-01 | 0.012 |
| R-HSA-69231 | Cyclin D associated events in G1 | 9.728505e-01 | 0.012 |
| R-HSA-69236 | G1 Phase | 9.728505e-01 | 0.012 |
| R-HSA-8978934 | Metabolism of cofactors | 9.730079e-01 | 0.012 |
| R-HSA-5654741 | Signaling by FGFR3 | 9.746725e-01 | 0.011 |
| R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 9.748728e-01 | 0.011 |
| R-HSA-1474290 | Collagen formation | 9.748728e-01 | 0.011 |
| R-HSA-5663084 | Diseases of carbohydrate metabolism | 9.760092e-01 | 0.011 |
| R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 9.761699e-01 | 0.010 |
| R-HSA-2299718 | Condensation of Prophase Chromosomes | 9.763724e-01 | 0.010 |
| R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 9.763724e-01 | 0.010 |
| R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 9.773862e-01 | 0.010 |
| R-HSA-1236394 | Signaling by ERBB4 | 9.773862e-01 | 0.010 |
| R-HSA-8955332 | Carboxyterminal post-translational modifications of tubulin | 9.779582e-01 | 0.010 |
| R-HSA-2046104 | alpha-linolenic (omega3) and linoleic (omega6) acid metabolism | 9.779582e-01 | 0.010 |
| R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 9.781052e-01 | 0.010 |
| R-HSA-2730905 | Role of LAT2/NTAL/LAB on calcium mobilization | 9.785755e-01 | 0.009 |
| R-HSA-1296071 | Potassium Channels | 9.785755e-01 | 0.009 |
| R-HSA-8852135 | Protein ubiquitination | 9.786865e-01 | 0.009 |
| R-HSA-71403 | Citric acid cycle (TCA cycle) | 9.786865e-01 | 0.009 |
| R-HSA-8963899 | Plasma lipoprotein remodeling | 9.794377e-01 | 0.009 |
| R-HSA-389661 | Glyoxylate metabolism and glycine degradation | 9.808180e-01 | 0.008 |
| R-HSA-9694635 | Translation of Structural Proteins | 9.810734e-01 | 0.008 |
| R-HSA-192105 | Synthesis of bile acids and bile salts | 9.817547e-01 | 0.008 |
| R-HSA-2162123 | Synthesis of Prostaglandins (PG) and Thromboxanes (TX) | 9.821057e-01 | 0.008 |
| R-HSA-9748787 | Azathioprine ADME | 9.821057e-01 | 0.008 |
| R-HSA-383280 | Nuclear Receptor transcription pathway | 9.821675e-01 | 0.008 |
| R-HSA-9955298 | SLC-mediated transport of organic anions | 9.821675e-01 | 0.008 |
| R-HSA-5619084 | ABC transporter disorders | 9.821675e-01 | 0.008 |
| R-HSA-5358351 | Signaling by Hedgehog | 9.823146e-01 | 0.008 |
| R-HSA-5610787 | Hedgehog 'off' state | 9.827103e-01 | 0.008 |
| R-HSA-382556 | ABC-family proteins mediated transport | 9.827103e-01 | 0.008 |
| R-HSA-2514856 | The phototransduction cascade | 9.833070e-01 | 0.007 |
| R-HSA-202733 | Cell surface interactions at the vascular wall | 9.834662e-01 | 0.007 |
| R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 9.837376e-01 | 0.007 |
| R-HSA-9664422 | FCGR3A-mediated phagocytosis | 9.838942e-01 | 0.007 |
| R-HSA-9664417 | Leishmania phagocytosis | 9.838942e-01 | 0.007 |
| R-HSA-9664407 | Parasite infection | 9.838942e-01 | 0.007 |
| R-HSA-8866654 | E3 ubiquitin ligases ubiquitinate target proteins | 9.844277e-01 | 0.007 |
| R-HSA-9018677 | Biosynthesis of DHA-derived SPMs | 9.850938e-01 | 0.007 |
| R-HSA-977225 | Amyloid fiber formation | 9.850938e-01 | 0.007 |
| R-HSA-6809371 | Formation of the cornified envelope | 9.860096e-01 | 0.006 |
| R-HSA-9658195 | Leishmania infection | 9.866558e-01 | 0.006 |
| R-HSA-9824443 | Parasitic Infection Pathways | 9.866558e-01 | 0.006 |
| R-HSA-9833110 | RSV-host interactions | 9.868129e-01 | 0.006 |
| R-HSA-2871837 | FCERI mediated NF-kB activation | 9.872818e-01 | 0.006 |
| R-HSA-9753281 | Paracetamol ADME | 9.873587e-01 | 0.006 |
| R-HSA-209776 | Metabolism of amine-derived hormones | 9.882076e-01 | 0.005 |
| R-HSA-5621480 | Dectin-2 family | 9.889996e-01 | 0.005 |
| R-HSA-382551 | Transport of small molecules | 9.892145e-01 | 0.005 |
| R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 9.896116e-01 | 0.005 |
| R-HSA-1614635 | Sulfur amino acid metabolism | 9.896116e-01 | 0.005 |
| R-HSA-194068 | Bile acid and bile salt metabolism | 9.905091e-01 | 0.004 |
| R-HSA-977443 | GABA receptor activation | 9.910706e-01 | 0.004 |
| R-HSA-1660661 | Sphingolipid de novo biosynthesis | 9.910706e-01 | 0.004 |
| R-HSA-445717 | Aquaporin-mediated transport | 9.916705e-01 | 0.004 |
| R-HSA-8956321 | Nucleotide salvage | 9.916705e-01 | 0.004 |
| R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 9.918212e-01 | 0.004 |
| R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 9.932100e-01 | 0.003 |
| R-HSA-211981 | Xenobiotics | 9.932390e-01 | 0.003 |
| R-HSA-5690714 | CD22 mediated BCR regulation | 9.932390e-01 | 0.003 |
| R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 9.936123e-01 | 0.003 |
| R-HSA-5663205 | Infectious disease | 9.938413e-01 | 0.003 |
| R-HSA-6782315 | tRNA modification in the nucleus and cytosol | 9.941171e-01 | 0.003 |
| R-HSA-196807 | Nicotinate metabolism | 9.945124e-01 | 0.002 |
| R-HSA-196071 | Metabolism of steroid hormones | 9.945124e-01 | 0.002 |
| R-HSA-1643685 | Disease | 9.948827e-01 | 0.002 |
| R-HSA-597592 | Post-translational protein modification | 9.954512e-01 | 0.002 |
| R-HSA-3000178 | ECM proteoglycans | 9.958455e-01 | 0.002 |
| R-HSA-74259 | Purine catabolism | 9.961248e-01 | 0.002 |
| R-HSA-977606 | Regulation of Complement cascade | 9.963372e-01 | 0.002 |
| R-HSA-2187338 | Visual phototransduction | 9.965535e-01 | 0.001 |
| R-HSA-425397 | Transport of vitamins, nucleosides, and related molecules | 9.966283e-01 | 0.001 |
| R-HSA-446203 | Asparagine N-linked glycosylation | 9.975138e-01 | 0.001 |
| R-HSA-416476 | G alpha (q) signalling events | 9.975882e-01 | 0.001 |
| R-HSA-5579029 | Metabolic disorders of biological oxidation enzymes | 9.976193e-01 | 0.001 |
| R-HSA-390918 | Peroxisomal lipid metabolism | 9.983192e-01 | 0.001 |
| R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.984256e-01 | 0.001 |
| R-HSA-166663 | Initial triggering of complement | 9.985551e-01 | 0.001 |
| R-HSA-15869 | Metabolism of nucleotides | 9.988191e-01 | 0.001 |
| R-HSA-2980736 | Peptide hormone metabolism | 9.988759e-01 | 0.000 |
| R-HSA-8978868 | Fatty acid metabolism | 9.989976e-01 | 0.000 |
| R-HSA-71291 | Metabolism of amino acids and derivatives | 9.990011e-01 | 0.000 |
| R-HSA-9748784 | Drug ADME | 9.990764e-01 | 0.000 |
| R-HSA-166658 | Complement cascade | 9.990841e-01 | 0.000 |
| R-HSA-1474244 | Extracellular matrix organization | 9.991821e-01 | 0.000 |
| R-HSA-2142753 | Arachidonate metabolism | 9.993934e-01 | 0.000 |
| R-HSA-196854 | Metabolism of vitamins and cofactors | 9.995116e-01 | 0.000 |
| R-HSA-9009391 | Extra-nuclear estrogen signaling | 9.995829e-01 | 0.000 |
| R-HSA-1474228 | Degradation of the extracellular matrix | 9.996167e-01 | 0.000 |
| R-HSA-163125 | Post-translational modification: synthesis of GPI-anchored proteins | 9.996844e-01 | 0.000 |
| R-HSA-6803157 | Antimicrobial peptides | 9.998063e-01 | 0.000 |
| R-HSA-418555 | G alpha (s) signalling events | 9.998161e-01 | 0.000 |
| R-HSA-9018678 | Biosynthesis of specialized proresolving mediators (SPMs) | 9.998330e-01 | 0.000 |
| R-HSA-6805567 | Keratinization | 9.998845e-01 | 0.000 |
| R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 9.998935e-01 | 0.000 |
| R-HSA-156580 | Phase II - Conjugation of compounds | 9.999189e-01 | 0.000 |
| R-HSA-392499 | Metabolism of proteins | 9.999273e-01 | 0.000 |
| R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.999339e-01 | 0.000 |
| R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 9.999438e-01 | 0.000 |
| R-HSA-9824439 | Bacterial Infection Pathways | 9.999462e-01 | 0.000 |
| R-HSA-8956319 | Nucleotide catabolism | 9.999553e-01 | 0.000 |
| R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 9.999638e-01 | 0.000 |
| R-HSA-418594 | G alpha (i) signalling events | 9.999761e-01 | 0.000 |
| R-HSA-9664433 | Leishmania parasite growth and survival | 9.999775e-01 | 0.000 |
| R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 9.999775e-01 | 0.000 |
| R-HSA-5173105 | O-linked glycosylation | 9.999778e-01 | 0.000 |
| R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 9.999949e-01 | 0.000 |
| R-HSA-211897 | Cytochrome P450 - arranged by substrate type | 9.999975e-01 | 0.000 |
| R-HSA-388396 | GPCR downstream signalling | 9.999987e-01 | 0.000 |
| R-HSA-611105 | Respiratory electron transport | 9.999989e-01 | 0.000 |
| R-HSA-3781865 | Diseases of glycosylation | 9.999993e-01 | 0.000 |
| R-HSA-375276 | Peptide ligand-binding receptors | 9.999994e-01 | 0.000 |
| R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.999995e-01 | 0.000 |
| R-HSA-428157 | Sphingolipid metabolism | 9.999998e-01 | 0.000 |
| R-HSA-372790 | Signaling by GPCR | 1.000000e+00 | 0.000 |
| R-HSA-556833 | Metabolism of lipids | 1.000000e+00 | 0.000 |
| R-HSA-5668914 | Diseases of metabolism | 1.000000e+00 | 0.000 |
| R-HSA-211945 | Phase I - Functionalization of compounds | 1.000000e+00 | 0.000 |
| R-HSA-211859 | Biological oxidations | 1.000000e+00 | 0.000 |
| R-HSA-373076 | Class A/1 (Rhodopsin-like receptors) | 1.000000e+00 | 0.000 |
| R-HSA-9752946 | Expression and translocation of olfactory receptors | 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-9709957 | Sensory Perception | 1.000000e+00 | -0.000 |
| R-HSA-500792 | GPCR ligand binding | 1.000000e+00 | -0.000 |
Download
| kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
|---|---|---|---|---|
COT |
0.902 | 0.106 | 2 | 0.841 |
CLK3 |
0.894 | 0.229 | 1 | 0.896 |
FAM20C |
0.894 | 0.477 | 2 | 0.851 |
MARK4 |
0.892 | 0.305 | 4 | 0.926 |
CDC7 |
0.890 | 0.008 | 1 | 0.861 |
NLK |
0.888 | 0.119 | 1 | 0.912 |
PRPK |
0.888 | -0.075 | -1 | 0.878 |
MTOR |
0.887 | 0.004 | 1 | 0.863 |
CAMK1B |
0.887 | 0.079 | -3 | 0.897 |
MOS |
0.887 | 0.036 | 1 | 0.897 |
TBK1 |
0.886 | -0.006 | 1 | 0.805 |
RAF1 |
0.885 | -0.040 | 1 | 0.890 |
GCN2 |
0.885 | -0.121 | 2 | 0.760 |
PDHK4 |
0.885 | -0.082 | 1 | 0.907 |
NDR2 |
0.885 | 0.034 | -3 | 0.877 |
DSTYK |
0.885 | 0.023 | 2 | 0.862 |
PIM3 |
0.884 | 0.032 | -3 | 0.874 |
CDKL1 |
0.884 | 0.078 | -3 | 0.836 |
CAMK2G |
0.884 | 0.005 | 2 | 0.825 |
NUAK2 |
0.883 | 0.108 | -3 | 0.872 |
AMPKA1 |
0.883 | 0.173 | -3 | 0.885 |
BMPR2 |
0.882 | -0.057 | -2 | 0.939 |
PRKD1 |
0.882 | 0.101 | -3 | 0.850 |
IKKB |
0.882 | -0.088 | -2 | 0.805 |
HIPK4 |
0.881 | 0.135 | 1 | 0.869 |
PKN3 |
0.881 | 0.040 | -3 | 0.862 |
ULK2 |
0.881 | -0.137 | 2 | 0.748 |
TSSK1 |
0.880 | 0.200 | -3 | 0.903 |
ATR |
0.880 | 0.002 | 1 | 0.870 |
WNK1 |
0.880 | 0.043 | -2 | 0.909 |
MST4 |
0.880 | 0.062 | 2 | 0.807 |
IKKE |
0.880 | -0.053 | 1 | 0.802 |
ERK5 |
0.880 | 0.050 | 1 | 0.857 |
SKMLCK |
0.879 | 0.097 | -2 | 0.898 |
PDHK1 |
0.879 | -0.133 | 1 | 0.898 |
TGFBR2 |
0.879 | 0.013 | -2 | 0.866 |
NIK |
0.879 | 0.016 | -3 | 0.917 |
QSK |
0.878 | 0.254 | 4 | 0.923 |
TSSK2 |
0.878 | 0.162 | -5 | 0.891 |
CAMK2D |
0.878 | 0.087 | -3 | 0.872 |
SRPK1 |
0.878 | 0.116 | -3 | 0.781 |
CDKL5 |
0.878 | 0.069 | -3 | 0.825 |
NDR1 |
0.878 | 0.011 | -3 | 0.870 |
MARK2 |
0.878 | 0.321 | 4 | 0.886 |
RSK2 |
0.878 | 0.067 | -3 | 0.804 |
CAMLCK |
0.877 | 0.044 | -2 | 0.900 |
MARK3 |
0.877 | 0.312 | 4 | 0.917 |
RIPK3 |
0.877 | -0.045 | 3 | 0.808 |
PRKD2 |
0.877 | 0.088 | -3 | 0.797 |
KIS |
0.877 | 0.116 | 1 | 0.789 |
AMPKA2 |
0.876 | 0.148 | -3 | 0.852 |
NEK6 |
0.876 | -0.068 | -2 | 0.917 |
NIM1 |
0.876 | 0.084 | 3 | 0.832 |
PKCD |
0.876 | 0.058 | 2 | 0.749 |
P90RSK |
0.875 | 0.042 | -3 | 0.806 |
ICK |
0.875 | 0.086 | -3 | 0.869 |
NEK7 |
0.875 | -0.131 | -3 | 0.870 |
PIM1 |
0.875 | 0.078 | -3 | 0.817 |
DAPK2 |
0.875 | 0.029 | -3 | 0.901 |
SIK |
0.874 | 0.201 | -3 | 0.796 |
PKN2 |
0.874 | 0.010 | -3 | 0.869 |
CAMK2B |
0.874 | 0.142 | 2 | 0.833 |
LATS2 |
0.874 | 0.017 | -5 | 0.788 |
MLK1 |
0.873 | -0.110 | 2 | 0.771 |
RSK3 |
0.873 | 0.037 | -3 | 0.799 |
QIK |
0.873 | 0.136 | -3 | 0.866 |
HUNK |
0.873 | -0.095 | 2 | 0.755 |
WNK3 |
0.872 | -0.125 | 1 | 0.871 |
MAPKAPK3 |
0.872 | 0.029 | -3 | 0.807 |
CDK8 |
0.872 | 0.111 | 1 | 0.762 |
BCKDK |
0.872 | -0.111 | -1 | 0.830 |
NUAK1 |
0.872 | 0.092 | -3 | 0.825 |
SRPK2 |
0.871 | 0.102 | -3 | 0.706 |
IKKA |
0.871 | -0.032 | -2 | 0.794 |
LATS1 |
0.871 | 0.146 | -3 | 0.895 |
ATM |
0.871 | 0.052 | 1 | 0.807 |
MARK1 |
0.869 | 0.248 | 4 | 0.912 |
PKACG |
0.869 | 0.028 | -2 | 0.782 |
ULK1 |
0.868 | -0.193 | -3 | 0.847 |
MAPKAPK2 |
0.868 | 0.060 | -3 | 0.763 |
CHAK2 |
0.868 | -0.099 | -1 | 0.861 |
DYRK2 |
0.868 | 0.138 | 1 | 0.792 |
P70S6KB |
0.868 | 0.001 | -3 | 0.831 |
GRK1 |
0.868 | 0.004 | -2 | 0.816 |
GRK5 |
0.868 | -0.206 | -3 | 0.899 |
ANKRD3 |
0.868 | -0.100 | 1 | 0.904 |
GRK6 |
0.868 | -0.058 | 1 | 0.864 |
MASTL |
0.867 | -0.224 | -2 | 0.867 |
BRSK1 |
0.867 | 0.094 | -3 | 0.825 |
TGFBR1 |
0.867 | 0.097 | -2 | 0.868 |
MELK |
0.866 | 0.049 | -3 | 0.836 |
NEK9 |
0.866 | -0.157 | 2 | 0.781 |
BRSK2 |
0.866 | 0.089 | -3 | 0.848 |
BMPR1B |
0.866 | 0.119 | 1 | 0.798 |
SRPK3 |
0.866 | 0.076 | -3 | 0.757 |
CDK19 |
0.866 | 0.107 | 1 | 0.725 |
PRKD3 |
0.866 | 0.066 | -3 | 0.771 |
CAMK2A |
0.866 | 0.063 | 2 | 0.811 |
CLK4 |
0.865 | 0.117 | -3 | 0.799 |
RIPK1 |
0.865 | -0.133 | 1 | 0.863 |
ALK4 |
0.865 | 0.025 | -2 | 0.896 |
AURC |
0.865 | 0.061 | -2 | 0.696 |
CDK7 |
0.865 | 0.089 | 1 | 0.768 |
PKR |
0.864 | 0.006 | 1 | 0.884 |
MNK2 |
0.864 | 0.037 | -2 | 0.837 |
IRE1 |
0.864 | -0.094 | 1 | 0.833 |
CLK1 |
0.864 | 0.131 | -3 | 0.773 |
CAMK4 |
0.864 | -0.042 | -3 | 0.854 |
CDK5 |
0.863 | 0.132 | 1 | 0.781 |
MLK2 |
0.863 | -0.159 | 2 | 0.772 |
DNAPK |
0.862 | 0.094 | 1 | 0.775 |
PKCA |
0.862 | 0.015 | 2 | 0.688 |
JNK2 |
0.862 | 0.155 | 1 | 0.720 |
CDK18 |
0.862 | 0.138 | 1 | 0.697 |
DLK |
0.862 | -0.217 | 1 | 0.873 |
IRE2 |
0.862 | -0.053 | 2 | 0.710 |
MSK2 |
0.862 | 0.000 | -3 | 0.773 |
MLK3 |
0.862 | -0.075 | 2 | 0.708 |
P38A |
0.862 | 0.135 | 1 | 0.793 |
PLK1 |
0.862 | -0.056 | -2 | 0.873 |
PHKG1 |
0.861 | -0.028 | -3 | 0.860 |
CHK1 |
0.861 | 0.070 | -3 | 0.862 |
RSK4 |
0.861 | 0.059 | -3 | 0.774 |
PKCB |
0.861 | 0.000 | 2 | 0.693 |
PKCG |
0.861 | -0.018 | 2 | 0.698 |
PAK1 |
0.861 | -0.018 | -2 | 0.822 |
GRK4 |
0.860 | -0.161 | -2 | 0.866 |
TTBK2 |
0.860 | -0.198 | 2 | 0.674 |
PAK3 |
0.860 | -0.050 | -2 | 0.825 |
JNK3 |
0.860 | 0.129 | 1 | 0.753 |
CDK1 |
0.860 | 0.122 | 1 | 0.722 |
MEK1 |
0.860 | -0.117 | 2 | 0.797 |
CLK2 |
0.860 | 0.171 | -3 | 0.785 |
PLK3 |
0.860 | 0.006 | 2 | 0.775 |
MYLK4 |
0.860 | 0.042 | -2 | 0.816 |
AURB |
0.859 | 0.048 | -2 | 0.697 |
HIPK1 |
0.859 | 0.146 | 1 | 0.807 |
ALK2 |
0.859 | 0.082 | -2 | 0.873 |
CAMK1G |
0.858 | 0.052 | -3 | 0.794 |
SSTK |
0.858 | 0.161 | 4 | 0.897 |
MNK1 |
0.858 | 0.023 | -2 | 0.846 |
ACVR2A |
0.858 | 0.032 | -2 | 0.863 |
CDK13 |
0.858 | 0.073 | 1 | 0.745 |
VRK2 |
0.858 | -0.181 | 1 | 0.919 |
P38B |
0.858 | 0.143 | 1 | 0.724 |
MSK1 |
0.857 | 0.042 | -3 | 0.780 |
PKCH |
0.857 | -0.032 | 2 | 0.681 |
SGK3 |
0.857 | 0.051 | -3 | 0.791 |
ACVR2B |
0.856 | 0.027 | -2 | 0.871 |
NEK2 |
0.856 | -0.105 | 2 | 0.752 |
CDK17 |
0.856 | 0.123 | 1 | 0.646 |
YSK4 |
0.856 | -0.132 | 1 | 0.825 |
PKACB |
0.856 | 0.066 | -2 | 0.714 |
MLK4 |
0.856 | -0.106 | 2 | 0.693 |
DCAMKL1 |
0.856 | 0.039 | -3 | 0.816 |
HIPK2 |
0.856 | 0.141 | 1 | 0.709 |
PKCZ |
0.855 | -0.052 | 2 | 0.729 |
DYRK1A |
0.855 | 0.103 | 1 | 0.833 |
PAK6 |
0.855 | 0.018 | -2 | 0.757 |
ERK1 |
0.855 | 0.106 | 1 | 0.719 |
SMG1 |
0.855 | -0.047 | 1 | 0.820 |
GRK7 |
0.855 | 0.022 | 1 | 0.795 |
PLK4 |
0.855 | -0.057 | 2 | 0.604 |
AKT2 |
0.854 | 0.052 | -3 | 0.717 |
P38G |
0.854 | 0.127 | 1 | 0.642 |
PAK2 |
0.854 | -0.050 | -2 | 0.811 |
PKG2 |
0.854 | 0.028 | -2 | 0.713 |
CDK2 |
0.854 | 0.063 | 1 | 0.795 |
ERK2 |
0.854 | 0.078 | 1 | 0.766 |
PIM2 |
0.853 | 0.039 | -3 | 0.777 |
TLK2 |
0.853 | -0.084 | 1 | 0.842 |
CDK14 |
0.852 | 0.131 | 1 | 0.743 |
AURA |
0.852 | 0.032 | -2 | 0.671 |
SNRK |
0.852 | -0.129 | 2 | 0.649 |
CHAK1 |
0.852 | -0.174 | 2 | 0.713 |
HIPK3 |
0.852 | 0.098 | 1 | 0.814 |
WNK4 |
0.851 | -0.057 | -2 | 0.902 |
PERK |
0.851 | -0.109 | -2 | 0.901 |
DYRK4 |
0.851 | 0.139 | 1 | 0.721 |
BMPR1A |
0.851 | 0.096 | 1 | 0.780 |
CDK12 |
0.851 | 0.077 | 1 | 0.721 |
HRI |
0.851 | -0.133 | -2 | 0.915 |
CDK16 |
0.850 | 0.148 | 1 | 0.662 |
CDK9 |
0.850 | 0.056 | 1 | 0.753 |
PRKX |
0.850 | 0.080 | -3 | 0.708 |
DCAMKL2 |
0.850 | 0.012 | -3 | 0.840 |
DYRK1B |
0.850 | 0.125 | 1 | 0.748 |
BRAF |
0.850 | -0.072 | -4 | 0.865 |
PRP4 |
0.849 | 0.047 | -3 | 0.787 |
MAPKAPK5 |
0.849 | -0.078 | -3 | 0.751 |
CAMK1D |
0.849 | 0.080 | -3 | 0.716 |
MEKK1 |
0.849 | -0.128 | 1 | 0.865 |
PHKG2 |
0.849 | -0.010 | -3 | 0.828 |
CDK3 |
0.848 | 0.131 | 1 | 0.662 |
SMMLCK |
0.848 | 0.014 | -3 | 0.849 |
DYRK3 |
0.848 | 0.117 | 1 | 0.810 |
MEK5 |
0.848 | -0.226 | 2 | 0.779 |
MEKK2 |
0.847 | -0.095 | 2 | 0.758 |
PKCT |
0.847 | -0.015 | 2 | 0.689 |
ZAK |
0.847 | -0.141 | 1 | 0.835 |
NEK5 |
0.847 | -0.100 | 1 | 0.874 |
MEKK3 |
0.847 | -0.163 | 1 | 0.850 |
MST3 |
0.847 | -0.024 | 2 | 0.773 |
AKT1 |
0.846 | 0.061 | -3 | 0.735 |
DRAK1 |
0.846 | -0.120 | 1 | 0.792 |
IRAK4 |
0.846 | -0.104 | 1 | 0.845 |
TLK1 |
0.846 | -0.086 | -2 | 0.883 |
PINK1 |
0.845 | -0.149 | 1 | 0.879 |
P38D |
0.845 | 0.131 | 1 | 0.662 |
TAO3 |
0.845 | -0.039 | 1 | 0.848 |
MPSK1 |
0.844 | 0.034 | 1 | 0.816 |
CDK10 |
0.844 | 0.115 | 1 | 0.728 |
GRK2 |
0.843 | -0.097 | -2 | 0.753 |
PKACA |
0.843 | 0.053 | -2 | 0.663 |
PKCI |
0.842 | -0.021 | 2 | 0.697 |
P70S6K |
0.841 | -0.027 | -3 | 0.738 |
GAK |
0.840 | 0.001 | 1 | 0.865 |
CK1E |
0.840 | -0.049 | -3 | 0.578 |
DAPK3 |
0.839 | 0.048 | -3 | 0.833 |
PASK |
0.839 | -0.048 | -3 | 0.886 |
ERK7 |
0.839 | 0.018 | 2 | 0.510 |
IRAK1 |
0.839 | -0.174 | -1 | 0.769 |
TAO2 |
0.839 | -0.079 | 2 | 0.801 |
PKCE |
0.838 | 0.016 | 2 | 0.680 |
GSK3A |
0.838 | -0.002 | 4 | 0.403 |
TTBK1 |
0.838 | -0.167 | 2 | 0.604 |
NEK8 |
0.838 | -0.161 | 2 | 0.766 |
GSK3B |
0.837 | -0.053 | 4 | 0.396 |
CAMK1A |
0.837 | 0.083 | -3 | 0.680 |
PDK1 |
0.837 | -0.056 | 1 | 0.864 |
NEK11 |
0.836 | -0.173 | 1 | 0.855 |
GCK |
0.835 | -0.014 | 1 | 0.855 |
PKN1 |
0.835 | 0.004 | -3 | 0.752 |
MAK |
0.835 | 0.147 | -2 | 0.766 |
MST2 |
0.835 | -0.060 | 1 | 0.856 |
NEK4 |
0.835 | -0.098 | 1 | 0.849 |
PAK5 |
0.834 | -0.027 | -2 | 0.687 |
TNIK |
0.834 | 0.005 | 3 | 0.879 |
MINK |
0.834 | -0.014 | 1 | 0.851 |
HGK |
0.834 | -0.031 | 3 | 0.880 |
LKB1 |
0.834 | -0.107 | -3 | 0.864 |
JNK1 |
0.834 | 0.085 | 1 | 0.702 |
CAMKK1 |
0.834 | -0.196 | -2 | 0.815 |
CHK2 |
0.833 | 0.024 | -3 | 0.660 |
CK1G1 |
0.833 | -0.068 | -3 | 0.580 |
MAP3K15 |
0.833 | -0.071 | 1 | 0.824 |
MOK |
0.833 | 0.128 | 1 | 0.804 |
CDK6 |
0.833 | 0.083 | 1 | 0.725 |
MEKK6 |
0.832 | -0.099 | 1 | 0.844 |
PLK2 |
0.832 | 0.008 | -3 | 0.839 |
SGK1 |
0.832 | 0.056 | -3 | 0.635 |
EEF2K |
0.832 | -0.071 | 3 | 0.853 |
CAMKK2 |
0.832 | -0.155 | -2 | 0.814 |
CK1D |
0.832 | -0.037 | -3 | 0.526 |
AKT3 |
0.831 | 0.048 | -3 | 0.650 |
CK2A2 |
0.831 | 0.060 | 1 | 0.708 |
NEK1 |
0.831 | -0.061 | 1 | 0.853 |
CDK4 |
0.831 | 0.080 | 1 | 0.708 |
DAPK1 |
0.830 | 0.013 | -3 | 0.813 |
HPK1 |
0.830 | -0.015 | 1 | 0.844 |
MRCKA |
0.830 | 0.040 | -3 | 0.788 |
ROCK2 |
0.830 | 0.062 | -3 | 0.818 |
MRCKB |
0.830 | 0.041 | -3 | 0.768 |
PAK4 |
0.830 | -0.029 | -2 | 0.695 |
LRRK2 |
0.830 | -0.144 | 2 | 0.796 |
TAK1 |
0.829 | -0.123 | 1 | 0.873 |
KHS1 |
0.828 | 0.018 | 1 | 0.845 |
CK1A2 |
0.828 | -0.049 | -3 | 0.524 |
LOK |
0.827 | -0.084 | -2 | 0.822 |
SBK |
0.827 | 0.063 | -3 | 0.594 |
GRK3 |
0.827 | -0.097 | -2 | 0.703 |
BUB1 |
0.827 | 0.085 | -5 | 0.864 |
KHS2 |
0.827 | 0.037 | 1 | 0.856 |
MST1 |
0.827 | -0.085 | 1 | 0.844 |
PDHK3_TYR |
0.826 | 0.148 | 4 | 0.852 |
VRK1 |
0.826 | -0.174 | 2 | 0.777 |
YSK1 |
0.824 | -0.075 | 2 | 0.752 |
DMPK1 |
0.824 | 0.087 | -3 | 0.789 |
MEK2 |
0.822 | -0.214 | 2 | 0.759 |
PBK |
0.821 | -0.024 | 1 | 0.787 |
CK2A1 |
0.820 | 0.034 | 1 | 0.686 |
STK33 |
0.820 | -0.184 | 2 | 0.604 |
RIPK2 |
0.820 | -0.242 | 1 | 0.795 |
TTK |
0.820 | -0.002 | -2 | 0.882 |
SLK |
0.820 | -0.126 | -2 | 0.763 |
NEK3 |
0.819 | -0.117 | 1 | 0.823 |
ROCK1 |
0.817 | 0.044 | -3 | 0.784 |
TESK1_TYR |
0.817 | -0.054 | 3 | 0.914 |
PDHK4_TYR |
0.816 | 0.042 | 2 | 0.851 |
PKG1 |
0.816 | -0.006 | -2 | 0.622 |
MAP2K4_TYR |
0.815 | -0.061 | -1 | 0.900 |
PKMYT1_TYR |
0.815 | -0.029 | 3 | 0.890 |
CRIK |
0.815 | 0.044 | -3 | 0.731 |
MAP2K7_TYR |
0.814 | -0.118 | 2 | 0.826 |
MAP2K6_TYR |
0.814 | -0.036 | -1 | 0.895 |
HASPIN |
0.813 | -0.023 | -1 | 0.716 |
BMPR2_TYR |
0.813 | -0.001 | -1 | 0.881 |
BIKE |
0.812 | 0.015 | 1 | 0.735 |
LIMK2_TYR |
0.812 | -0.009 | -3 | 0.923 |
OSR1 |
0.811 | -0.132 | 2 | 0.748 |
PDHK1_TYR |
0.810 | -0.072 | -1 | 0.898 |
MYO3B |
0.810 | -0.069 | 2 | 0.769 |
ASK1 |
0.809 | -0.127 | 1 | 0.810 |
PINK1_TYR |
0.809 | -0.196 | 1 | 0.879 |
EPHA6 |
0.809 | 0.016 | -1 | 0.857 |
MYO3A |
0.808 | -0.079 | 1 | 0.844 |
RET |
0.807 | -0.085 | 1 | 0.858 |
TAO1 |
0.807 | -0.103 | 1 | 0.789 |
ALPHAK3 |
0.806 | -0.048 | -1 | 0.783 |
TYK2 |
0.806 | -0.106 | 1 | 0.856 |
LIMK1_TYR |
0.806 | -0.138 | 2 | 0.813 |
MST1R |
0.805 | -0.094 | 3 | 0.852 |
ROS1 |
0.805 | -0.079 | 3 | 0.823 |
YANK3 |
0.804 | -0.084 | 2 | 0.424 |
TYRO3 |
0.804 | -0.099 | 3 | 0.843 |
DDR1 |
0.803 | -0.081 | 4 | 0.800 |
EPHB4 |
0.803 | -0.038 | -1 | 0.839 |
JAK2 |
0.803 | -0.095 | 1 | 0.857 |
CSF1R |
0.802 | -0.064 | 3 | 0.833 |
ABL2 |
0.801 | -0.019 | -1 | 0.817 |
YES1 |
0.800 | -0.026 | -1 | 0.846 |
INSRR |
0.799 | -0.039 | 3 | 0.804 |
TXK |
0.799 | 0.030 | 1 | 0.840 |
JAK3 |
0.798 | -0.103 | 1 | 0.835 |
FGR |
0.798 | -0.101 | 1 | 0.867 |
TNNI3K_TYR |
0.797 | -0.007 | 1 | 0.864 |
HCK |
0.797 | -0.043 | -1 | 0.824 |
FER |
0.796 | -0.118 | 1 | 0.882 |
AAK1 |
0.796 | 0.057 | 1 | 0.628 |
ABL1 |
0.796 | -0.053 | -1 | 0.811 |
EPHA4 |
0.796 | -0.030 | 2 | 0.777 |
LCK |
0.796 | 0.006 | -1 | 0.823 |
FGFR2 |
0.796 | -0.079 | 3 | 0.843 |
TNK2 |
0.795 | -0.073 | 3 | 0.807 |
BLK |
0.795 | 0.045 | -1 | 0.827 |
JAK1 |
0.795 | -0.035 | 1 | 0.808 |
PDGFRB |
0.794 | -0.134 | 3 | 0.850 |
SRMS |
0.794 | -0.057 | 1 | 0.861 |
ITK |
0.793 | -0.072 | -1 | 0.801 |
FGFR1 |
0.793 | -0.090 | 3 | 0.820 |
TEK |
0.793 | -0.096 | 3 | 0.786 |
EPHB1 |
0.793 | -0.088 | 1 | 0.861 |
STLK3 |
0.793 | -0.223 | 1 | 0.800 |
KDR |
0.793 | -0.099 | 3 | 0.807 |
TNK1 |
0.793 | -0.091 | 3 | 0.824 |
FLT3 |
0.793 | -0.122 | 3 | 0.834 |
NEK10_TYR |
0.792 | -0.097 | 1 | 0.742 |
KIT |
0.792 | -0.116 | 3 | 0.833 |
EPHB2 |
0.791 | -0.044 | -1 | 0.815 |
EPHB3 |
0.791 | -0.084 | -1 | 0.821 |
AXL |
0.790 | -0.114 | 3 | 0.827 |
MERTK |
0.790 | -0.082 | 3 | 0.821 |
TEC |
0.788 | -0.074 | -1 | 0.747 |
CK1A |
0.787 | -0.095 | -3 | 0.434 |
BMX |
0.787 | -0.061 | -1 | 0.724 |
PDGFRA |
0.787 | -0.202 | 3 | 0.846 |
ALK |
0.787 | -0.132 | 3 | 0.772 |
BTK |
0.787 | -0.149 | -1 | 0.772 |
DDR2 |
0.786 | 0.002 | 3 | 0.791 |
MET |
0.786 | -0.135 | 3 | 0.827 |
LTK |
0.785 | -0.121 | 3 | 0.790 |
FYN |
0.785 | 0.003 | -1 | 0.797 |
EPHA7 |
0.785 | -0.060 | 2 | 0.774 |
FGFR3 |
0.784 | -0.108 | 3 | 0.818 |
WEE1_TYR |
0.784 | -0.137 | -1 | 0.765 |
EPHA1 |
0.783 | -0.096 | 3 | 0.804 |
EPHA3 |
0.783 | -0.120 | 2 | 0.749 |
NTRK1 |
0.783 | -0.181 | -1 | 0.825 |
LYN |
0.782 | -0.056 | 3 | 0.764 |
INSR |
0.782 | -0.123 | 3 | 0.779 |
ERBB2 |
0.782 | -0.163 | 1 | 0.801 |
FRK |
0.781 | -0.109 | -1 | 0.835 |
FLT1 |
0.781 | -0.148 | -1 | 0.829 |
NTRK2 |
0.780 | -0.189 | 3 | 0.808 |
FLT4 |
0.780 | -0.174 | 3 | 0.801 |
PTK6 |
0.780 | -0.243 | -1 | 0.735 |
PTK2B |
0.779 | -0.068 | -1 | 0.783 |
EPHA5 |
0.778 | -0.052 | 2 | 0.772 |
NTRK3 |
0.775 | -0.164 | -1 | 0.776 |
EGFR |
0.775 | -0.073 | 1 | 0.705 |
EPHA8 |
0.774 | -0.090 | -1 | 0.795 |
SRC |
0.774 | -0.089 | -1 | 0.799 |
MATK |
0.773 | -0.157 | -1 | 0.742 |
PTK2 |
0.772 | -0.019 | -1 | 0.778 |
YANK2 |
0.772 | -0.108 | 2 | 0.447 |
FGFR4 |
0.770 | -0.094 | -1 | 0.771 |
CSK |
0.770 | -0.170 | 2 | 0.770 |
CK1G3 |
0.768 | -0.092 | -3 | 0.385 |
IGF1R |
0.766 | -0.138 | 3 | 0.721 |
EPHA2 |
0.765 | -0.088 | -1 | 0.766 |
SYK |
0.765 | -0.056 | -1 | 0.764 |
ERBB4 |
0.760 | -0.080 | 1 | 0.709 |
MUSK |
0.759 | -0.201 | 1 | 0.690 |
FES |
0.750 | -0.173 | -1 | 0.704 |
CK1G2 |
0.745 | -0.114 | -3 | 0.489 |
ZAP70 |
0.738 | -0.116 | -1 | 0.695 |