Motif 480 (n=1,210)

Position-wise Probabilities

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uniprot	genes	site	source	protein	function
A0A0C4DFX4	None	S229	ochoa	Snf2 related CREBBP activator protein	None
A0A0C4DFX4	None	S2610	ochoa	Snf2 related CREBBP activator protein	None
A0MZ66	SHTN1	S492	ochoa	Shootin-1 (Shootin1)	Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons. {ECO:0000250\|UniProtKB:A0MZ67, ECO:0000250\|UniProtKB:Q8K2Q9}.
A3KN83	SBNO1	S807	ochoa	Protein strawberry notch homolog 1 (Monocyte protein 3) (MOP-3)	Plays a crucial role in the regulation of neural stem cells (NSCs) proliferation. Enhances the phosphorylation of GSK3B through the PI3K-Akt signaling pathway, thereby upregulating the Wnt/beta-catenin signaling pathway and promoting the proliferation of NSCs. Improves ischemic stroke recovery while inhibiting neuroinflammation through small extracellular vesicles (sEVs)-mediated mechanism. Enhances the secretion of sEVs from NSCs, which in turn inhibit both the MAPK and NF-kappaB pathways in microglia. This inhibition suppresses the pro-inflammatory M1 polarization of microglia, promoting a shift towards the M2 anti-inflammatory phenotype, which is beneficial for reducing neuroinflammation. {ECO:0000250\|UniProtKB:Q689Z5}.
A6NKD9	CCDC85C	S206	ochoa	Coiled-coil domain-containing protein 85C	May play a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family (Probable). May play an important role in cortical development, especially in the maintenance of radial glia (By similarity). {ECO:0000250\|UniProtKB:E9Q6B2, ECO:0000305\|PubMed:25009281}.
A6NKT7	RGPD3	S1472	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A6NKT7	RGPD3	S1573	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A6NKT7	RGPD3	S1583	ochoa	RanBP2-like and GRIP domain-containing protein 3	None
A7E2V4	ZSWIM8	S1146	ochoa	Zinc finger SWIM domain-containing protein 8	Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184234, PubMed:33184237). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237). Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target (PubMed:33184234). May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation (PubMed:24012004). Plays an essential role for proper embryonic development of heart and lung (By similarity). Controls protein quality of DAB1, a key signal molecule for brain development, thus protecting its signaling strength. Mechanistically, recognizes intrinsically disordered regions of DAB1 and eliminates misfolded DAB1 that cannot be properly phosphorylated (By similarity). {ECO:0000250\|UniProtKB:Q3UHH1, ECO:0000269\|PubMed:24012004, ECO:0000269\|PubMed:33184234, ECO:0000269\|PubMed:33184237}.; FUNCTION: (Microbial infection) Participates in Zika virus inhibition of IFN signaling by acting as a scaffold protein to connect ZSWIM8/CUL3 ligase complex and STAT2, leading to STAT2 degradation. {ECO:0000269\|PubMed:39145933}.
A8CG34	POM121C	S348	ochoa	Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)	Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269\|PubMed:17900573}.
A8MVS5	HIDE1	S203	ochoa	Protein HIDE1	None
A8MVS5	HIDE1	S205	ochoa	Protein HIDE1	None
H0YC42	None	S134	ochoa	Tumor protein D52	None
O00273	DFFA	S305	ochoa	DNA fragmentation factor subunit alpha (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) (ICAD)	Inhibitor of the caspase-activated DNase (DFF40).
O00418	EEF2K	Y60	ochoa	Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269\|PubMed:14709557, ECO:0000269\|PubMed:9144159}.
O00418	EEF2K	S61	psp	Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269\|PubMed:14709557, ECO:0000269\|PubMed:9144159}.
O00418	EEF2K	S464	ochoa	Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269\|PubMed:14709557, ECO:0000269\|PubMed:9144159}.
O00571	DDX3X	S76	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S584	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S605	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S606	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O00571	DDX3X	S609	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O14513	NCKAP5	S1277	ochoa	Nck-associated protein 5 (NAP-5) (Peripheral clock protein)	None
O14639	ABLIM1	S352	ochoa	Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin)	May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269\|PubMed:9245787}.
O14639	ABLIM1	S353	ochoa	Actin-binding LIM protein 1 (abLIM-1) (Actin-binding LIM protein family member 1) (Actin-binding double zinc finger protein) (LIMAB1) (Limatin)	May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269\|PubMed:9245787}.
O14646	CHD1	S1090	ochoa	Chromodomain-helicase-DNA-binding protein 1 (CHD-1) (EC 3.6.4.-) (ATP-dependent helicase CHD1)	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). {ECO:0000250\|UniProtKB:P40201, ECO:0000269\|PubMed:18042460, ECO:0000269\|PubMed:28866611}.
O14646	CHD1	S1371	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}.
O14681	EI24	Y310	ochoa	Etoposide-induced protein 2.4 homolog (p53-induced gene 8 protein)	Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.
O14681	EI24	S316	ochoa	Etoposide-induced protein 2.4 homolog (p53-induced gene 8 protein)	Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.
O14715	RGPD8	S1471	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14715	RGPD8	S1572	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14715	RGPD8	S1582	ochoa	RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3)	None
O14745	NHERF1	S280	ochoa\|psp	Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1)	Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269\|PubMed:10499588, ECO:0000269\|PubMed:18784102, ECO:0000269\|PubMed:9096337, ECO:0000269\|PubMed:9430655}.
O14757	CHEK1	S307	ochoa	Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758). {ECO:0000250\|UniProtKB:O35280, ECO:0000269\|PubMed:10673501, ECO:0000269\|PubMed:11535615, ECO:0000269\|PubMed:12399544, ECO:0000269\|PubMed:12446774, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12676583, ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:12759351, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:14681206, ECO:0000269\|PubMed:14988723, ECO:0000269\|PubMed:15311285, ECO:0000269\|PubMed:15650047, ECO:0000269\|PubMed:15659650, ECO:0000269\|PubMed:15665856, ECO:0000269\|PubMed:16511572, ECO:0000269\|PubMed:17296736, ECO:0000269\|PubMed:17380128, ECO:0000269\|PubMed:18451105, ECO:0000269\|PubMed:18728393, ECO:0000269\|PubMed:19734889, ECO:0000269\|PubMed:20090422, ECO:0000269\|PubMed:31316063, ECO:0000269\|PubMed:32357935, ECO:0000269\|PubMed:33108758, ECO:0000269\|PubMed:9278511}.; FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition. {ECO:0000269\|PubMed:22184239}.
O14777	NDC80	S66	ochoa	Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC)	Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327, PubMed:30409912, PubMed:9315664). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592, PubMed:30409912). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules (PubMed:23891108, PubMed:25743205). {ECO:0000269\|PubMed:12351790, ECO:0000269\|PubMed:14654001, ECO:0000269\|PubMed:14699129, ECO:0000269\|PubMed:15062103, ECO:0000269\|PubMed:15235793, ECO:0000269\|PubMed:15239953, ECO:0000269\|PubMed:15548592, ECO:0000269\|PubMed:16732327, ECO:0000269\|PubMed:23085020, ECO:0000269\|PubMed:23891108, ECO:0000269\|PubMed:25743205, ECO:0000269\|PubMed:30409912, ECO:0000269\|PubMed:9315664}.
O14917	PCDH17	S1026	ochoa	Protocadherin-17 (Protocadherin-68)	Potential calcium-dependent cell-adhesion protein.
O14920	IKBKB	S679	ochoa	Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697). {ECO:0000250\|UniProtKB:O88351, ECO:0000269\|PubMed:11297557, ECO:0000269\|PubMed:14673179, ECO:0000269\|PubMed:15084260, ECO:0000269\|PubMed:17213322, ECO:0000269\|PubMed:19716809, ECO:0000269\|PubMed:20410276, ECO:0000269\|PubMed:20434986, ECO:0000269\|PubMed:20797629, ECO:0000269\|PubMed:21138416, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:30337470, ECO:0000269\|PubMed:32209697, ECO:0000269\|PubMed:38621137, ECO:0000269\|PubMed:9346484}.
O14974	PPP1R12A	S886	ochoa	Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269\|PubMed:18477460, ECO:0000269\|PubMed:19245366, ECO:0000269\|PubMed:20354225}.
O15013	ARHGEF10	S1279	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15013	ARHGEF10	S1282	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15013	ARHGEF10	S1284	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15056	SYNJ2	S1433	ochoa	Synaptojanin-2 (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2)	Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis.
O15061	SYNM	S1153	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	S946	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}.
O15068	MCF2L	S963	ochoa	Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein)	Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42 (PubMed:15157669). {ECO:0000250\|UniProtKB:Q63406, ECO:0000269\|PubMed:15157669}.; FUNCTION: [Isoform 3]: Does not catalyze guanine nucleotide exchange on CDC42 (PubMed:15157669). {ECO:0000269\|PubMed:15157669}.
O15085	ARHGEF11	S232	ochoa	Rho guanine nucleotide exchange factor 11 (PDZ-RhoGEF)	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269\|PubMed:21670212}.
O15211	RGL2	S581	ochoa	Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) (RalGDS-like factor) (Ras-associated protein RAB2L)	Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity). {ECO:0000250}.
O15400	STX7	S137	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.
O15403	SLC16A6	S237	ochoa	Monocarboxylate transporter 7 (MCT 7) (Monocarboxylate transporter 6) (MCT 6) (Solute carrier family 16 member 6)	Monocarboxylate transporter selective for taurine. May associate with BSG/CD147 or EMB/GP70 ancillary proteins to mediate facilitative efflux or influx of taurine across the plasma membrane. The transport is pH- and sodium-independent. Rather low-affinity, is likely effective for taurine transport in tissues where taurine is present at high concentrations. {ECO:0000250\|UniProtKB:Q7TMR7}.
O15516	CLOCK	S427	ochoa\|psp	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O15516	CLOCK	S431	psp	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O15516	CLOCK	S437	psp	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O15516	CLOCK	S440	ochoa	Circadian locomoter output cycles protein kaput (hCLOCK) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 8) (bHLHe8)	Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). {ECO:0000250\|UniProtKB:O08785, ECO:0000269\|PubMed:14645221, ECO:0000269\|PubMed:18587630, ECO:0000269\|PubMed:21659603, ECO:0000269\|PubMed:21980503, ECO:0000269\|PubMed:22284746, ECO:0000269\|PubMed:23229515, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24005054, ECO:0000269\|PubMed:28985504}.
O43166	SIPA1L1	S1454	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43166	SIPA1L1	S1462	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43166	SIPA1L1	S1639	ochoa	Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)	Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.
O43182	ARHGAP6	S328	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43182	ARHGAP6	S330	ochoa	Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269\|PubMed:10699171}.
O43353	RIPK2	S168	ochoa	Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)	Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269\|PubMed:14638696, ECO:0000269\|PubMed:17054981, ECO:0000269\|PubMed:17562858, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:21123652, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:22607974, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:28545134, ECO:0000269\|PubMed:28656966, ECO:0000269\|PubMed:29452636, ECO:0000269\|PubMed:30026309, ECO:0000269\|PubMed:30279485, ECO:0000269\|PubMed:30478312, ECO:0000269\|PubMed:9575181, ECO:0000269\|PubMed:9642260}.
O43524	FOXO3	S311	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43524	FOXO3	S432	ochoa	Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)	Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250\|UniProtKB:Q9WVH4, ECO:0000269\|PubMed:10102273, ECO:0000269\|PubMed:16751106, ECO:0000269\|PubMed:21329882, ECO:0000269\|PubMed:23283301, ECO:0000269\|PubMed:30513302}.
O43566	RGS14	S42	ochoa	Regulator of G-protein signaling 14 (RGS14)	Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. May be involved in visual memory processing capacity and hippocampal-based learning and memory. {ECO:0000269\|PubMed:15917656, ECO:0000269\|PubMed:17635935}.
O43663	PRC1	S577	psp	Protein regulator of cytokinesis 1	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269\|PubMed:12082078, ECO:0000269\|PubMed:15297875, ECO:0000269\|PubMed:15625105, ECO:0000269\|PubMed:16431929, ECO:0000269\|PubMed:17409436, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:20691902, ECO:0000269\|PubMed:9885575}.
O43741	PRKAB2	S174	ochoa	5'-AMP-activated protein kinase subunit beta-2 (AMPK subunit beta-2)	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).
O60245	PCDH7	S966	ochoa	Protocadherin-7 (Brain-heart protocadherin) (BH-Pcdh)	None
O60307	MAST3	S1091	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60307	MAST3	S1093	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60315	ZEB2	S840	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}.
O60315	ZEB2	S841	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}.
O60315	ZEB2	S843	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}.
O60346	PHLPP1	S131	ochoa	PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) (hSCOP)	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 AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). 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 suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). 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 (PubMed:19079341). Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). May act as a negative regulator of K-Ras signaling in membrane rafts (By similarity). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T-cells (By similarity). {ECO:0000250\|UniProtKB:Q8CHE4, ECO:0000250\|UniProtKB:Q9WTR8, ECO:0000269\|PubMed:15808505, ECO:0000269\|PubMed:17386267, ECO:0000269\|PubMed:18162466, ECO:0000269\|PubMed:19079341, ECO:0000269\|PubMed:21986499, ECO:0000269\|PubMed:24530606}.
O60346	PHLPP1	S139	ochoa	PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) (hSCOP)	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 AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). 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 suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). 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 (PubMed:19079341). Dephosphorylates RAF1 inhibiting its kinase activity (PubMed:24530606). May act as a negative regulator of K-Ras signaling in membrane rafts (By similarity). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T-cells (By similarity). {ECO:0000250\|UniProtKB:Q8CHE4, ECO:0000250\|UniProtKB:Q9WTR8, ECO:0000269\|PubMed:15808505, ECO:0000269\|PubMed:17386267, ECO:0000269\|PubMed:18162466, ECO:0000269\|PubMed:19079341, ECO:0000269\|PubMed:21986499, ECO:0000269\|PubMed:24530606}.
O60664	PLIN3	S374	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}.
O75044	SRGAP2	S854	ochoa	SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)	Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250\|UniProtKB:Q91Z67, ECO:0000269\|PubMed:20810653, ECO:0000269\|PubMed:21148482, ECO:0000269\|PubMed:22559944, ECO:0000269\|PubMed:27373832, ECO:0000269\|PubMed:28333212}.
O75122	CLASP2	S313	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S316	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S320	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S993	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S1003	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75128	COBL	S741	ochoa	Protein cordon-bleu	Plays an important role in the reorganization of the actin cytoskeleton. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells (By similarity). Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. {ECO:0000250, ECO:0000269\|PubMed:21816349}.
O75381	PEX14	S261	ochoa	Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14)	Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:24235149, PubMed:28765278, PubMed:9653144). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role for peroxisome movement through a direct interaction with tubulin (PubMed:21525035). {ECO:0000250\|UniProtKB:P53112, ECO:0000269\|PubMed:21525035, ECO:0000269\|PubMed:24235149, ECO:0000269\|PubMed:28765278, ECO:0000269\|PubMed:9653144}.
O75385	ULK1	S403	ochoa	Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1)	Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708). {ECO:0000269\|PubMed:11146101, ECO:0000269\|PubMed:18936157, ECO:0000269\|PubMed:20921139, ECO:0000269\|PubMed:21460634, ECO:0000269\|PubMed:21795849, ECO:0000269\|PubMed:23524951, ECO:0000269\|PubMed:25040165, ECO:0000269\|PubMed:25126726, ECO:0000269\|PubMed:28821708, ECO:0000269\|PubMed:29487085, ECO:0000269\|PubMed:31123703, ECO:0000269\|PubMed:37306101}.
O75473	LGR5	S844	psp	Leucine-rich repeat-containing G-protein coupled receptor 5 (G-protein coupled receptor 49) (G-protein coupled receptor 67) (G-protein coupled receptor HG38)	Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269\|PubMed:21693646, ECO:0000269\|PubMed:21727895, ECO:0000269\|PubMed:21909076, ECO:0000269\|PubMed:22815884, ECO:0000269\|PubMed:23809763}.
O75473	LGR5	S851	psp	Leucine-rich repeat-containing G-protein coupled receptor 5 (G-protein coupled receptor 49) (G-protein coupled receptor 67) (G-protein coupled receptor HG38)	Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269\|PubMed:21693646, ECO:0000269\|PubMed:21727895, ECO:0000269\|PubMed:21909076, ECO:0000269\|PubMed:22815884, ECO:0000269\|PubMed:23809763}.
O75626	PRDM1	S341	ochoa	PR domain zinc finger protein 1 (EC 2.1.1.-) (BLIMP-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) (Positive regulatory domain I-binding factor 1) (PRDI-BF1) (PRDI-binding factor 1)	Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (By similarity). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (PubMed:1851123). Drives the maturation of B-lymphocytes into Ig secreting cells (PubMed:12626569). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (By similarity). Binds to the promoter and acts as a transcriptional repressor of IRF8, thereby promotes transcription of osteoclast differentiation factors such as NFATC1 and EEIG1 (By similarity). {ECO:0000250\|UniProtKB:Q60636, ECO:0000269\|PubMed:12626569, ECO:0000269\|PubMed:1851123}.
O75674	TOM1L1	S311	ochoa	TOM1-like protein 1 (Src-activating and signaling molecule protein) (Target of Myb-like protein 1)	Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.
O75970	MPDZ	S1585	ochoa	Multiple PDZ domain protein (Multi-PDZ domain protein 1)	Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of HT2RC at the cell surface (By similarity). {ECO:0000250\|UniProtKB:O55164, ECO:0000269\|PubMed:11150294, ECO:0000269\|PubMed:15312654}.
O76094	SRP72	S611	ochoa	Signal recognition particle subunit SRP72 (SRP72) (Signal recognition particle 72 kDa protein)	Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68 (PubMed:21073748, PubMed:27899666). Can bind 7SL RNA with low affinity (PubMed:21073748, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity). {ECO:0000250\|UniProtKB:P38688, ECO:0000269\|PubMed:21073748, ECO:0000269\|PubMed:27899666, ECO:0000269\|PubMed:34020957}.
O94804	STK10	S438	ochoa	Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269\|PubMed:11903060, ECO:0000269\|PubMed:12639966, ECO:0000269\|PubMed:19255442}.
O94875	SORBS2	S235	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94875	SORBS2	S278	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94875	SORBS2	S288	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94875	SORBS2	S1015	ochoa	Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Sorbin)	Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269\|PubMed:12475393, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:9211900}.
O94887	FARP2	S425	ochoa	FERM, ARHGEF and pleckstrin domain-containing protein 2 (FERM domain-including RhoGEF) (FIR) (FERM, RhoGEF and pleckstrin domain-containing protein 2) (Pleckstrin homology domain-containing family C member 3) (PH domain-containing family C member 3)	Functions as a guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity). {ECO:0000250}.
O94915	FRYL	S1935	ochoa	Protein furry homolog-like (ALL1-fused gene from chromosome 4p12 protein)	Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269\|PubMed:16061630}.
O94915	FRYL	S2330	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}.
O95155	UBE4B	S76	ochoa	Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250\|UniProtKB:P54860, ECO:0000250\|UniProtKB:Q9ES00, ECO:0000269\|PubMed:17369820}.
O95155	UBE4B	S78	ochoa	Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (Homozygously deleted in neuroblastoma 1) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2)	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). {ECO:0000250\|UniProtKB:P54860, ECO:0000250\|UniProtKB:Q9ES00, ECO:0000269\|PubMed:17369820}.
O95208	EPN2	S476	ochoa	Epsin-2 (EPS-15-interacting protein 2)	Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269\|PubMed:10567358}.
O95249	GOSR1	S41	ochoa	Golgi SNAP receptor complex member 1 (28 kDa Golgi SNARE protein) (28 kDa cis-Golgi SNARE p28) (GOS-28)	Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. {ECO:0000269\|PubMed:15215310, ECO:0000269\|PubMed:21860593}.
O95251	KAT7	S46	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}.
O95297	MPZL1	Y200	ochoa	Myelin protein zero-like protein 1 (Protein zero-related)	Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269\|PubMed:11751924, ECO:0000269\|PubMed:12410637}.
O95425	SVIL	S221	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95613	PCNT	S2342	ochoa	Pericentrin (Kendrin) (Pericentrin-B)	Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269\|PubMed:10823944, ECO:0000269\|PubMed:11171385, ECO:0000269\|PubMed:18955030, ECO:0000269\|PubMed:20599736, ECO:0000269\|PubMed:30420784}.
O95674	CDS2	S23	ochoa	Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2)	Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (PubMed:25375833). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (PubMed:25375833). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540, PubMed:31548309). {ECO:0000269\|PubMed:25375833, ECO:0000269\|PubMed:26946540, ECO:0000269\|PubMed:31548309}.
O95810	CAVIN2	S25	ochoa	Caveolae-associated protein 2 (Cavin-2) (PS-p68) (Phosphatidylserine-binding protein) (Serum deprivation-response protein)	Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity). {ECO:0000250\|UniProtKB:Q66H98, ECO:0000269\|PubMed:19525939}.
O95817	BAG3	S177	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S180	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S181	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
O95817	BAG3	S269	ochoa	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
P00533	EGFR	S1026	ochoa\|psp	Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)	Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity). {ECO:0000250\|UniProtKB:Q01279, ECO:0000269\|PubMed:10805725, ECO:0000269\|PubMed:11116146, ECO:0000269\|PubMed:11483589, ECO:0000269\|PubMed:11602604, ECO:0000269\|PubMed:12297049, ECO:0000269\|PubMed:12297050, ECO:0000269\|PubMed:12620237, ECO:0000269\|PubMed:12873986, ECO:0000269\|PubMed:15374980, ECO:0000269\|PubMed:15590694, ECO:0000269\|PubMed:15611079, ECO:0000269\|PubMed:17115032, ECO:0000269\|PubMed:17909029, ECO:0000269\|PubMed:19560417, ECO:0000269\|PubMed:20462955, ECO:0000269\|PubMed:20837704, ECO:0000269\|PubMed:21258366, ECO:0000269\|PubMed:27153536, ECO:0000269\|PubMed:2790960, ECO:0000269\|PubMed:35538033, ECO:0000269\|PubMed:7679104, ECO:0000269\|PubMed:8144591, ECO:0000269\|PubMed:9419975}.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269\|PubMed:21516087}.
P02545	LMNA	S612	ochoa	Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]	[Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269\|PubMed:10080180, ECO:0000269\|PubMed:10580070, ECO:0000269\|PubMed:10587585, ECO:0000269\|PubMed:10814726, ECO:0000269\|PubMed:11799477, ECO:0000269\|PubMed:12075506, ECO:0000269\|PubMed:12927431, ECO:0000269\|PubMed:15317753, ECO:0000269\|PubMed:18551513, ECO:0000269\|PubMed:18611980, ECO:0000269\|PubMed:2188730, ECO:0000269\|PubMed:22431096, ECO:0000269\|PubMed:2344612, ECO:0000269\|PubMed:23666920, ECO:0000269\|PubMed:23990565, ECO:0000269\|PubMed:24741066, ECO:0000269\|PubMed:25127216, ECO:0000269\|PubMed:31434876, ECO:0000269\|PubMed:31548606, ECO:0000269\|PubMed:37788673, ECO:0000269\|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269\|PubMed:20458013}.
P02686	MBP	S285	ochoa	Myelin basic protein (MBP) (Myelin A1 protein) (Myelin membrane encephalitogenic protein)	The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. {ECO:0000269\|PubMed:8544862}.
P04004	VTN	S393	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.
P04004	VTN	S397	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.
P04049	RAF1	S285	ochoa	RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269\|PubMed:11427728, ECO:0000269\|PubMed:11719507, ECO:0000269\|PubMed:15385642, ECO:0000269\|PubMed:15618521, ECO:0000269\|PubMed:15849194, ECO:0000269\|PubMed:16892053, ECO:0000269\|PubMed:16924233, ECO:0000269\|PubMed:9360956}.
P04083	ANXA1	S27	ochoa\|psp	Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26]	Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). {ECO:0000250\|UniProtKB:P10107, ECO:0000250\|UniProtKB:P19619, ECO:0000269\|PubMed:17008549, ECO:0000269\|PubMed:19625660, ECO:0000269\|PubMed:2532504, ECO:0000269\|PubMed:2936963, ECO:0000269\|PubMed:8425544, ECO:0000269\|PubMed:8557678}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:22879591, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Promotes resolution of inflammation and wound healing (PubMed:25664854). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). {ECO:0000269\|PubMed:15187149, ECO:0000269\|PubMed:22879591, ECO:0000269\|PubMed:25664854}.
P07947	YES1	S30	ochoa	Tyrosine-protein kinase Yes (EC 2.7.10.2) (Proto-oncogene c-Yes) (p61-Yes)	Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (PubMed:26979622). {ECO:0000269\|PubMed:11901164, ECO:0000269\|PubMed:18479465, ECO:0000269\|PubMed:19276087, ECO:0000269\|PubMed:21566460, ECO:0000269\|PubMed:21713032, ECO:0000269\|PubMed:26979622}.
P07949	RET	S686	ochoa	Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]	Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (PubMed:20064382, PubMed:20616503, PubMed:20702524, PubMed:21357690, PubMed:21454698, PubMed:24560924, PubMed:28846097, PubMed:28846099, PubMed:28953886, PubMed:31118272). In contrast to most receptor tyrosine kinases, RET requires not only its cognate ligands but also coreceptors, for activation (PubMed:21994944, PubMed:23333276, PubMed:28846097, PubMed:28846099, PubMed:28953886). GDNF ligands (GDNF, NRTN, ARTN, PSPN and GDF15) first bind their corresponding GDNFR coreceptors (GFRA1, GFRA2, GFRA3, GFRA4 and GFRAL, respectively), triggering RET autophosphorylation and activation, leading to activation of downstream signaling pathways, including the MAPK- and AKT-signaling pathways (PubMed:21994944, PubMed:23333276, PubMed:24560924, PubMed:25242331, PubMed:28846097, PubMed:28846099, PubMed:28953886). Acts as a dependence receptor via the GDNF-GFRA1 signaling: in the presence of the ligand GDNF in somatotrophs within pituitary, promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF (PubMed:20616503, PubMed:21994944). Required for the molecular mechanisms orchestration during intestine organogenesis via the ARTN-GFRA3 signaling: involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which triggers an aversive response, characterized by nausea, vomiting, and/or loss of appetite in response to various stresses (PubMed:28846097, PubMed:28846099, PubMed:28953886). Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner (PubMed:20702524, PubMed:21357690). Also active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage (PubMed:21357690). Triggers the differentiation of rapidly adapting (RA) mechanoreceptors (PubMed:20064382). Involved in the development of the neural crest (By similarity). Regulates nociceptor survival and size (By similarity). Phosphorylates PTK2/FAK1 (PubMed:21454698). {ECO:0000250\|UniProtKB:P35546, ECO:0000269\|PubMed:20064382, ECO:0000269\|PubMed:20616503, ECO:0000269\|PubMed:20702524, ECO:0000269\|PubMed:21357690, ECO:0000269\|PubMed:21454698, ECO:0000269\|PubMed:21994944, ECO:0000269\|PubMed:23333276, ECO:0000269\|PubMed:24560924, ECO:0000269\|PubMed:25242331, ECO:0000269\|PubMed:28846097, ECO:0000269\|PubMed:28846099, ECO:0000269\|PubMed:28953886, ECO:0000269\|PubMed:31118272}.; FUNCTION: [Isoform 1]: Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL. {ECO:0000269\|PubMed:28846099}.
P08238	HSP90AB1	S48	ochoa	Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3)	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269\|PubMed:16478993, ECO:0000269\|PubMed:18239673, ECO:0000269\|PubMed:19696785, ECO:0000269\|PubMed:20353823, ECO:0000269\|PubMed:24613385, ECO:0000269\|PubMed:32272059, ECO:0000303\|PubMed:25973397, ECO:0000303\|PubMed:26991466, ECO:0000303\|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269\|PubMed:21949862, ECO:0000305\|PubMed:22066472}.
P08670	VIM	S29	ochoa	Vimentin	Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250\|UniProtKB:A0A8C0N8E3, ECO:0000250\|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269\|PubMed:21746880}.
P09874	PARP1	S375	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}.
P0DJD0	RGPD1	S1456	ochoa	RANBP2-like and GRIP domain-containing protein 1 (Ran-binding protein 2-like 6) (RanBP2-like 6) (RanBP2L6)	None
P0DJD1	RGPD2	S1464	ochoa	RANBP2-like and GRIP domain-containing protein 2 (Ran-binding protein 2-like 2) (RanBP2-like 2) (RanBP2L2)	None
P11277	SPTB	S2114	ochoa\|psp	Spectrin beta chain, erythrocytic (Beta-I spectrin)	Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
P12830	CDH1	S840	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}.
P13804	ETFA	S179	ochoa	Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF)	Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:10356313, PubMed:15159392, PubMed:15975918, PubMed:27499296, PubMed:9334218). It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:9334218). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism (PubMed:12815589, PubMed:1430199, PubMed:1882842). {ECO:0000269\|PubMed:10356313, ECO:0000269\|PubMed:12815589, ECO:0000269\|PubMed:1430199, ECO:0000269\|PubMed:15159392, ECO:0000269\|PubMed:15975918, ECO:0000269\|PubMed:27499296, ECO:0000269\|PubMed:9334218, ECO:0000303\|PubMed:17941859, ECO:0000305\|PubMed:1882842}.
P13804	ETFA	S182	ochoa	Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF)	Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:10356313, PubMed:15159392, PubMed:15975918, PubMed:27499296, PubMed:9334218). It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:9334218). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism (PubMed:12815589, PubMed:1430199, PubMed:1882842). {ECO:0000269\|PubMed:10356313, ECO:0000269\|PubMed:12815589, ECO:0000269\|PubMed:1430199, ECO:0000269\|PubMed:15159392, ECO:0000269\|PubMed:15975918, ECO:0000269\|PubMed:27499296, ECO:0000269\|PubMed:9334218, ECO:0000303\|PubMed:17941859, ECO:0000305\|PubMed:1882842}.
P13807	GYS1	S710	ochoa\|psp	Glycogen [starch] synthase, muscle (EC 2.4.1.11) (Glycogen synthase 1)	Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. {ECO:0000269\|PubMed:35835870}.
P13807	GYS1	S717	ochoa	Glycogen [starch] synthase, muscle (EC 2.4.1.11) (Glycogen synthase 1)	Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. {ECO:0000269\|PubMed:35835870}.
P14859	POU2F1	S78	psp	POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1)	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. {ECO:0000269\|PubMed:10480874, ECO:0000269\|PubMed:1684878, ECO:0000269\|PubMed:7859290}.; FUNCTION: (Microbial infection) In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000305\|PubMed:12826401}.
P14921	ETS1	S272	ochoa	Protein C-ets-1 (p54)	Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518). {ECO:0000269\|PubMed:10698492, ECO:0000269\|PubMed:11909962, ECO:0000269\|PubMed:15247905, ECO:0000269\|PubMed:15592518, ECO:0000303\|PubMed:20378371}.; FUNCTION: [Isoform Ets-1 p27]: Acts as a dominant-negative for isoform c-ETS-1A. {ECO:0000269\|PubMed:19377509}.
P15056	BRAF	S419	ochoa\|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}.
P15884	TCF4	S333	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15884	TCF4	S505	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15923	TCF3	Y340	ochoa	Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)	Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (By similarity). Together with TCF15, required for the mesenchymal to epithelial transition (By similarity). Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (By similarity). Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (PubMed:2493990). Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (By similarity). {ECO:0000250\|UniProtKB:P15806, ECO:0000269\|PubMed:2493990}.; FUNCTION: [Isoform E47]: Facilitates ATOH7 binding to DNA at the consensus sequence 5'-CAGGTG-3', and positively regulates transcriptional activity. {ECO:0000269\|PubMed:31696227}.
P15924	DSP	S2575	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2597	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2815	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P15924	DSP	S2827	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P16144	ITGB4	S1511	ochoa	Integrin beta-4 (GP150) (CD antigen CD104)	Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). {ECO:0000269\|PubMed:12482924, ECO:0000269\|PubMed:19403692, ECO:0000269\|PubMed:20682778, ECO:0000269\|PubMed:22351760, ECO:0000269\|PubMed:28873464}.
P17661	DES	S72	ochoa	Desmin	Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (PubMed:25358400). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity). {ECO:0000250\|UniProtKB:P31001, ECO:0000269\|PubMed:24200904, ECO:0000269\|PubMed:25394388, ECO:0000269\|PubMed:26724190, ECO:0000303\|PubMed:25358400}.
P17676	CEBPB	S218	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P17676	CEBPB	S220	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P17676	CEBPB	S221	ochoa	CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)	Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:12048245, ECO:0000269\|PubMed:18647749, ECO:0000269\|PubMed:20829347, ECO:0000269\|PubMed:9374525, ECO:0000303\|PubMed:25451943}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250\|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250\|UniProtKB:P21272, ECO:0000250\|UniProtKB:P28033, ECO:0000269\|PubMed:11741938}.
P18583	SON	S1759	ochoa	Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3)	RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269\|PubMed:20581448, ECO:0000269\|PubMed:21504830, ECO:0000269\|PubMed:27545680}.
P18583	SON	S1774	ochoa	Protein SON (Bax antagonist selected in saccharomyces 1) (BASS1) (Negative regulatory element-binding protein) (NRE-binding protein) (Protein DBP-5) (SON3)	RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. Essential for correct RNA splicing of multiple genes critical for brain development, neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). {ECO:0000269\|PubMed:20581448, ECO:0000269\|PubMed:21504830, ECO:0000269\|PubMed:27545680}.
P18846	ATF1	S41	psp	Cyclic AMP-dependent transcription factor ATF-1 (cAMP-dependent transcription factor ATF-1) (Activating transcription factor 1) (Protein TREB36)	This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269\|PubMed:18794154, ECO:0000269\|PubMed:20980392}.
P19525	EIF2AK2	S83	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}.
P19532	TFE3	S554	ochoa	Transcription factor E3 (Class E basic helix-loop-helix protein 33) (bHLHe33)	Transcription factor that acts as a master regulator of lysosomal biogenesis and immune response (PubMed:2338243, PubMed:24448649, PubMed:29146937, PubMed:30733432, PubMed:31672913, PubMed:37079666). Specifically recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF (PubMed:24448649). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, TFE3 phosphorylation by MTOR promotes its inactivation (PubMed:24448649, PubMed:31672913, PubMed:36608670). Upon starvation or lysosomal stress, inhibition of MTOR induces TFE3 dephosphorylation, resulting in transcription factor activity (PubMed:24448649, PubMed:31672913, PubMed:36608670). Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression, thereby playing a central role in expression of lysosomal genes (PubMed:24448649). Maintains the pluripotent state of embryonic stem cells by promoting the expression of genes such as ESRRB; mTOR-dependent TFE3 cytosolic retention and inactivation promotes exit from pluripotency (By similarity). Required to maintain the naive pluripotent state of hematopoietic stem cell; mTOR-dependent cytoplasmic retention of TFE3 promotes the exit of hematopoietic stem cell from pluripotency (PubMed:30733432). TFE3 activity is also involved in the inhibition of neuronal progenitor differentiation (By similarity). Acts as a positive regulator of browning of adipose tissue by promoting expression of target genes; mTOR-dependent phosphorylation promotes cytoplasmic retention of TFE3 and inhibits browning of adipose tissue (By similarity). In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity (By similarity). Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer (PubMed:2338243). It also binds very well to a USF/MLTF site (PubMed:2338243). Promotes TGF-beta-induced transcription of COL1A2; via its interaction with TSC22D1 at E-boxes in the gene proximal promoter (By similarity). May regulate lysosomal positioning in response to nutrient deprivation by promoting the expression of PIP4P1 (PubMed:29146937). {ECO:0000250\|UniProtKB:Q64092, ECO:0000269\|PubMed:2338243, ECO:0000269\|PubMed:24448649, ECO:0000269\|PubMed:29146937, ECO:0000269\|PubMed:30733432, ECO:0000269\|PubMed:31672913, ECO:0000269\|PubMed:36608670, ECO:0000269\|PubMed:37079666}.
P19838	NFKB1	S893	ochoa\|psp	Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. {ECO:0000269\|PubMed:15485931, ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:2203531, ECO:0000269\|PubMed:2234062, ECO:0000269\|PubMed:7830764}.; FUNCTION: [Nuclear factor NF-kappa-B p105 subunit]: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B (PubMed:1423592). Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105 (PubMed:1423592). {ECO:0000269\|PubMed:1423592}.; FUNCTION: [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor (PubMed:1740106, PubMed:7830764). Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions (PubMed:1740106, PubMed:7830764). {ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:7830764}.
P19838	NFKB1	S927	psp	Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. {ECO:0000269\|PubMed:15485931, ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:2203531, ECO:0000269\|PubMed:2234062, ECO:0000269\|PubMed:7830764}.; FUNCTION: [Nuclear factor NF-kappa-B p105 subunit]: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B (PubMed:1423592). Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105 (PubMed:1423592). {ECO:0000269\|PubMed:1423592}.; FUNCTION: [Nuclear factor NF-kappa-B p50 subunit]: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor (PubMed:1740106, PubMed:7830764). Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions (PubMed:1740106, PubMed:7830764). {ECO:0000269\|PubMed:1740106, ECO:0000269\|PubMed:7830764}.
P20700	LMNB1	S395	ochoa\|psp	Lamin-B1	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28716252, PubMed:32910914). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:28716252, PubMed:32910914). {ECO:0000269\|PubMed:28716252, ECO:0000269\|PubMed:32910914}.
P21359	NF1	S2587	ochoa	Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]	Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269\|PubMed:2121371, ECO:0000269\|PubMed:8417346}.
P21462	FPR1	S328	psp	fMet-Leu-Phe receptor (fMLP receptor) (N-formyl peptide receptor) (FPR) (N-formylpeptide chemoattractant receptor)	High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:10514456, PubMed:15153520, PubMed:2161213, PubMed:2176894). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:15153520, PubMed:15210802, PubMed:1712023, PubMed:2161213). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:10514456, PubMed:1712023). Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release (PubMed:25109685). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (PubMed:15210802). {ECO:0000269\|PubMed:10514456, ECO:0000269\|PubMed:15153520, ECO:0000269\|PubMed:2161213, ECO:0000269\|PubMed:2176894, ECO:0000269\|PubMed:25109685, ECO:0000303\|PubMed:10514456, ECO:0000303\|PubMed:1712023, ECO:0000303\|PubMed:2161213, ECO:0000303\|PubMed:2176894}.
P22059	OSBP	S379	ochoa	Oxysterol-binding protein 1	Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269\|PubMed:15746430, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18450749, ECO:0000269\|PubMed:24209621}.
P23588	EIF4B	S424	ochoa	Eukaryotic translation initiation factor 4B (eIF-4B)	Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
P23588	EIF4B	S488	ochoa	Eukaryotic translation initiation factor 4B (eIF-4B)	Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
P23677	ITPKA	S121	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P23677	ITPKA	S123	ochoa	Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A)	Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269\|PubMed:12747803, ECO:0000269\|PubMed:15350214, ECO:0000269\|PubMed:1847047}.
P25054	APC	S1346	ochoa	Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000250\|UniProtKB:Q61315, ECO:0000269\|PubMed:10947987, ECO:0000269\|PubMed:17293347, ECO:0000269\|PubMed:17599059, ECO:0000269\|PubMed:19151759, ECO:0000269\|PubMed:19893577, ECO:0000269\|PubMed:20937854}.
P27448	MARK3	S368	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P27448	MARK3	S369	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P27448	MARK3	S374	ochoa	MAP/microtubule affinity-regulating kinase 3 (EC 2.7.11.1) (C-TAK1) (cTAK1) (Cdc25C-associated protein kinase 1) (ELKL motif kinase 2) (EMK-2) (Protein kinase STK10) (Ser/Thr protein kinase PAR-1) (Par-1a) (Serine/threonine-protein kinase p78)	Serine/threonine-protein kinase (PubMed:16822840, PubMed:16980613, PubMed:23666762). Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Phosphorylates CDC25C on 'Ser-216' (PubMed:12941695). Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (PubMed:16980613). Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol (PubMed:16822840). Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1 (PubMed:28087714). Phosphorylates PKP2 and KSR1 (PubMed:12941695). {ECO:0000269\|PubMed:12941695, ECO:0000269\|PubMed:16822840, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:23666762, ECO:0000269\|PubMed:28087714}.
P27816	MAP4	S853	ochoa	Microtubule-associated protein 4 (MAP-4)	Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269\|PubMed:10791892, ECO:0000269\|PubMed:34782749}.
P28290	ITPRID2	S1053	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
P29401	TKT	S439	ochoa	Transketolase (TK) (EC 2.2.1.1)	Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000269\|PubMed:27259054}.
P29558	RBMS1	S38	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29558	RBMS1	S40	ochoa	RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2)	Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
P29692	EEF1D	S60	ochoa	Elongation factor 1-delta (EF-1-delta) (Antigen NY-CO-4)	[Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
P29692	EEF1D	S64	ochoa	Elongation factor 1-delta (EF-1-delta) (Antigen NY-CO-4)	[Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
P30622	CLIP1	S152	ochoa	CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)	Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269\|PubMed:12433698, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:17889670}.
P31629	HIVEP2	S807	ochoa	Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2) (HIV-EP2) (MHC-binding protein 2) (MBP-2)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
P33527	ABCC1	S905	ochoa	Multidrug resistance-associated protein 1 (EC 7.6.2.2) (ATP-binding cassette sub-family C member 1) (Glutathione-S-conjugate-translocating ATPase ABCC1) (EC 7.6.2.3) (Leukotriene C(4) transporter) (LTC4 transporter)	Mediates export of organic anions and drugs from the cytoplasm (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export (PubMed:9281595). Hydrolyzes ATP with low efficiency (PubMed:16230346). Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation (PubMed:17050692). Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthesizing cells (By similarity). Mediates ATP-dependent, GSH-independent cyclic GMP-AMP (cGAMP) export (PubMed:36070769). Thus, by limiting intracellular cGAMP concentrations negatively regulates the cGAS-STING pathway (PubMed:36070769). Exports S-geranylgeranyl-glutathione (GGG) in lymphoid cells and stromal compartments of lymphoid organs. ABCC1 (via extracellular transport) with GGT5 (via GGG catabolism) establish GGG gradients within lymphoid tissues to position P2RY8-positive lymphocytes at germinal centers in lymphoid follicles and restrict their chemotactic transmigration from blood vessels to the bone marrow parenchyma (By similarity). Mediates basolateral export of GSH-conjugated R- and S-prostaglandin A2 diastereomers in polarized epithelial cells (PubMed:9426231). {ECO:0000250\|UniProtKB:O35379, ECO:0000269\|PubMed:10064732, ECO:0000269\|PubMed:11114332, ECO:0000269\|PubMed:16230346, ECO:0000269\|PubMed:17050692, ECO:0000269\|PubMed:36070769, ECO:0000269\|PubMed:7961706, ECO:0000269\|PubMed:9281595, ECO:0000269\|PubMed:9426231}.
P33981	TTK	S837	ochoa	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}.
P34910	EVI2B	S268	ochoa	Protein EVI2B (Ecotropic viral integration site 2B protein homolog) (EVI-2B) (CD antigen CD361)	Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells. {ECO:0000269\|PubMed:28186500}.
P35222	CTNNB1	S23	psp	Catenin beta-1 (Beta-catenin)	Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250\|UniProtKB:Q02248, ECO:0000269\|PubMed:17524503, ECO:0000269\|PubMed:18077326, ECO:0000269\|PubMed:18086858, ECO:0000269\|PubMed:18957423, ECO:0000269\|PubMed:21262353, ECO:0000269\|PubMed:22155184, ECO:0000269\|PubMed:22187462, ECO:0000269\|PubMed:22647378, ECO:0000269\|PubMed:22699938, ECO:0000269\|PubMed:29910125}.
P35414	APLNR	S335	psp	Apelin receptor (Angiotensin receptor-like 1) (G-protein coupled receptor APJ) (G-protein coupled receptor HG11)	G protein-coupled receptor for peptide hormones apelin (APLN) and apelin receptor early endogenous ligand (APELA/ELA), that plays a role in the regulation of normal cardiovascular function and fluid homeostasis (PubMed:11090199, PubMed:22810587, PubMed:25639753, PubMed:28137936, PubMed:35817871, PubMed:38428423). When acting as apelin receptor, activates both G(i) protein pathway that inhibits adenylate cyclase activity, and the beta-arrestin pathway that promotes internalization of the receptor (PubMed:11090199, PubMed:25639753, PubMed:28137936, PubMed:35817871, PubMed:38428423). APLNR/APJ also functions as mechanoreceptor that is activated by pathological stimuli in a G-protein-independent fashion to induce beta-arrestin signaling, hence eliciting cardiac hypertrophy (PubMed:22810587, PubMed:38428423). However, the presence of apelin ligand blunts cardiac hypertrophic induction from APLNR/APJ on response to pathological stimuli (PubMed:22810587, PubMed:38428423). Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a APELA receptor (By similarity). May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (By similarity). Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Also plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (PubMed:25639753, PubMed:28137936). {ECO:0000250\|UniProtKB:Q7SZP9, ECO:0000250\|UniProtKB:Q9WV08, ECO:0000269\|PubMed:11090199, ECO:0000269\|PubMed:22810587, ECO:0000269\|PubMed:25639753, ECO:0000269\|PubMed:28137936, ECO:0000269\|PubMed:35817871, ECO:0000269\|PubMed:38428423}.; FUNCTION: (Microbial infection) Alternative coreceptor with CD4 for HIV-1 infection; may be involved in the development of AIDS dementia (PubMed:11090199). {ECO:0000269\|PubMed:11090199}.
P37275	ZEB1	S309	ochoa	Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8)	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2 transcription via binding to the E-box in the upstream enhancer region (By similarity). {ECO:0000250\|UniProtKB:Q64318, ECO:0000269\|PubMed:19935649, ECO:0000269\|PubMed:20175752, ECO:0000269\|PubMed:20418909}.
P38159	RBMX	S277	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38159	RBMX	S316	ochoa	RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269\|PubMed:12165565, ECO:0000269\|PubMed:12761049, ECO:0000269\|PubMed:16707624, ECO:0000269\|PubMed:18445477, ECO:0000269\|PubMed:18541147, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:21327109}.
P38398	BRCA1	S1473	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}.
P39880	CUX1	S1227	ochoa	Homeobox protein cut-like 1 (CCAAT displacement protein) (CDP) (CDP/Cux p200) (Homeobox protein cux-1) [Cleaved into: CDP/Cux p110]	Transcription factor involved in the control of neuronal differentiation in the brain. Regulates dendrite development and branching, and dendritic spine formation in cortical layers II-III. Also involved in the control of synaptogenesis. In addition, it has probably a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator. {ECO:0000250\|UniProtKB:P53564}.; FUNCTION: [CDP/Cux p110]: Plays a role in cell cycle progression, in particular at the G1/S transition. As cells progress into S phase, a fraction of CUX1 molecules is proteolytically processed into N-terminally truncated proteins of 110 kDa. While CUX1 only transiently binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110 makes a stable interaction with DNA and stimulates expression of genes such as POLA1. {ECO:0000269\|PubMed:15099520}.
P41235	HNF4A	S138	psp	Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)	Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes (PubMed:30597922). Activates the transcription of CYP2C38 (By similarity). Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells (PubMed:30530698). {ECO:0000250\|UniProtKB:P49698, ECO:0000269\|PubMed:30530698, ECO:0000269\|PubMed:30597922}.
P42166	TMPO	S158	ochoa	Lamina-associated polypeptide 2, isoform alpha (Thymopoietin isoform alpha) (TP alpha) (Thymopoietin-related peptide isoform alpha) (TPRP isoform alpha) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)]	May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
P42331	ARHGAP25	S391	ochoa	Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.
P42331	ARHGAP25	S397	ochoa	Rho GTPase-activating protein 25 (Rho-type GTPase-activating protein 25)	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.
P43243	MATR3	S61	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}.
P46019	PHKA2	S969	ochoa	Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit)	Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
P46379	BAG6	S96	ochoa	Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe)	ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (PubMed:26565908). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250\|UniProtKB:Q9Z1R2, ECO:0000269\|PubMed:20516149, ECO:0000269\|PubMed:20676083, ECO:0000269\|PubMed:21636303, ECO:0000269\|PubMed:21743475, ECO:0000269\|PubMed:23129660, ECO:0000269\|PubMed:24981174, ECO:0000269\|PubMed:25179605, ECO:0000269\|PubMed:26565908, ECO:0000269\|PubMed:26692333, ECO:0000269\|PubMed:27193484, ECO:0000269\|PubMed:28104892}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity (PubMed:17403783). When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). {ECO:0000269\|PubMed:17403783, ECO:0000269\|PubMed:18765639}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000269\|PubMed:18055229, ECO:0000269\|PubMed:18852879}.; FUNCTION: Mediates ricin-induced apoptosis. {ECO:0000269\|PubMed:14960581}.
P46821	MAP1B	S1242	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1244	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1643	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46934	NEDD4	S733	ochoa	E3 ubiquitin-protein ligase NEDD4 (EC 2.3.2.26) (Cell proliferation-inducing gene 53 protein) (HECT-type E3 ubiquitin transferase NEDD4) (Neural precursor cell expressed developmentally down-regulated protein 4) (NEDD-4)	E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:19920177, PubMed:21399620, PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes (By similarity). Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes (PubMed:21765395). Promotes ubiquitination of RAPGEF2 (PubMed:11598133). According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD (By similarity). Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development (By similarity). Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2 (PubMed:20086093). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Ubiquitinates DAZAP2, leading to its proteasomal degradation (PubMed:11342538). Ubiquitinates POLR2A (PubMed:19920177). Functions as a platform to recruit USP13 to form an NEDD4-USP13 deubiquitination complex that plays a critical role in cleaving the 'Lys-48'-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes (PubMed:32101753). {ECO:0000250\|UniProtKB:P46935, ECO:0000269\|PubMed:11342538, ECO:0000269\|PubMed:11598133, ECO:0000269\|PubMed:17218260, ECO:0000269\|PubMed:18562292, ECO:0000269\|PubMed:21399620, ECO:0000269\|PubMed:21765395, ECO:0000269\|PubMed:23644597, ECO:0000269\|PubMed:25631046, ECO:0000269\|PubMed:32101753}.; FUNCTION: (Microbial infection) Involved in the ubiquitination of Ebola virus protein VP40 which plays a role in viral budding. {ECO:0000269\|PubMed:12559917, ECO:0000269\|PubMed:18305167}.
P46937	YAP1	S393	ochoa	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P46939	UTRN	S2213	ochoa	Utrophin (Dystrophin-related protein 1) (DRP-1)	May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}.
P48681	NES	S1492	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}.
P49023	PXN	S85	ochoa\|psp	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	Y88	ochoa\|psp	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49023	PXN	S130	ochoa\|psp	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49321	NASP	S680	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}.
P49790	NUP153	S182	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S189	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49792	RANBP2	S778	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	S2270	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	S2447	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	S2548	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	S2558	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}.
P49815	TSC2	S1365	ochoa	Tuberin (Tuberous sclerosis 2 protein)	Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:35772404). Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12820960, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:33436626). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:35772404). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 (By similarity). {ECO:0000250\|UniProtKB:P49816, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12820960, ECO:0000269\|PubMed:12842888, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:22819219, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:33436626, ECO:0000269\|PubMed:35772404}.
P50402	EMD	S52	ochoa	Emerin	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:32923640}.
P50552	VASP	S314	ochoa	Vasodilator-stimulated phosphoprotein (VASP)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. {ECO:0000269\|PubMed:10087267, ECO:0000269\|PubMed:10438535, ECO:0000269\|PubMed:15939738, ECO:0000269\|PubMed:17082196, ECO:0000269\|PubMed:18559661}.
P50750	CDK9	S347	ochoa\|psp	Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)	Protein kinase involved in the regulation of transcription (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094, PubMed:29335245). Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:16427012, PubMed:20930849, PubMed:28426094, PubMed:30134174). This complex is inactive when in the 7SK snRNP complex form (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094). Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR and the negative elongation factors DSIF and NELFE (PubMed:10912001, PubMed:11112772, PubMed:12037670, PubMed:16427012, PubMed:20081228, PubMed:20980437, PubMed:21127351, PubMed:9857195). Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling) (PubMed:17956865, PubMed:18362169). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis (PubMed:10393184, PubMed:11112772). P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export (PubMed:15564463, PubMed:19575011, PubMed:19844166). Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing (PubMed:15564463, PubMed:19575011, PubMed:19844166). The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro (PubMed:21127351). Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage (PubMed:20493174). In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6 (PubMed:20493174). Promotes cardiac myocyte enlargement (PubMed:20081228). RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription (PubMed:21127351). AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect (PubMed:10912001, PubMed:11112772, PubMed:9857195). The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (PubMed:12037670). Catalyzes phosphorylation of KAT5, promoting KAT5 recruitment to chromatin and histone acetyltransferase activity (PubMed:29335245). {ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:10574912, ECO:0000269\|PubMed:10757782, ECO:0000269\|PubMed:10912001, ECO:0000269\|PubMed:11112772, ECO:0000269\|PubMed:11145967, ECO:0000269\|PubMed:11575923, ECO:0000269\|PubMed:11809800, ECO:0000269\|PubMed:11884399, ECO:0000269\|PubMed:12037670, ECO:0000269\|PubMed:14701750, ECO:0000269\|PubMed:15564463, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:16427012, ECO:0000269\|PubMed:17956865, ECO:0000269\|PubMed:18362169, ECO:0000269\|PubMed:19575011, ECO:0000269\|PubMed:19844166, ECO:0000269\|PubMed:20081228, ECO:0000269\|PubMed:20493174, ECO:0000269\|PubMed:20930849, ECO:0000269\|PubMed:20980437, ECO:0000269\|PubMed:21127351, ECO:0000269\|PubMed:28426094, ECO:0000269\|PubMed:29335245, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:9857195}.
P50851	LRBA	S1757	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}.
P51114	FXR1	S413	ochoa	RNA-binding protein FXR1 (FMR1 autosomal homolog 1) (hFXR1p)	mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis (PubMed:17382880, PubMed:20417602, PubMed:30067974, PubMed:34731628, PubMed:35989368, PubMed:36306353). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:17382880, PubMed:34731628). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity). Required to activate translation of stored mRNAs during late spermatogenesis: acts by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules that recruit translation initiation factor EIF4G3 to activate translation of stored mRNAs in late spermatids (By similarity). Promotes translation of MYC transcripts by recruiting the eIF4F complex to the translation start site (PubMed:34731628). Acts as a negative regulator of inflammation in response to IL19 by promoting destabilization of pro-inflammatory transcripts (PubMed:30067974). Also acts as an inhibitor of inflammation by binding to TNF mRNA, decreasing TNF protein production (By similarity). Acts as a negative regulator of AMPA receptor GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting its translation (By similarity). Regulates proliferation of adult neural stem cells by binding to CDKN1A mRNA and promoting its expression (By similarity). Acts as a regulator of sleep and synaptic homeostasis by regulating translation of transcripts in neurons (By similarity). Required for embryonic and postnatal development of muscle tissue by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules (PubMed:30770808). Involved in the nuclear pore complex localization to the nuclear envelope by preventing cytoplasmic aggregation of nucleoporins: acts by preventing ectopic phase separation of nucleoporins in the cytoplasm via a microtubule-dependent mechanism (PubMed:32706158). Plays a role in the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with PKP3 (PubMed:25225333). May also do the same for PKP2, PKP3 and DSP via its interaction with PKP1 (PubMed:25225333). Forms a cytoplasmic messenger ribonucleoprotein (mRNP) network by packaging long mRNAs, serving as a scaffold that recruits proteins and signaling molecules. This network facilitates signaling reactions by maintaining proximity between kinases and substrates, crucial for processes like actomyosin reorganization (PubMed:39106863). {ECO:0000250\|UniProtKB:Q61584, ECO:0000269\|PubMed:17382880, ECO:0000269\|PubMed:20417602, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:30067974, ECO:0000269\|PubMed:30770808, ECO:0000269\|PubMed:32706158, ECO:0000269\|PubMed:34731628, ECO:0000269\|PubMed:35989368, ECO:0000269\|PubMed:36306353, ECO:0000269\|PubMed:39106863}.
P51116	FXR2	S404	ochoa	RNA-binding protein FXR2 (FXR2P) (FMR1 autosomal homolog 2)	mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for adult hippocampal neurogenesis (By similarity). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity). Acts as a regulator of adult hippocampal neurogenesis by regulating translation and/or stability of NOG mRNA, thereby preventing NOG protein expression in the dentate gyrus (By similarity). {ECO:0000250\|UniProtKB:Q61584, ECO:0000250\|UniProtKB:Q9WVR4}.
P52943	CRIP2	S104	ochoa	Cysteine-rich protein 2 (CRP-2) (Protein ESP1)	None
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	S1028	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}.
P53671	LIMK2	S283	psp	LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1)	Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics (PubMed:10436159, PubMed:11018042). Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11018042). Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP (PubMed:22328514). Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro (PubMed:8537403). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). {ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:11018042, ECO:0000269\|PubMed:22328514, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:8537403}.
P53814	SMTN	S368	ochoa	Smoothelin	Structural protein of the cytoskeleton.
P53999	SUB1	S46	ochoa	Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269\|PubMed:16605275, ECO:0000269\|PubMed:16689930, ECO:0000269\|PubMed:7628453, ECO:0000269\|PubMed:8062391, ECO:0000269\|PubMed:8062392, ECO:0000269\|PubMed:9360603, ECO:0000269\|PubMed:9482861}.
P54198	HIRA	S533	ochoa	Protein HIRA (TUP1-like enhancer of split protein 1)	Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269\|PubMed:12370293, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527}.
P54578	USP14	S222	ochoa	Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14)	Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029). {ECO:0000250\|UniProtKB:Q9JMA1, ECO:0000269\|PubMed:18162577, ECO:0000269\|PubMed:19106094, ECO:0000269\|PubMed:19135427, ECO:0000269\|PubMed:27666593, ECO:0000269\|PubMed:28396413, ECO:0000269\|PubMed:35145029}.
P54646	PRKAA2	S491	ochoa\|psp	5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (PubMed:7959015). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation (By similarity). Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity). Upon glucose starvation, promotes ARF6 activation in a kinase-independent manner leading to cell migration (PubMed:36017701). Upon glucose deprivation mediates the phosphorylation of ACSS2 at 'Ser-659', which exposes the nuclear localization signal of ACSS2, required for its interaction with KPNA1 and nuclear translocation (PubMed:28552616). Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:Q09137, ECO:0000250\|UniProtKB:Q8BRK8, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:25687571, ECO:0000269\|PubMed:28552616, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36017701, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:7959015, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
P54646	PRKAA2	S501	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (PubMed:7959015). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation (By similarity). Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity). Upon glucose starvation, promotes ARF6 activation in a kinase-independent manner leading to cell migration (PubMed:36017701). Upon glucose deprivation mediates the phosphorylation of ACSS2 at 'Ser-659', which exposes the nuclear localization signal of ACSS2, required for its interaction with KPNA1 and nuclear translocation (PubMed:28552616). Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:Q09137, ECO:0000250\|UniProtKB:Q8BRK8, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:25687571, ECO:0000269\|PubMed:28552616, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36017701, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:7959015, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
P54725	RAD23A	S133	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P55085	F2RL1	S376	ochoa	Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]	Receptor for trypsin and trypsin-like enzymes coupled to G proteins (PubMed:28445455). Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho (PubMed:28445455). Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3 (PubMed:23202369). Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion (PubMed:10086357). Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o)-alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to PubMed:21627585 can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to GNAQ and GNA11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as pro-inflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders. Probably mediates activation of pro-inflammatory and pro-fibrotic responses in fibroblasts, triggered by coagulation factor Xa (F10) (By similarity). Mediates activation of barrier protective signaling responses in endothelial cells, triggered by coagulation factor Xa (F10) (PubMed:22409427). {ECO:0000250\|UniProtKB:P55086, ECO:0000269\|PubMed:10086357, ECO:0000269\|PubMed:10725339, ECO:0000269\|PubMed:11413129, ECO:0000269\|PubMed:11441110, ECO:0000269\|PubMed:11447194, ECO:0000269\|PubMed:11714832, ECO:0000269\|PubMed:12832443, ECO:0000269\|PubMed:15155775, ECO:0000269\|PubMed:16359518, ECO:0000269\|PubMed:16410250, ECO:0000269\|PubMed:16478888, ECO:0000269\|PubMed:16714334, ECO:0000269\|PubMed:17404307, ECO:0000269\|PubMed:17500066, ECO:0000269\|PubMed:18424071, ECO:0000269\|PubMed:18453611, ECO:0000269\|PubMed:18474671, ECO:0000269\|PubMed:18622013, ECO:0000269\|PubMed:19494303, ECO:0000269\|PubMed:19781631, ECO:0000269\|PubMed:19864598, ECO:0000269\|PubMed:19865078, ECO:0000269\|PubMed:20826780, ECO:0000269\|PubMed:21501162, ECO:0000269\|PubMed:22409427, ECO:0000269\|PubMed:23202369, ECO:0000269\|PubMed:28445455}.
P55196	AFDN	S551	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55196	AFDN	S1315	ochoa	Afadin (ALL1-fused gene from chromosome 6 protein) (Protein AF-6) (Afadin adherens junction formation factor)	Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (PubMed:11024295). May play a key role in the organization of epithelial structures of the embryonic ectoderm (By similarity). Essential for the organization of adherens junctions (PubMed:30463011). {ECO:0000250\|UniProtKB:O35889, ECO:0000250\|UniProtKB:Q9QZQ1, ECO:0000269\|PubMed:11024295, ECO:0000269\|PubMed:30463011}.
P55795	HNRNPH2	S272	ochoa	Heterogeneous nuclear ribonucleoprotein H2 (hnRNP H2) (FTP-3) (Heterogeneous nuclear ribonucleoprotein H') (hnRNP H') [Cleaved into: Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed]	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).
P56945	BCAR1	S428	ochoa	Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12432078, PubMed:12832404). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). {ECO:0000250\|UniProtKB:Q61140, ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:12832404, ECO:0000269\|PubMed:17038317}.
P57078	RIPK4	S420	ochoa	Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-delta-interacting protein kinase)	Serine/threonine protein kinase (By similarity). Required for embryonic skin development and correct skin homeostasis in adults, via phosphorylation of PKP1 and subsequent promotion of keratinocyte differentiation and cell adhesion (By similarity). It is a direct transcriptional target of TP63 (PubMed:22197488). Plays a role in NF-kappa-B activation (PubMed:12446564). {ECO:0000250\|UniProtKB:Q9ERK0, ECO:0000269\|PubMed:12446564, ECO:0000269\|PubMed:22197488}.
P57078	RIPK4	S424	ochoa	Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-delta-interacting protein kinase)	Serine/threonine protein kinase (By similarity). Required for embryonic skin development and correct skin homeostasis in adults, via phosphorylation of PKP1 and subsequent promotion of keratinocyte differentiation and cell adhesion (By similarity). It is a direct transcriptional target of TP63 (PubMed:22197488). Plays a role in NF-kappa-B activation (PubMed:12446564). {ECO:0000250\|UniProtKB:Q9ERK0, ECO:0000269\|PubMed:12446564, ECO:0000269\|PubMed:22197488}.
P60709	ACTB	S338	ochoa	Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]	Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250\|UniProtKB:Q6QAQ1, ECO:0000269\|PubMed:25255767, ECO:0000269\|PubMed:29581253, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:38609661, ECO:0000269\|PubMed:39321809}.
P61073	CXCR4	S312	ochoa	C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (FB22) (Fusin) (HM89) (LCR1) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Lipopolysaccharide-associated protein 3) (LAP-3) (LPS-associated protein 3) (NPYRL) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)	Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:18799424, PubMed:24912431, PubMed:28978524). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). {ECO:0000250\|UniProtKB:P70658, ECO:0000269\|PubMed:10074102, ECO:0000269\|PubMed:10452968, ECO:0000269\|PubMed:10644702, ECO:0000269\|PubMed:10825158, ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:17197449, ECO:0000269\|PubMed:18799424, ECO:0000269\|PubMed:20048153, ECO:0000269\|PubMed:20228059, ECO:0000269\|PubMed:20505072, ECO:0000269\|PubMed:24912431, ECO:0000269\|PubMed:28978524, ECO:0000269\|PubMed:8752280, ECO:0000269\|PubMed:8752281}.; FUNCTION: (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:10074122, PubMed:10756055, PubMed:8849450, PubMed:8929542, PubMed:9427609). {ECO:0000269\|PubMed:10074122, ECO:0000269\|PubMed:10756055, ECO:0000269\|PubMed:8849450, ECO:0000269\|PubMed:8929542, ECO:0000269\|PubMed:9427609}.
P63261	ACTG1	S338	ochoa	Actin, cytoplasmic 2 (EC 3.6.4.-) (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity). {ECO:0000250\|UniProtKB:P63260, ECO:0000305\|PubMed:29581253}.
P78312	FAM193A	S260	ochoa	Protein FAM193A (Protein IT14)	None
P82094	TMF1	S328	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P82094	TMF1	S330	ochoa	TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269\|PubMed:10428808, ECO:0000269\|PubMed:1409643, ECO:0000269\|PubMed:15467733, ECO:0000269\|PubMed:17698061}.
P98082	DAB2	S316	ochoa	Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)	Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269\|PubMed:11387212, ECO:0000269\|PubMed:12805222, ECO:0000269\|PubMed:16267015, ECO:0000269\|PubMed:16984970, ECO:0000269\|PubMed:19306879, ECO:0000269\|PubMed:21995445, ECO:0000269\|PubMed:22323290, ECO:0000269\|PubMed:22491013}.
Q00341	HDLBP	S1236	ochoa	Vigilin (High density lipoprotein-binding protein) (HDL-binding protein)	Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.
Q00587	CDC42EP1	S142	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q01082	SPTBN1	S2304	ochoa	Spectrin beta chain, non-erythrocytic 1 (Beta-II spectrin) (Fodrin beta chain) (Spectrin, non-erythroid beta chain 1)	Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function. {ECO:0000269\|PubMed:34211179}.
Q01196	RUNX1	S423	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}.
Q01831	XPC	S496	ochoa	DNA repair protein complementing XP-C cells (Xeroderma pigmentosum group C-complementing protein) (p125)	Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19609301, PubMed:19941824, PubMed:20028083, PubMed:20649465, PubMed:20798892, PubMed:9734359). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083). {ECO:0000269\|PubMed:10734143, ECO:0000269\|PubMed:10873465, ECO:0000269\|PubMed:12509299, ECO:0000269\|PubMed:12547395, ECO:0000269\|PubMed:19609301, ECO:0000269\|PubMed:19941824, ECO:0000269\|PubMed:20028083, ECO:0000269\|PubMed:20649465, ECO:0000269\|PubMed:20798892, ECO:0000269\|PubMed:9734359}.; FUNCTION: In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT) (PubMed:29973595, PubMed:31527837). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes (PubMed:31527837). {ECO:0000269\|PubMed:29973595, ECO:0000269\|PubMed:31527837}.
Q02241	KIF23	S902	ochoa	Kinesin-like protein KIF23 (Kinesin-like protein 5) (Mitotic kinesin-like protein 1)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. {ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:22522702, ECO:0000269\|PubMed:23570799}.
Q02446	SP4	S124	ochoa	Transcription factor Sp4 (SPR-1)	Binds to GT and GC boxes promoters elements. Probable transcriptional activator.
Q03164	KMT2A	S3508	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S3511	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03164	KMT2A	S3515	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q03252	LMNB2	S410	ochoa	Lamin-B2	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:33033404). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:33033404). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:33033404). {ECO:0000269\|PubMed:33033404}.
Q04656	ATP7A	S262	ochoa	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S339	ochoa\|psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S349	psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S1463	ochoa\|psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04656	ATP7A	S1466	ochoa\|psp	Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)	ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250\|UniProtKB:Q64430, ECO:0000269\|PubMed:10419525, ECO:0000269\|PubMed:11092760, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:19917612, ECO:0000269\|PubMed:28389643, ECO:0000269\|PubMed:31283225}.
Q04726	TLE3	S197	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04726	TLE3	S253	ochoa	Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3) (ESG3)	Transcriptional corepressor that binds to a number of transcription factors (PubMed:28689657). Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling (PubMed:28689657). The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250\|UniProtKB:Q04724, ECO:0000269\|PubMed:28689657}.
Q04912	MST1R	S1031	ochoa	Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (CDw136) (Protein-tyrosine kinase 8) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain]	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Also plays a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. {ECO:0000269\|PubMed:18836480, ECO:0000269\|PubMed:7939629, ECO:0000269\|PubMed:9764835}.
Q05209	PTPN12	S596	ochoa	Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1)	Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). {ECO:0000269\|PubMed:17329398, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:27134172}.
Q05209	PTPN12	S603	ochoa	Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1)	Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). {ECO:0000269\|PubMed:17329398, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:27134172}.
Q07157	TJP1	S280	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S284	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S290	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S303	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S821	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S824	ochoa	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
Q07157	TJP1	S831	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}.
Q07955	SRSF1	S201	ochoa\|psp	Serine/arginine-rich splicing factor 1 (Alternative-splicing factor 1) (ASF-1) (Splicing factor, arginine/serine-rich 1) (pre-mRNA-splicing factor SF2, P33 subunit)	Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway. {ECO:0000269\|PubMed:8139654}.
Q08050	FOXM1	S498	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	S268	ochoa	Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160)	Golgi auto-antigen; probably involved in maintaining Golgi structure.
Q08378	GOLGA3	S272	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.
Q08999	RBL2	S952	ochoa\|psp	Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Q08999	RBL2	S962	ochoa\|psp	Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Q08AD1	CAMSAP2	S406	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S408	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S680	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S960	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q08AD1	CAMSAP2	S1301	ochoa	Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:23169647, PubMed:24486153, PubMed:24706919). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153, PubMed:24706919). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:27666745). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (PubMed:28726242). {ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:24706919, ECO:0000269\|PubMed:24908486, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28726242}.
Q09666	AHNAK	S5739	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5854	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5857	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q09666	AHNAK	S5860	ochoa	Neuroblast differentiation-associated protein AHNAK (Desmoyokin)	May be required for neuronal cell differentiation.
Q0JRZ9	FCHO2	S468	ochoa	F-BAR domain only protein 2	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269\|PubMed:17540576, ECO:0000269\|PubMed:20448150, ECO:0000269\|PubMed:21762413, ECO:0000269\|PubMed:22323290}.
Q12778	FOXO1	S319	ochoa\|psp	Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)	Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). {ECO:0000250\|UniProtKB:A4L7N3, ECO:0000250\|UniProtKB:G3V7R4, ECO:0000250\|UniProtKB:Q9R1E0, ECO:0000269\|PubMed:10358076, ECO:0000269\|PubMed:12228231, ECO:0000269\|PubMed:15220471, ECO:0000269\|PubMed:15890677, ECO:0000269\|PubMed:17024043, ECO:0000269\|PubMed:18356527, ECO:0000269\|PubMed:19221179, ECO:0000269\|PubMed:19483080, ECO:0000269\|PubMed:20543840, ECO:0000269\|PubMed:21245099, ECO:0000269\|PubMed:31063815}.
Q12789	GTF3C1	S751	ochoa	General transcription factor 3C polypeptide 1 (TF3C-alpha) (TFIIIC box B-binding subunit) (Transcription factor IIIC 220 kDa subunit) (TFIIIC 220 kDa subunit) (TFIIIC220) (Transcription factor IIIC subunit alpha)	Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.
Q12824	SMARCB1	S129	ochoa	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (BRG1-associated factor 47) (BAF47) (Integrase interactor 1 protein) (SNF5 homolog) (hSNF5)	Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. 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). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. {ECO:0000250\|UniProtKB:Q9Z0H3, ECO:0000269\|PubMed:10078207, ECO:0000269\|PubMed:12226744, ECO:0000269\|PubMed:14604992, ECO:0000269\|PubMed:16267391, ECO:0000269\|PubMed:16314535, ECO:0000269\|PubMed:9448295}.
Q12830	BPTF	S2455	ochoa	Nucleosome-remodeling factor subunit BPTF (Bromodomain and PHD finger-containing transcription factor) (Fetal Alz-50 clone 1 protein) (Fetal Alzheimer antigen)	Regulatory subunit of the ATP-dependent NURF-1 and NURF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:14609955, PubMed:28801535). The NURF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NURF-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NURF-1 ISWI chromatin-remodeling complex, binds to the promoters of En1 and En2 to positively regulate their expression and promote brain development (PubMed:14609955). Histone-binding protein which binds to H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of active genes (PubMed:16728976, PubMed:16728978). Binds to histone H3 tails dimethylated on 'Lys-4' (H3K4Me2) to a lesser extent (PubMed:16728976, PubMed:16728978, PubMed:18042461). May also regulate transcription through direct binding to DNA or transcription factors (PubMed:10575013). {ECO:0000269\|PubMed:10575013, ECO:0000269\|PubMed:14609955, ECO:0000269\|PubMed:16728976, ECO:0000269\|PubMed:16728978, ECO:0000269\|PubMed:18042461, ECO:0000269\|PubMed:28801535}.
Q12872	SFSWAP	S891	ochoa	Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog)	Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:8940107}.
Q12888	TP53BP1	S310	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S349	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S356	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S888	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1310	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1634	ochoa	TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1)	Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250\|UniProtKB:P70399, ECO:0000269\|PubMed:12364621, ECO:0000269\|PubMed:17190600, ECO:0000269\|PubMed:21144835, ECO:0000269\|PubMed:22553214, ECO:0000269\|PubMed:23333306, ECO:0000269\|PubMed:23345425, ECO:0000269\|PubMed:23727112, ECO:0000269\|PubMed:23760478, ECO:0000269\|PubMed:27153538, ECO:0000269\|PubMed:28241136, ECO:0000269\|PubMed:31135337, ECO:0000269\|PubMed:37696958}.
Q12888	TP53BP1	S1635	ochoa\|psp	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}.
Q12986	NFX1	S140	ochoa	Transcriptional repressor NF-X1 (EC 2.3.2.-) (Nuclear transcription factor, X box-binding protein 1)	Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269\|PubMed:10500182, ECO:0000269\|PubMed:15371341, ECO:0000269\|PubMed:17267499}.
Q13085	ACACA	S50	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	S513	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}.
Q13131	PRKAA1	S496	ochoa\|psp	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13131	PRKAA1	S517	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13131	PRKAA1	S520	ochoa	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13136	PPFIA1	S232	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13136	PPFIA1	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}.
Q13148	TARDBP	S369	psp	TAR DNA-binding protein 43 (TDP-43)	RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:19765185, PubMed:23398327). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563). {ECO:0000269\|PubMed:11285240, ECO:0000269\|PubMed:17481916, ECO:0000269\|PubMed:19760257, ECO:0000269\|PubMed:19765185, ECO:0000269\|PubMed:21358640, ECO:0000269\|PubMed:23398327, ECO:0000269\|PubMed:23519609, ECO:0000269\|PubMed:24240615, ECO:0000269\|PubMed:24464995, ECO:0000269\|PubMed:25678563, ECO:0000269\|PubMed:27123980, ECO:0000269\|PubMed:28794432, ECO:0000269\|PubMed:29438978, ECO:0000269\|PubMed:30464263, ECO:0000269\|PubMed:30520513}.
Q13242	SRSF9	S189	ochoa	Serine/arginine-rich splicing factor 9 (Pre-mRNA-splicing factor SRp30C) (Splicing factor, arginine/serine-rich 9)	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:10196175, ECO:0000269\|PubMed:11875052, ECO:0000269\|PubMed:12024014, ECO:0000269\|PubMed:12604611, ECO:0000269\|PubMed:15009090, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:15695522, ECO:0000269\|PubMed:7556075}.
Q13439	GOLGA4	S27	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}.
Q13439	GOLGA4	S78	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}.
Q13464	ROCK1	S1098	ochoa	Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)	Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250\|UniProtKB:P70335, ECO:0000250\|UniProtKB:Q8MIT6, ECO:0000269\|PubMed:10436159, ECO:0000269\|PubMed:10652353, ECO:0000269\|PubMed:11018042, ECO:0000269\|PubMed:11283607, ECO:0000269\|PubMed:17158456, ECO:0000269\|PubMed:18573880, ECO:0000269\|PubMed:18694941, ECO:0000269\|PubMed:19036714, ECO:0000269\|PubMed:19131646, ECO:0000269\|PubMed:19181962, ECO:0000269\|PubMed:19997641, ECO:0000269\|PubMed:21072057, ECO:0000269\|PubMed:23093407, ECO:0000269\|PubMed:23355470, ECO:0000269\|PubMed:8617235, ECO:0000269\|PubMed:9722579}.
Q13480	GAB1	S256	ochoa	GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1)	Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway (PubMed:29408807). {ECO:0000269\|PubMed:29408807}.
Q13501	SQSTM1	S170	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S277	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13501	SQSTM1	S355	ochoa	Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62)	Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250\|UniProtKB:Q64337, ECO:0000269\|PubMed:10356400, ECO:0000269\|PubMed:10747026, ECO:0000269\|PubMed:11244088, ECO:0000269\|PubMed:12471037, ECO:0000269\|PubMed:15340068, ECO:0000269\|PubMed:15802564, ECO:0000269\|PubMed:15911346, ECO:0000269\|PubMed:15953362, ECO:0000269\|PubMed:16079148, ECO:0000269\|PubMed:16286508, ECO:0000269\|PubMed:17580304, ECO:0000269\|PubMed:19931284, ECO:0000269\|PubMed:20168092, ECO:0000269\|PubMed:20452972, ECO:0000269\|PubMed:22017874, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:24128730, ECO:0000269\|PubMed:25101860, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:27368102, ECO:0000269\|PubMed:28380357, ECO:0000269\|PubMed:28404643, ECO:0000269\|PubMed:29343546, ECO:0000269\|PubMed:29496741, ECO:0000269\|PubMed:29507397, ECO:0000269\|PubMed:31857589, ECO:0000269\|PubMed:33393215, ECO:0000269\|PubMed:33472082, ECO:0000269\|PubMed:33509017, ECO:0000269\|PubMed:34471133, ECO:0000269\|PubMed:34893540, ECO:0000269\|PubMed:35831301, ECO:0000269\|PubMed:37306101, ECO:0000269\|PubMed:37802024}.
Q13523	PRP4K	S559	ochoa	Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 kinase) (PRP4 pre-mRNA-processing factor 4 homolog)	Serine/threonine kinase involved in spliceosomal assembly as well as mitosis and signaling regulation (PubMed:10799319, PubMed:12077342, PubMed:17513757, PubMed:17998396). Connects chromatin mediated regulation of transcription and pre-mRNA splicing (PubMed:12077342). During spliceosomal assembly, interacts with and phosphorylates PRPF6 and PRPF31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), to facilitate the formation of the spliceosome B complex. Plays a role in regulating transcription and the spindle assembly checkpoint (SAC) (PubMed:20118938). Associates with U5 snRNP and NCOR1 deacetylase complexes which may allow a coordination of pre-mRNA splicing with chromatin remodeling events involved in transcriptional regulation (PubMed:12077342). Associates and probably phosphorylates SMARCA4 and NCOR1 (PubMed:12077342). Phosphorylates SRSF1 (PubMed:11418604). Associates with kinetochores during mitosis and is necessary for recruitment and maintenance of the checkpoint proteins such as MAD1L1 and MAD12L1 at the kinetochores (PubMed:17998396). Phosphorylates and regulates the activity of the transcription factors such as ELK1 and KLF13 (PubMed:10799319, PubMed:17513757). Phosphorylates nuclear YAP1 and WWTR1/TAZ which induces nuclear exclusion and regulates Hippo signaling pathway, involved in tissue growth control (PubMed:29695716). {ECO:0000269\|PubMed:10799319, ECO:0000269\|PubMed:11418604, ECO:0000269\|PubMed:12077342, ECO:0000269\|PubMed:17513757, ECO:0000269\|PubMed:17998396, ECO:0000269\|PubMed:20118938, ECO:0000269\|PubMed:29695716}.
Q13526	PIN1	S32	ochoa	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1)	Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (PubMed:23623683, PubMed:27561354). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells (PubMed:29686383). Catalyzes cis-trans isomerization of phosphorylated phosphoglycerate kinase PGK1 under hypoxic conditions to promote its binding to the TOM complex and targeting to the mitochondrion (PubMed:26942675). {ECO:0000269\|PubMed:15664191, ECO:0000269\|PubMed:16644721, ECO:0000269\|PubMed:17828269, ECO:0000269\|PubMed:21497122, ECO:0000269\|PubMed:22033920, ECO:0000269\|PubMed:22608923, ECO:0000269\|PubMed:23623683, ECO:0000269\|PubMed:26942675, ECO:0000269\|PubMed:27561354, ECO:0000269\|PubMed:29686383}.
Q13586	STIM1	S608	ochoa\|psp	Stromal interaction molecule 1	Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671). {ECO:0000269\|PubMed:15866891, ECO:0000269\|PubMed:16005298, ECO:0000269\|PubMed:16208375, ECO:0000269\|PubMed:16537481, ECO:0000269\|PubMed:16733527, ECO:0000269\|PubMed:16766533, ECO:0000269\|PubMed:16807233, ECO:0000269\|PubMed:18854159, ECO:0000269\|PubMed:19182790, ECO:0000269\|PubMed:19249086, ECO:0000269\|PubMed:19622606, ECO:0000269\|PubMed:19706554, ECO:0000269\|PubMed:22464749, ECO:0000269\|PubMed:24069340, ECO:0000269\|PubMed:24351972, ECO:0000269\|PubMed:24591628, ECO:0000269\|PubMed:24621671, ECO:0000269\|PubMed:25326555, ECO:0000269\|PubMed:26322679, ECO:0000269\|PubMed:28219928, ECO:0000269\|PubMed:32415068}.
Q13613	MTMR1	S645	ochoa	Phosphatidylinositol-3-phosphate phosphatase MTMR1 (EC 3.1.3.-) (Myotubularin-related protein 1) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate, generating phosphatidylinositol (PubMed:11733541, PubMed:27018598). Could also dephosphorylate phosphatidylinositol 3,5-bisphosphate to produce phosphatidylinositol 5-phosphate (PubMed:27018598). {ECO:0000269\|PubMed:11733541, ECO:0000269\|PubMed:27018598}.
Q13615	MTMR3	S903	ochoa	Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 (EC 3.1.3.95) (FYVE domain-containing dual specificity protein phosphatase 1) (FYVE-DSP1) (Myotubularin-related protein 3) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Zinc finger FYVE domain-containing protein 10)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:10733931, PubMed:11302699, PubMed:11676921, PubMed:12646134). Decreases the levels of phosphatidylinositol 3-phosphate, a phospholipid found in cell membranes where it acts as key regulator of both cell signaling and intracellular membrane traffic (PubMed:11302699, PubMed:11676921, PubMed:12646134). Could also have a molecular sequestering/adapter activity and regulate biological processes independently of its phosphatase activity. It includes the regulation of midbody abscission during mitotic cytokinesis (PubMed:25659891). {ECO:0000269\|PubMed:10733931, ECO:0000269\|PubMed:11302699, ECO:0000269\|PubMed:11676921, ECO:0000269\|PubMed:12646134, ECO:0000269\|PubMed:25659891}.
Q13620	CUL4B	S53	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13835	PKP1	S59	psp	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q13905	RAPGEF1	S335	ochoa	Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G)	Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1 (PubMed:12432078). Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:7806500}.
Q14157	UBAP2L	S467	ochoa	Ubiquitin-associated protein 2-like (Protein NICE-4) (RNA polymerase II degradation factor UBAP2L)	Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled nucleotide excision repair (TC-NER) machinery fails to resolve DNA damage (PubMed:35633597). Plays an important role in the activity of long-term repopulating hematopoietic stem cells (LT-HSCs) (By similarity). Is a regulator of stress granule assembly, required for their efficient formation (PubMed:29395067, PubMed:35977029). Required for proper brain development and neocortex lamination (By similarity). {ECO:0000250\|UniProtKB:Q80X50, ECO:0000269\|PubMed:29395067, ECO:0000269\|PubMed:35633597}.
Q14185	DOCK1	S1751	ochoa	Dedicator of cytokinesis protein 1 (180 kDa protein downstream of CRK) (DOCK180)	Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (PubMed:19004829). Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1 (PubMed:8657152). {ECO:0000269\|PubMed:19004829, ECO:0000269\|PubMed:8657152}.
Q14432	PDE3A	S428	ochoa\|psp	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}.
Q14432	PDE3A	S465	psp	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}.
Q14676	MDC1	S495	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}.
Q14687	GSE1	S899	ochoa	Genetic suppressor element 1	None
Q14699	RFTN1	Y165	ochoa	Raftlin (Cell migration-inducing gene 2 protein) (Raft-linking protein)	Involved in protein trafficking via association with clathrin and AP2 complex (PubMed:21266579, PubMed:27022195). Upon bacterial lipopolysaccharide stimulation, mediates internalization of TLR4 to endosomes in dendritic cells and macrophages; and internalization of poly(I:C) to TLR3-positive endosomes in myeloid dendritic cells and epithelial cells; resulting in activation of TICAM1-mediated signaling and subsequent IFNB1 production (PubMed:21266579, PubMed:27022195). Involved in T-cell antigen receptor-mediated signaling by regulating tyrosine kinase LCK localization, T-cell dependent antibody production and cytokine secretion (By similarity). May regulate B-cell antigen receptor-mediated signaling (PubMed:12805216). May play a pivotal role in the formation and/or maintenance of lipid rafts (PubMed:12805216). {ECO:0000250\|UniProtKB:Q6A0D4, ECO:0000269\|PubMed:12805216, ECO:0000269\|PubMed:21266579, ECO:0000269\|PubMed:27022195}.
Q14739	LBR	S59	ochoa	Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (LMN2R) (Lamin-B receptor) (Sterol C14-reductase)	Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963). {ECO:0000250\|UniProtKB:Q3U9G9, ECO:0000269\|PubMed:10828963, ECO:0000269\|PubMed:12618959, ECO:0000269\|PubMed:16784888, ECO:0000269\|PubMed:21327084, ECO:0000269\|PubMed:27336722, ECO:0000269\|PubMed:9630650}.
Q14980	NUMA1	S1782	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	S1830	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	S1834	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1837	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q15032	R3HDM1	S383	ochoa	R3H domain-containing protein 1	None
Q15036	SNX17	S326	ochoa	Sorting nexin-17	Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels (PubMed:15121882, PubMed:15769472, PubMed:39587083). Binds to NPxY sequences in the cytoplasmic tails of target cargos (PubMed:21512128). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (PubMed:22492727, PubMed:28892079, PubMed:39587083). Also required for maintenance of normal cell surface levels of APP and LRP1 (PubMed:16712798, PubMed:19005208). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (PubMed:16712798). {ECO:0000269\|PubMed:15121882, ECO:0000269\|PubMed:15769472, ECO:0000269\|PubMed:16712798, ECO:0000269\|PubMed:19005208, ECO:0000269\|PubMed:21512128, ECO:0000269\|PubMed:22492727, ECO:0000269\|PubMed:28892079}.
Q15052	ARHGEF6	S131	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15052	ARHGEF6	S555	ochoa	Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)	Acts as a RAC1 guanine nucleotide exchange factor (GEF).
Q15058	KIF14	S1217	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	S4382	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	S4386	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	Y4612	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	S4616	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	S4620	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}.
Q15398	DLGAP5	S624	ochoa	Disks large-associated protein 5 (DAP-5) (Discs large homolog 7) (Disks large-associated protein DLG7) (Hepatoma up-regulated protein) (HURP)	Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269\|PubMed:12527899, ECO:0000269\|PubMed:14699157, ECO:0000269\|PubMed:15145941}.
Q15464	SHB	S307	ochoa	SH2 domain-containing adapter protein B	Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells. {ECO:0000269\|PubMed:10828022, ECO:0000269\|PubMed:10837138, ECO:0000269\|PubMed:12084069, ECO:0000269\|PubMed:12464388, ECO:0000269\|PubMed:12520086, ECO:0000269\|PubMed:15026417, ECO:0000269\|PubMed:15919073, ECO:0000269\|PubMed:8806685, ECO:0000269\|PubMed:9484780, ECO:0000269\|PubMed:9751119}.
Q15555	MAPRE2	S209	ochoa	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15555	MAPRE2	S222	ochoa	Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)	Adapter protein that is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. Therefore, ensures mitotic progression and genome stability (PubMed:27030108). Acts as a central regulator of microtubule reorganization in apico-basal epithelial differentiation (By similarity). Plays a role during oocyte meiosis by regulating microtubule dynamics (By similarity). Participates in neurite growth by interacting with plexin B3/PLXNB3 and microtubule reorganization during apico-basal epithelial differentiation (PubMed:22373814). Also plays an essential role for cell migration and focal adhesion dynamics. Mechanistically, recruits HAX1 to microtubules in order to regulate focal adhesion dynamics (PubMed:26527684). {ECO:0000250\|UniProtKB:Q8R001, ECO:0000269\|PubMed:22373814, ECO:0000269\|PubMed:23844040, ECO:0000269\|PubMed:26527684, ECO:0000269\|PubMed:27030108}.
Q15722	LTB4R	S310	ochoa\|psp	Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (Chemoattractant receptor-like 1) (G-protein coupled receptor 16) (P2Y purinoceptor 7) (P2Y7)	Receptor for extracellular ATP > UTP and ADP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.
Q15751	HERC1	S1502	ochoa	Probable E3 ubiquitin-protein ligase HERC1 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 1) (HECT-type E3 ubiquitin transferase HERC1) (p532) (p619)	Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269\|PubMed:15642342, ECO:0000269\|PubMed:8861955, ECO:0000269\|PubMed:9233772}.
Q15811	ITSN1	S976	ochoa	Intersectin-1 (SH3 domain-containing protein 1A) (SH3P17)	Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (PubMed:22648170). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (By similarity). Inhibits ARHGAP31 activity toward RAC1 (PubMed:11744688). {ECO:0000250\|UniProtKB:Q9WVE9, ECO:0000250\|UniProtKB:Q9Z0R4, ECO:0000269\|PubMed:11584276, ECO:0000269\|PubMed:11744688, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:29887380}.; FUNCTION: [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250\|UniProtKB:Q9Z0R4}.
Q16204	CCDC6	S351	ochoa	Coiled-coil domain-containing protein 6 (Papillary thyroid carcinoma-encoded protein) (Protein H4)	None
Q16512	PKN1	S566	ochoa	Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)	PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269\|PubMed:11104762, ECO:0000269\|PubMed:12514133, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:21224381, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:24248594, ECO:0000269\|PubMed:8557118, ECO:0000269\|PubMed:8621664, ECO:0000269\|PubMed:9175763}.
Q16513	PKN2	S19	ochoa	Serine/threonine-protein kinase N2 (EC 2.7.11.13) (PKN gamma) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2)	PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (PubMed:27104747). {ECO:0000269\|PubMed:10226025, ECO:0000269\|PubMed:10926925, ECO:0000269\|PubMed:11777936, ECO:0000269\|PubMed:11781095, ECO:0000269\|PubMed:15123640, ECO:0000269\|PubMed:15364941, ECO:0000269\|PubMed:17332740, ECO:0000269\|PubMed:20188095, ECO:0000269\|PubMed:20974804, ECO:0000269\|PubMed:21754995, ECO:0000269\|PubMed:27104747, ECO:0000269\|PubMed:9121475}.; FUNCTION: (Microbial infection) Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. {ECO:0000269\|PubMed:15364941}.
Q16891	IMMT	S103	ochoa\|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}.
Q27J81	INF2	S1192	ochoa	Inverted formin-2 (HBEBP2-binding protein C)	Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.
Q27J81	INF2	S1194	ochoa	Inverted formin-2 (HBEBP2-binding protein C)	Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.
Q29RF7	PDS5A	S1172	ochoa	Sister chromatid cohesion protein PDS5 homolog A (Cell proliferation-inducing gene 54 protein) (Sister chromatid cohesion protein 112) (SCC-112)	Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19907496}.
Q29RF7	PDS5A	S1177	ochoa	Sister chromatid cohesion protein PDS5 homolog A (Cell proliferation-inducing gene 54 protein) (Sister chromatid cohesion protein 112) (SCC-112)	Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19907496}.
Q2KHR3	QSER1	S981	ochoa	Glutamine and serine-rich protein 1	Plays an essential role in the protection and maintenance of transcriptional and developmental programs. Protects many bivalent promoters and poised enhancers from hypermethylation, showing a marked preference for these regulatory elements over other types of promoters or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in a common complex to inhibit the binding of DNMT3A/3B and therefore de novo methylation. {ECO:0000269\|PubMed:33833093}.
Q2M1P5	KIF7	S452	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}.
Q2M2I8	AAK1	S668	ochoa	AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1)	Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis (PubMed:11877457, PubMed:11877461, PubMed:12952931, PubMed:14617351, PubMed:17494869, PubMed:25653444). Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1 (PubMed:17494869). Preferentially, may phosphorylate substrates on threonine residues (PubMed:11877457, PubMed:18657069). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (PubMed:12952931). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (PubMed:18657069). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (PubMed:21464124). {ECO:0000269\|PubMed:11877457, ECO:0000269\|PubMed:11877461, ECO:0000269\|PubMed:12952931, ECO:0000269\|PubMed:14617351, ECO:0000269\|PubMed:17494869, ECO:0000269\|PubMed:18657069, ECO:0000269\|PubMed:21464124, ECO:0000269\|PubMed:25653444}.; FUNCTION: (Microbial infection) By regulating clathrin-mediated endocytosis, AAK1 plays a role in the entry of hepatitis C virus as well as for the lifecycle of other viruses such as Ebola and Dengue. {ECO:0000269\|PubMed:25653444, ECO:0000305\|PubMed:31136173}.
Q32MZ4	LRRFIP1	S110	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}.
Q4G0J3	LARP7	S244	ochoa	La-related protein 7 (La ribonucleoprotein domain family member 7) (hLARP7) (P-TEFb-interaction protein for 7SK stability) (PIP7S)	RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function (PubMed:18249148, PubMed:32017898). Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (PubMed:18249148, PubMed:18483487). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:18249148, PubMed:18483487). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (PubMed:18281698, PubMed:18483487). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing (PubMed:32017898). Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (PubMed:32017898). U6 snRNA processing is required for spermatogenesis (By similarity). {ECO:0000250\|UniProtKB:Q05CL8, ECO:0000269\|PubMed:18249148, ECO:0000269\|PubMed:18281698, ECO:0000269\|PubMed:18483487, ECO:0000269\|PubMed:28254838, ECO:0000269\|PubMed:32017898}.
Q4KMP7	TBC1D10B	S282	ochoa	TBC1 domain family member 10B (Rab27A-GAP-beta)	Acts as a GTPase-activating protein for RAB3A, RAB22A, RAB27A, and RAB35. Does not act on RAB2A and RAB6A. {ECO:0000269\|PubMed:16923811, ECO:0000269\|PubMed:19077034}.
Q4L180	FILIP1L	S1041	ochoa	Filamin A-interacting protein 1-like (130 kDa GPBP-interacting protein) (90 kDa GPBP-interacting protein) (Protein down-regulated in ovarian cancer 1) (DOC-1)	Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269\|PubMed:18794120}.
Q4V328	GRIPAP1	S655	ochoa	GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]	Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity). {ECO:0000250\|UniProtKB:Q9JHZ4}.; FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity. {ECO:0000269\|PubMed:17761173}.
Q53EL6	PDCD4	S68	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}.
Q53H80	AKIRIN2	S111	ochoa	Akirin-2	Molecular adapter that acts as a bridge between a variety of multiprotein complexes, and which is involved in embryonic development, immunity, myogenesis and brain development (PubMed:34711951). Plays a key role in nuclear protein degradation by promoting import of proteasomes into the nucleus: directly binds to fully assembled 20S proteasomes at one end and to nuclear import receptor IPO9 at the other end, bridging them together and mediating the import of pre-assembled proteasome complexes through the nuclear pore (PubMed:34711951). Involved in innate immunity by regulating the production of interleukin-6 (IL6) downstream of Toll-like receptor (TLR): acts by bridging the NF-kappa-B inhibitor NFKBIZ and the SWI/SNF complex, leading to promote induction of IL6 (By similarity). Also involved in adaptive immunity by promoting B-cell activation (By similarity). Involved in brain development: required for the survival and proliferation of cerebral cortical progenitor cells (By similarity). Involved in myogenesis: required for skeletal muscle formation and skeletal development, possibly by regulating expression of muscle differentiation factors (By similarity). Also plays a role in facilitating interdigital tissue regression during limb development (By similarity). {ECO:0000250\|UniProtKB:B1AXD8, ECO:0000269\|PubMed:34711951}.
Q5F1R6	DNAJC21	S511	ochoa	DnaJ homolog subfamily C member 21 (DnaJ homolog subfamily A member 5) (Protein GS3)	May act as a co-chaperone for HSP70. May play a role in ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S subunit. Binds the precursor 45S rRNA. {ECO:0000269\|PubMed:27346687}.
Q5HYJ3	FAM76B	S148	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5JRA6	MIA3	S1731	ochoa	Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)	Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum (PubMed:19269366, PubMed:27138255). Required for correct assembly of COPII coat components at endoplasmic reticulum exit sites (ERES) and for the localization of SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and PREB/SEC12 to ERES (PubMed:28442536). {ECO:0000269\|PubMed:19269366, ECO:0000269\|PubMed:27138255, ECO:0000269\|PubMed:28442536}.
Q5JSH3	WDR44	S561	ochoa	WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11)	Downstream effector for Rab11 which regulates Rab11 intracellular membrane trafficking functions such as endocytic recycling, intracellular ciliogenesis and protein export (PubMed:31204173, PubMed:32344433). ATK1-mediated phosphorylation of WDR44 induces binding to Rab11 which activates endocytic recycling of transferrin receptor back to the plasma membrane (PubMed:31204173). When bound to Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-RAB11FIP3 complex, therefore inhibiting preciliary trafficking and ciliogenesis (PubMed:31204173). Participates in neo-synthesized protein export by connecting the endoplasmic reticulum (ER) with the endosomal tubule via direct interactions with the integral ER proteins VAPA or VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route (PubMed:32344433). {ECO:0000269\|PubMed:31204173, ECO:0000269\|PubMed:32344433}.
Q5JSZ5	PRRC2B	S1676	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5JTV8	TOR1AIP1	S305	ochoa\|psp	Torsin-1A-interacting protein 1 (Lamin-associated protein 1B) (LAP1B)	Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269\|PubMed:23569223}.
Q5SW79	CEP170	S861	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}.
Q5T1M5	FKBP15	S297	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T1M5	FKBP15	S301	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T200	ZC3H13	S328	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T200	ZC3H13	S338	ochoa	Zinc finger CCCH domain-containing protein 13	Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250\|UniProtKB:E9Q784}.
Q5T200	ZC3H13	S865	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}.
Q5TBA9	FRY	S1936	ochoa	Protein furry homolog	Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. {ECO:0000269\|PubMed:22753416}.
Q5TCX8	MAP3K21	S779	ochoa	Mitogen-activated protein kinase kinase kinase 21 (EC 2.7.11.25) (Mitogen-activated protein kinase kinase kinase MLK4) (Mixed lineage kinase 4)	Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways. {ECO:0000269\|PubMed:21602844}.
Q5THJ4	VPS13D	S2682	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	S1190	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	S1542	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	S1547	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}.
Q5VT52	RPRD2	S936	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VT52	RPRD2	S1134	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5VU43	PDE4DIP	S726	ochoa	Myomegalin (Cardiomyopathy-associated protein 2) (Phosphodiesterase 4D-interacting protein)	Functions as an anchor sequestering components of the cAMP-dependent pathway to Golgi and/or centrosomes (By similarity). {ECO:0000250\|UniProtKB:Q9WUJ3}.; FUNCTION: [Isoform 13]: Participates in microtubule dynamics, promoting microtubule assembly. Depending upon the cell context, may act at the level of the Golgi apparatus or that of the centrosome (PubMed:25217626, PubMed:27666745, PubMed:28814570, PubMed:29162697). In complex with AKAP9, recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:27666745, PubMed:28814570). In complex with AKAP9, EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation and extension from the centrosome to the cell periphery, a crucial process for directed cell migration, mitotic spindle orientation and cell-cycle progression (PubMed:29162697). {ECO:0000269\|PubMed:25217626, ECO:0000269\|PubMed:27666745, ECO:0000269\|PubMed:28814570, ECO:0000269\|PubMed:29162697}.
Q5VUA4	ZNF318	S1610	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q5VZ89	DENND4C	S989	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}.
Q5W0Z9	ZDHHC20	S305	ochoa	Palmitoyltransferase ZDHHC20 (EC 2.3.1.225) (Acyltransferase ZDHHC20) (EC 2.3.1.-) (DHHC domain-containing cysteine-rich protein 20) (DHHC20) (Zinc finger DHHC domain-containing protein 20)	Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (PubMed:27153536, PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation (PubMed:27153536). Has a preference for acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245). May palmitoylate CALHM1 subunit of gustatory voltage-gated ion channels and modulate channel gating and kinetics. {ECO:0000250\|UniProtKB:Q5Y5T1, ECO:0000269\|PubMed:27153536, ECO:0000269\|PubMed:29326245, ECO:0000269\|PubMed:33219126}.; FUNCTION: (Microbial infection) Dominant palmitoyltransferase responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike protein. Through a sequential action with ZDHHC9, rapidly and efficiently palmitoylates spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell. {ECO:0000269\|PubMed:34599882}.
Q68CZ2	TNS3	S1105	ochoa	Tensin-3 (EC 3.1.3.-) (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)	May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115). EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115). Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433). Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433). Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021). Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841). {ECO:0000250\|UniProtKB:Q5SSZ5, ECO:0000269\|PubMed:17643115, ECO:0000269\|PubMed:26166433, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:31905841, ECO:0000269\|PubMed:35687021, ECO:0000305}.
Q68CZ2	TNS3	S1113	ochoa	Tensin-3 (EC 3.1.3.-) (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)	May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in the dissociation of the integrin-tensin-actin complex (PubMed:17643115). EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1 (PubMed:17643115). Increases DOCK5 guanine nucleotide exchange activity towards Rac and plays a role in osteoclast podosome organization (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces TNS3 phosphorylation which changes its binding preference from DLC1 to the p85 regulatory subunit of the PI3K kinase complex, displacing PI3K inhibitor PTEN and resulting in translocation of the TNS3-p85 complex to the leading edge of migrating cells to promote RAC1 activation (PubMed:26166433). Meanwhile, PTEN switches binding preference from p85 to DLC1 and the PTEN-DLC1 complex translocates to the posterior of migrating cells to activate RHOA (PubMed:26166433). Acts as an adapter protein by bridging the association of scaffolding protein PEAK1 with integrins ITGB1, ITGB3 and ITGB5 which contributes to the promotion of cell migration (PubMed:35687021). Controls tonsil-derived mesenchymal stem cell proliferation and differentiation by regulating the activity of integrin ITGB1 (PubMed:31905841). {ECO:0000250\|UniProtKB:Q5SSZ5, ECO:0000269\|PubMed:17643115, ECO:0000269\|PubMed:26166433, ECO:0000269\|PubMed:26427649, ECO:0000269\|PubMed:31905841, ECO:0000269\|PubMed:35687021, ECO:0000305}.
Q68DQ2	CRYBG3	S2094	ochoa	Very large A-kinase anchor protein (vlAKAP) (Beta/gamma crystallin domain-containing protein 3)	[Isoform vlAKAP]: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269\|PubMed:25097019}.
Q6AI08	HEATR6	S385	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6AI08	HEATR6	S388	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6AI08	HEATR6	S389	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6H8Q1	ABLIM2	S280	ochoa	Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2)	May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269\|PubMed:17194709}.
Q6H8Q1	ABLIM2	S282	ochoa	Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2)	May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269\|PubMed:17194709}.
Q6IA17	SIGIRR	S373	ochoa	Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)	Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP. {ECO:0000269\|PubMed:12925853, ECO:0000269\|PubMed:14715412, ECO:0000269\|PubMed:15866876, ECO:0000269\|PubMed:25963006}.
Q6L8Q7	PDE12	S214	ochoa	2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4)	Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of oligoadenylates (PubMed:21666256, PubMed:26055709, PubMed:30389976). Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells (PubMed:26055709). {ECO:0000269\|PubMed:15231837, ECO:0000269\|PubMed:21245038, ECO:0000269\|PubMed:21666256, ECO:0000269\|PubMed:22285541, ECO:0000269\|PubMed:26055709, ECO:0000269\|PubMed:30389976}.
Q6P1L5	FAM117B	S404	ochoa	Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein)	None
Q6PKG0	LARP1	S574	ochoa	La-related protein 1 (La ribonucleoprotein domain family member 1)	RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543). {ECO:0000269\|PubMed:20430826, ECO:0000269\|PubMed:23711370, ECO:0000269\|PubMed:24532714, ECO:0000269\|PubMed:25940091, ECO:0000269\|PubMed:26206669, ECO:0000269\|PubMed:28379136, ECO:0000269\|PubMed:28650797, ECO:0000269\|PubMed:28673543, ECO:0000269\|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269\|PubMed:26735137}.
Q6R327	RICTOR	S1282	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1571	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1577	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	S1581	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6T4R5	NHS	S1319	ochoa	Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein)	May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development. {ECO:0000269\|PubMed:20332100}.
Q6VN20	RANBP10	S355	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S410	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S411	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VN20	RANBP10	S412	ochoa	Ran-binding protein 10 (RanBP10)	May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). {ECO:0000250\|UniProtKB:Q6VN19, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q6VY07	PACS1	S485	ochoa	Phosphofurin acidic cluster sorting protein 1 (PACS-1)	Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (By similarity). {ECO:0000250\|UniProtKB:Q8K212, ECO:0000269\|PubMed:11331585, ECO:0000269\|PubMed:15692563}.
Q6VY07	PACS1	S519	ochoa	Phosphofurin acidic cluster sorting protein 1 (PACS-1)	Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (By similarity). {ECO:0000250\|UniProtKB:Q8K212, ECO:0000269\|PubMed:11331585, ECO:0000269\|PubMed:15692563}.
Q6WCQ1	MPRIP	S179	ochoa	Myosin phosphatase Rho-interacting protein (M-RIP) (Rho-interacting protein 3) (RIP3) (p116Rip)	Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250\|UniProtKB:P97434, ECO:0000269\|PubMed:15545284, ECO:0000269\|PubMed:16257966}.
Q6XZF7	DNMBP	S1351	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6XZF7	DNMBP	S1359	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6XZF7	DNMBP	S1361	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6Y7W6	GIGYF2	S367	ochoa	GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein)	Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:31439631, PubMed:35878012). In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:31439631). Also recruits and bridges the association of the 4EHP complex with the decapping effector protein DDX6, which is required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). In association with EIF4E2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide (PubMed:32726578). GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578). {ECO:0000269\|PubMed:12771153, ECO:0000269\|PubMed:22751931, ECO:0000269\|PubMed:31439631, ECO:0000269\|PubMed:32726578, ECO:0000269\|PubMed:35878012}.; FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1. {ECO:0000269\|PubMed:35878012}.
Q6Y7W6	GIGYF2	S374	ochoa	GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein)	Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:31439631, PubMed:35878012). In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:31439631). Also recruits and bridges the association of the 4EHP complex with the decapping effector protein DDX6, which is required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). In association with EIF4E2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide (PubMed:32726578). GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578). {ECO:0000269\|PubMed:12771153, ECO:0000269\|PubMed:22751931, ECO:0000269\|PubMed:31439631, ECO:0000269\|PubMed:32726578, ECO:0000269\|PubMed:35878012}.; FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1. {ECO:0000269\|PubMed:35878012}.
Q6ZRS2	SRCAP	S248	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q6ZRS2	SRCAP	S2787	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q6ZU80	CEP128	S1033	ochoa	Centrosomal protein of 128 kDa (Cep128)	None
Q6ZUJ8	PIK3AP1	S720	ochoa	Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1)	Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269\|PubMed:15893754}.
Q6ZUJ8	PIK3AP1	S727	ochoa	Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1)	Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269\|PubMed:15893754}.
Q6ZUJ8	PIK3AP1	S730	ochoa	Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1)	Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269\|PubMed:15893754}.
Q6ZVL6	KIAA1549L	S1536	ochoa	UPF0606 protein KIAA1549L	None
Q70E73	RAPH1	S536	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q70E73	RAPH1	S538	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q71RC2	LARP4	S382	ochoa	La-related protein 4 (La ribonucleoprotein domain family member 4)	RNA binding protein that binds to the poly-A tract of mRNA molecules (PubMed:21098120). Associates with the 40S ribosomal subunit and with polysomes (PubMed:21098120). Plays a role in the regulation of mRNA translation (PubMed:21098120). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987, PubMed:27615744). {ECO:0000269\|PubMed:21098120, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:27615744}.
Q765P7	MTSS2	S322	ochoa	Protein MTSS 2 (Actin-bundling with BAIAP2 homology protein 1) (ABBA-1) (MTSS1-like protein)	Involved in plasma membrane dynamics. Potentiated PDGF-mediated formation of membrane ruffles and lamellipodia in fibroblasts, acting via RAC1 activation (PubMed:14752106). May function in actin bundling (PubMed:14752106). {ECO:0000269\|PubMed:14752106}.
Q765P7	MTSS2	S639	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	S380	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}.
Q7L2J0	MEPCE	S330	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}.
Q7L9B9	EEPD1	S102	ochoa	Endonuclease/exonuclease/phosphatase family domain-containing protein 1	None
Q7LBC6	KDM3B	S455	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}.
Q7Z2W4	ZC3HAV1	S492	ochoa	Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)	Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of RIGI signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269\|PubMed:18225958, ECO:0000269\|PubMed:21102435, ECO:0000269\|PubMed:21876179, ECO:0000269\|PubMed:22720057}.
Q7Z3J3	RGPD4	S1472	ochoa	RanBP2-like and GRIP domain-containing protein 4	None
Q7Z3J3	RGPD4	S1583	ochoa	RanBP2-like and GRIP domain-containing protein 4	None
Q7Z417	NUFIP2	S373	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S374	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S376	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S572	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S582	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z417	NUFIP2	S586	ochoa	FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2)	Binds RNA. {ECO:0000269\|PubMed:12837692}.
Q7Z460	CLASP1	S545	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S552	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S588	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S590	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z460	CLASP1	S636	ochoa	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z4V5	HDGFL2	S230	ochoa	Hepatoma-derived growth factor-related protein 2 (HDGF-related protein 2) (HRP-2) (Hepatoma-derived growth factor 2) (HDGF-2)	Acts as an epigenetic regulator of myogenesis in cooperation with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350). Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350). Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (PubMed:26721387). Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2 (PubMed:26721387, PubMed:32459350). Involved in cellular growth control, through the regulation of cyclin D1 expression (PubMed:25689719). {ECO:0000269\|PubMed:25689719, ECO:0000269\|PubMed:26721387, ECO:0000269\|PubMed:32459350}.
Q7Z5J4	RAI1	S568	ochoa	Retinoic acid-induced protein 1	Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269\|PubMed:22578325}.
Q7Z6E9	RBBP6	S1263	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6E9	RBBP6	S1695	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6Z7	HUWE1	S3555	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	S555	ochoa	Pleckstrin homology-like domain family B member 2 (Protein LL5-beta)	Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12376540}.
Q86SQ4	ADGRG6	S1160	ochoa	Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: Adhesion G-protein coupled receptor G6, N-terminal fragment (ADGRG6 N-terminal fragment) (ADGRG6-NTF); Adhesion G-protein coupled receptor G6, C-terminal fragment (ADGRG6 C-terminal fragment) (ADGRG6-CTF)]	Adhesion G-protein coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (PubMed:35394864, PubMed:39884271). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:24227709, PubMed:35394864). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:24227709, PubMed:35394864). Also able to couple to G(q) G proteins (PubMed:24227709). Involved in myelination of the peripheral nervous system: required for differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Also acts as a regulator of body length and bone mass (PubMed:18391950). Acts as a regulator of blood-brain barrier formation in the central nervous system vie its association with LRP1 and ITGB1 (By similarity). {ECO:0000250\|UniProtKB:Q6F3F9, ECO:0000269\|PubMed:18391950, ECO:0000269\|PubMed:24227709, ECO:0000269\|PubMed:35394864, ECO:0000269\|PubMed:39884271}.
Q86UE4	MTDH	S298	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q86UE4	MTDH	S341	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q86UE4	MTDH	S347	ochoa	Protein LYRIC (3D3/LYRIC) (Astrocyte elevated gene-1 protein) (AEG-1) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein)	Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269\|PubMed:15927426, ECO:0000269\|PubMed:16452207, ECO:0000269\|PubMed:18316612, ECO:0000269\|PubMed:19111877}.
Q86UE8	TLK2	S34	ochoa	Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)	Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:20016786, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:29955062, ECO:0000269\|PubMed:33323470, ECO:0000269\|PubMed:35136069, ECO:0000269\|PubMed:9427565}.
Q86UK7	ZNF598	S502	ochoa	E3 ubiquitin-protein ligase ZNF598 (EC 2.3.2.27) (Zinc finger protein 598)	E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, leading to degradation of nascent peptide chains (PubMed:28065601, PubMed:28132843, PubMed:28685749, PubMed:32099016, PubMed:32579943, PubMed:33581075). ZNF598 is activated when ribosomes are stalled within an mRNA following translation of prematurely polyadenylated mRNAs (PubMed:28065601, PubMed:28132843, PubMed:28685749). Acts as a ribosome collision sensor: specifically recognizes and binds collided di-ribosome, which arises when a trailing ribosome encounters a slower leading ribosome, leading to terminally arrest translation (PubMed:28065601, PubMed:28132843, PubMed:28685749, PubMed:30293783). Following binding to colliding ribosomes, mediates monoubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS3/uS3, and 'Lys-63'-linked polyubiquitination of RPS20/uS10 (PubMed:28065601, PubMed:28132843, PubMed:28685749). Polyubiquitination of RPS20/uS10 promotes recruitment of the RQT (ribosome quality control trigger) complex, which drives the disassembly of stalled ribosomes, followed by degradation of nascent peptides (PubMed:32099016, PubMed:32579943, PubMed:36302773). E3 ubiquitin-protein ligase activity is dependent on the E2 ubiquitin-conjugating enzyme UBE2D3 (PubMed:28685749). Also acts as an adapter that recruits the 4EHP-GYF2 complex to mRNAs (PubMed:22751931, PubMed:32726578). Independently of its role in RQC, may also act as a negative regulator of interferon-stimulated gene (ISG) expression (PubMed:29719242). {ECO:0000269\|PubMed:22751931, ECO:0000269\|PubMed:28065601, ECO:0000269\|PubMed:28132843, ECO:0000269\|PubMed:28685749, ECO:0000269\|PubMed:29719242, ECO:0000269\|PubMed:30293783, ECO:0000269\|PubMed:32099016, ECO:0000269\|PubMed:32579943, ECO:0000269\|PubMed:32726578, ECO:0000269\|PubMed:33581075, ECO:0000269\|PubMed:36302773}.; FUNCTION: (Microbial infection) Required for poxvirus protein synthesis by mediating ubiquitination of RPS10/eS10 and RPS20/uS10 (PubMed:29719242). Poxvirus encoding mRNAs contain unusual 5' poly(A) leaders and ZNF598 is required for their translational efficiency, possibly via its ability to suppress readthrough or sliding on shorter poly(A) tracts (PubMed:29719242). {ECO:0000269\|PubMed:29719242}.
Q86UU1	PHLDB1	S978	ochoa	Pleckstrin homology-like domain family B member 1 (Protein LL5-alpha)	None
Q86V48	LUZP1	S569	ochoa	Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin)	F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250\|UniProtKB:Q8R4U7, ECO:0000269\|PubMed:30990684, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:38009294, ECO:0000269\|PubMed:38832964}.
Q86WB0	ZC3HC1	S344	ochoa\|psp	Zinc finger C3HC-type protein 1 (Nuclear-interacting partner of ALK) (hNIPA) (Nuclear-interacting partner of anaplastic lymphoma kinase)	Required for proper positioning of a substantial amount of TPR at the nuclear basket (NB) through interaction with TPR. {ECO:0000269\|PubMed:34440706}.
Q86X10	RALGAPB	S716	ochoa	Ral GTPase-activating protein subunit beta (p170)	Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.
Q86XZ4	SPATS2	S114	ochoa	Spermatogenesis-associated serine-rich protein 2 (Serine-rich spermatocytes and round spermatid 59 kDa protein) (p59scr)	None
Q86YD5	LDLRAD3	S299	ochoa	Low-density lipoprotein receptor class A domain-containing protein 3 (LDLR class A domain-containing protein 3)	May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (PubMed:26854353). {ECO:0000250, ECO:0000269\|PubMed:26854353}.; FUNCTION: (Microbial infection) Acts as a receptor for Venezuelan equine encephalitis virus. {ECO:0000269\|PubMed:33208938, ECO:0000269\|PubMed:34646020, ECO:0000269\|PubMed:34646021}.
Q86YS7	C2CD5	S295	ochoa	C2 domain-containing protein 5 (C2 domain-containing phosphoprotein of 138 kDa)	Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. {ECO:0000269\|PubMed:21907143}.
Q86YV5	PRAG1	S737	ochoa	Inactive tyrosine-protein kinase PRAG1 (PEAK1-related kinase-activating pseudokinase 1) (Pragmin) (Sugen kinase 223) (SgK223)	Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (By similarity). {ECO:0000250\|UniProtKB:D3ZMK9, ECO:0000250\|UniProtKB:Q571I4}.
Q86YW5	TREML1	S201	ochoa	Trem-like transcript 1 protein (TLT-1) (Triggering receptor expressed on myeloid cells-like protein 1)	Cell surface receptor that may play a role in the innate and adaptive immune response. {ECO:0000269\|PubMed:15128762}.
Q8IV50	LYSMD2	S21	ochoa	LysM and putative peptidoglycan-binding domain-containing protein 2	None
Q8IVL1	NAV2	S2462	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}.
Q8IWB9	TEX2	S738	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}.
Q8IWS0	PHF6	S183	ochoa	PHD finger protein 6 (PHD-like zinc finger protein)	Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269\|PubMed:23229552}.
Q8IWS0	PHF6	S184	ochoa	PHD finger protein 6 (PHD-like zinc finger protein)	Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269\|PubMed:23229552}.
Q8IWZ3	ANKHD1	S2287	ochoa	Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK)	May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269\|PubMed:16098192}.
Q8IX03	WWC1	S141	ochoa	Protein KIBRA (HBeAg-binding protein 3) (Kidney and brain protein) (KIBRA) (WW domain-containing protein 1)	Regulator of the Hippo signaling pathway, also known as the Salvador-Warts-Hippo (SWH) pathway (PubMed:24682284). Enhances phosphorylation of LATS1 and YAP1 and negatively regulates cell proliferation and organ growth due to a suppression of the transcriptional activity of YAP1, the major effector of the Hippo pathway (PubMed:24682284). Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and function in the regulation of Hippo signaling pathway (PubMed:20159598). Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation (PubMed:16684779). Regulates collagen-stimulated activation of the ERK/MAPK cascade (PubMed:18190796). Modulates directional migration of podocytes (PubMed:18596123). Plays a role in cognition and memory performance (PubMed:18672031). Plays an important role in regulating AMPA-selective glutamate receptors (AMPARs) trafficking underlying synaptic plasticity and learning (By similarity). {ECO:0000250\|UniProtKB:Q5SXA9, ECO:0000269\|PubMed:16684779, ECO:0000269\|PubMed:18190796, ECO:0000269\|PubMed:18596123, ECO:0000269\|PubMed:18672031, ECO:0000269\|PubMed:20159598, ECO:0000269\|PubMed:24682284}.
Q8IY57	YAF2	S141	ochoa	YY1-associated factor 2	Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. {ECO:0000269\|PubMed:11593398, ECO:0000269\|PubMed:12706874, ECO:0000269\|PubMed:9016636}.
Q8IY57	YAF2	S144	ochoa	YY1-associated factor 2	Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. {ECO:0000269\|PubMed:11593398, ECO:0000269\|PubMed:12706874, ECO:0000269\|PubMed:9016636}.
Q8IY57	YAF2	S153	ochoa	YY1-associated factor 2	Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling. {ECO:0000269\|PubMed:11593398, ECO:0000269\|PubMed:12706874, ECO:0000269\|PubMed:9016636}.
Q8IYB3	SRRM1	S738	ochoa	Serine/arginine repetitive matrix protein 1 (SR-related nuclear matrix protein of 160 kDa) (SRm160) (Ser/Arg-related nuclear matrix protein)	Part of pre- and post-splicing multiprotein mRNP complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates. {ECO:0000269\|PubMed:10339552, ECO:0000269\|PubMed:10668804, ECO:0000269\|PubMed:11739730, ECO:0000269\|PubMed:12600940, ECO:0000269\|PubMed:12944400, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q8IYB3	SRRM1	S740	ochoa	Serine/arginine repetitive matrix protein 1 (SR-related nuclear matrix protein of 160 kDa) (SRm160) (Ser/Arg-related nuclear matrix protein)	Part of pre- and post-splicing multiprotein mRNP complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates. {ECO:0000269\|PubMed:10339552, ECO:0000269\|PubMed:10668804, ECO:0000269\|PubMed:11739730, ECO:0000269\|PubMed:12600940, ECO:0000269\|PubMed:12944400, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q8IZD0	SAMD14	S130	ochoa	Sterile alpha motif domain-containing protein 14 (SAM domain-containing protein 14)	None
Q8IZH2	XRN1	S1639	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8IZP0	ABI1	S319	ochoa	Abl interactor 1 (Abelson interactor 1) (Abi-1) (Abl-binding protein 4) (AblBP4) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (Nap1-binding protein) (Nap1BP) (Spectrin SH3 domain-binding protein 1) (e3B1)	May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. {ECO:0000269\|PubMed:11003655, ECO:0000269\|PubMed:18328268}.
Q8IZT6	ASPM	S253	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}.
Q8N108	MIER1	S367	ochoa	Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) (hMi-er1)	Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269\|PubMed:12482978}.
Q8N122	RPTOR	S877	ochoa\|psp	Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein)	Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity). {ECO:0000250\|UniProtKB:Q8K4Q0, ECO:0000269\|PubMed:12150925, ECO:0000269\|PubMed:12150926, ECO:0000269\|PubMed:12747827, ECO:0000269\|PubMed:24403073, ECO:0000269\|PubMed:26588989, ECO:0000269\|PubMed:32561715, ECO:0000269\|PubMed:37541260}.
Q8N1F7	NUP93	S72	ochoa	Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93)	Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725). {ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:15703211, ECO:0000269\|PubMed:26878725, ECO:0000269\|PubMed:9348540}.
Q8N1G0	ZNF687	S1106	ochoa	Zinc finger protein 687	May be involved in transcriptional regulation.
Q8N1G2	CMTR1	S37	ochoa	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (hMTr1) (FtsJ methyltransferase domain-containing protein 2) (Interferon-stimulated gene 95 kDa protein) (ISG95)	S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269\|PubMed:18533109, ECO:0000269\|PubMed:20713356, ECO:0000269\|PubMed:21310715}.
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}.
Q8N3F8	MICALL1	S553	ochoa	MICAL-like protein 1 (Molecule interacting with Rab13) (MIRab13)	Lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, acts as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation (PubMed:19864458, PubMed:20801876, PubMed:23596323, PubMed:34100897). Involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking (PubMed:21795389). Alternatively, regulates slow endocytic recycling of endocytosed proteins back to the plasma membrane (PubMed:19864458). Also involved in cargo protein delivery to the plasma membrane (PubMed:34100897). Plays a role in ciliogenesis coordination, recruits EHD1 to primary cilium where it is anchored to the centriole through interaction with tubulins (PubMed:31615969). May indirectly play a role in neurite outgrowth (By similarity). {ECO:0000250\|UniProtKB:Q8BGT6, ECO:0000269\|PubMed:19864458, ECO:0000269\|PubMed:20801876, ECO:0000269\|PubMed:21795389, ECO:0000269\|PubMed:23596323, ECO:0000269\|PubMed:31615969, ECO:0000269\|PubMed:34100897}.
Q8N3U4	STAG2	S1058	ochoa	Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2)	Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269\|PubMed:12034751}.
Q8N3V7	SYNPO	S580	ochoa	Synaptopodin	Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.
Q8N3V7	SYNPO	S744	ochoa	Synaptopodin	Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.
Q8N4V1	MMGT1	S110	ochoa	ER membrane protein complex subunit 5 (Membrane magnesium transporter 1) (Transmembrane protein 32)	Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151, PubMed:30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (By similarity). May be involved in Mg(2+) transport (By similarity). {ECO:0000250\|UniProtKB:Q8K273, ECO:0000269\|PubMed:29242231, ECO:0000269\|PubMed:29809151, ECO:0000269\|PubMed:30415835, ECO:0000269\|PubMed:32439656, ECO:0000269\|PubMed:32459176}.
Q8N612	FHIP1B	S500	ochoa	FHF complex subunit HOOK-interacting protein 1B (FHIP1B) (FTS- and Hook-interacting protein) (FHIP)	Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). {ECO:0000269\|PubMed:18799622, ECO:0000269\|PubMed:32073997}.
Q8N699	MYCT1	S104	ochoa	Myc target protein 1 (Myc target in myeloid cells protein 1)	May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability, and inhibition of hematopoietic differentiation (By similarity). {ECO:0000250}.
Q8N806	UBR7	S257	ochoa	Putative E3 ubiquitin-protein ligase UBR7 (EC 2.3.2.27) (N-recognin-7) (RING-type E3 ubiquitin transferase UBR7)	E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. {ECO:0000250}.
Q8N8S7	ENAH	S531	ochoa	Protein enabled homolog	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11696321, ECO:0000269\|PubMed:18158903}.
Q8N8Z6	DCBLD1	S683	psp	Discoidin, CUB and LCCL domain-containing protein 1	None
Q8ND83	SLAIN1	S240	ochoa	SLAIN motif-containing protein 1	Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269\|PubMed:21646404}.
Q8ND83	SLAIN1	S243	ochoa	SLAIN motif-containing protein 1	Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation. {ECO:0000269\|PubMed:21646404}.
Q8NDF8	TENT4B	S46	ochoa	Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)	Terminal nucleotidyltransferase that catalyzes preferentially the transfer of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:21788334, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro) (PubMed:21788334, PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation (PubMed:22442037). {ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:21788334, ECO:0000269\|PubMed:21855801, ECO:0000269\|PubMed:22442037, ECO:0000269\|PubMed:25049417, ECO:0000269\|PubMed:28383716, ECO:0000269\|PubMed:30026317}.
Q8NDI1	EHBP1	S656	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}.
Q8NDX5	PHC3	S286	ochoa	Polyhomeotic-like protein 3 (Early development regulatory protein 3) (Homolog of polyhomeotic 3) (hPH3)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269\|PubMed:12167701}.
Q8NEY1	NAV1	S296	ochoa	Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)	May be involved in neuronal migration. {ECO:0000250}.
Q8NEY8	PPHLN1	S153	ochoa	Periphilin-1 (CDC7 expression repressor) (CR) (Gastric cancer antigen Ga50)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269\|PubMed:15474462, ECO:0000269\|PubMed:17963697, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:30487602, ECO:0000305\|PubMed:12853457}.
Q8NF50	DOCK8	S2077	ochoa\|psp	Dedicator of cytokinesis protein 8	Guanine nucleotide exchange factor (GEF) which specifically activates small GTPase CDC42 by exchanging bound GDP for free GTP (PubMed:22461490, PubMed:28028151). During immune responses, required for interstitial dendritic cell (DC) migration by locally activating CDC42 at the leading edge membrane of DC (By similarity). Required for CD4(+) T-cell migration in response to chemokine stimulation by promoting CDC42 activation at T cell leading edge membrane (PubMed:28028151). Is involved in NK cell cytotoxicity by controlling polarization of microtubule-organizing center (MTOC), and possibly regulating CCDC88B-mediated lytic granule transport to MTOC during cell killing (PubMed:25762780). {ECO:0000250\|UniProtKB:Q8C147, ECO:0000269\|PubMed:22461490, ECO:0000269\|PubMed:25762780, ECO:0000269\|PubMed:28028151}.
Q8NF91	SYNE1	S8663	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	S1366	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}.
Q8NFH3	NUP43	S299	ochoa	Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) (p42)	Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269\|PubMed:17363900}.
Q8NFH5	NUP35	S251	ochoa	Nucleoporin NUP35 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53)	Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC. {ECO:0000269\|PubMed:15703211}.
Q8NHG8	ZNRF2	S106	ochoa	E3 ubiquitin-protein ligase ZNRF2 (EC 2.3.2.27) (Protein Ells2) (RING finger protein 202) (RING-type E3 ubiquitin transferase ZNRF2) (Zinc/RING finger protein 2)	E3 ubiquitin-protein ligase that plays a role in the establishment and maintenance of neuronal transmission and plasticity. Ubiquitinates the Na(+)/K(+) ATPase alpha-1 subunit/ATP1A1 and thereby influences its endocytosis and/or degradation (PubMed:22797923). Acts also as a positive regulator of mTORC1 activation by amino acids, which functions upstream of the V-ATPase and of Rag-GTPases (PubMed:27244671). In turn, phosphorylation by mTOR leads to its inhibition via targeting to the cytosol allowing a self-regulating feedback mechanism (PubMed:27244671). {ECO:0000269\|PubMed:14561866, ECO:0000269\|PubMed:22797923, ECO:0000269\|PubMed:27244671}.
Q8NHV4	NEDD1	S496	psp	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NHV4	NEDD1	S506	ochoa	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NHV4	NEDD1	S548	ochoa	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NI27	THOC2	S1209	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8NI27	THOC2	S1212	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8TB45	DEPTOR	S283	ochoa\|psp	DEP domain-containing mTOR-interacting protein (hDEPTOR) (DEP domain-containing protein 6)	Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519268, PubMed:34519269). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity (PubMed:34519268, PubMed:34519269). {ECO:0000269\|PubMed:19446321, ECO:0000269\|PubMed:22017875, ECO:0000269\|PubMed:22017876, ECO:0000269\|PubMed:22017877, ECO:0000269\|PubMed:25936805, ECO:0000269\|PubMed:29382726, ECO:0000269\|PubMed:34519268, ECO:0000269\|PubMed:34519269}.
Q8WUB8	PHF10	S321	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}.
Q8WUD1	RAB2B	S192	ochoa	Ras-related protein Rab-2B (EC 3.6.5.2)	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Regulates the compacted morphology of the Golgi (Probable). Promotes cytosolic DNA-induced innate immune responses. Regulates IFN responses against DNA viruses by regulating the CGAS-STING signaling axis (By similarity). Together with RAB2A redundantly required for efficient autophagic flux (PubMed:28483915). {ECO:0000250\|UniProtKB:P59279, ECO:0000269\|PubMed:28483915, ECO:0000305\|PubMed:26209634}.
Q8WUM0	NUP133	S50	ochoa\|psp	Nuclear pore complex protein Nup133 (133 kDa nucleoporin) (Nucleoporin Nup133)	Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269\|PubMed:11684705, ECO:0000269\|PubMed:30179222}.
Q8WUM0	NUP133	S489	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}.
Q8WUX9	CHMP7	S431	ochoa	Charged multivesicular body protein 7 (Chromatin-modifying protein 7)	ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (PubMed:26040712). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712, PubMed:28242692). Recruited to the reforming NE during anaphase by LEMD2 (PubMed:28242692). Plays a role in the endosomal sorting pathway (PubMed:16856878). {ECO:0000269\|PubMed:16856878, ECO:0000269\|PubMed:26040712, ECO:0000269\|PubMed:28242692}.
Q8WV41	SNX33	S61	ochoa	Sorting nexin-33 (SH3 and PX domain-containing protein 3)	Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes. {ECO:0000269\|PubMed:18353773, ECO:0000269\|PubMed:18419754, ECO:0000269\|PubMed:19487689, ECO:0000269\|PubMed:20964629, ECO:0000269\|PubMed:21048941, ECO:0000269\|PubMed:22718350}.
Q8WVD3	RNF138	S127	ochoa	E3 ubiquitin-protein ligase RNF138 (EC 2.3.2.27) (Nemo-like kinase-associated RING finger protein) (NLK-associated RING finger protein) (hNARF) (RING finger protein 138) (RING-type E3 ubiquitin transferase RNF138)	E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination (PubMed:26502055, PubMed:26502057). Recruited to sites of double-strand breaks following DNA damage and specifically promotes double-strand break repair via homologous recombination (PubMed:26502055, PubMed:26502057). Two different, non-exclusive, mechanisms have been proposed. According to a report, regulates the choice of double-strand break repair by favoring homologous recombination over non-homologous end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80, leading to remove the Ku complex from DNA breaks, thereby promoting homologous recombination (PubMed:26502055). According to another report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2, UBE2D3 or UBE2D4) to promote homologous recombination by mediating ubiquitination of RBBP8/CtIP (PubMed:26502057). Together with NLK, involved in the ubiquitination and degradation of TCF/LEF (PubMed:16714285). Also exhibits auto-ubiquitination activity in combination with UBE2K (PubMed:16714285). May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway (PubMed:16714285). {ECO:0000269\|PubMed:16714285, ECO:0000269\|PubMed:26502055, ECO:0000269\|PubMed:26502057}.
Q8WWI1	LMO7	S252	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWI1	LMO7	S1197	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WWY3	PRPF31	S439	ochoa	U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (Serologically defined breast cancer antigen NY-BR-99) (U4/U6 snRNP 61 kDa protein) (Protein 61K) (hPrp31)	Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11867543, PubMed:20118938, PubMed:28781166). Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:11867543). {ECO:0000269\|PubMed:11867543, ECO:0000269\|PubMed:20118938, ECO:0000269\|PubMed:28781166}.
Q8WX93	PALLD	S747	ochoa	Palladin (SIH002) (Sarcoma antigen NY-SAR-77)	Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci. {ECO:0000269\|PubMed:11598191, ECO:0000269\|PubMed:15147863, ECO:0000269\|PubMed:17537434}.
Q8WXG6	MADD	S820	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S826	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WYP5	AHCTF1	S1129	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	S1132	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	S1150	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}.
Q8WZ73	RFFL	S232	ochoa	E3 ubiquitin-protein ligase rififylin (EC 2.3.2.27) (Caspase regulator CARP2) (Caspases-8 and -10-associated RING finger protein 2) (CARP-2) (FYVE-RING finger protein Sakura) (Fring) (RING finger and FYVE-like domain-containing protein 1) (RING finger protein 189) (RING finger protein 34-like) (RING-type E3 ubiquitin transferase rififylin)	E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269\|PubMed:15069192, ECO:0000269\|PubMed:17121812, ECO:0000269\|PubMed:18382127, ECO:0000269\|PubMed:18450452, ECO:0000269\|PubMed:22609986}.
Q92536	SLC7A6	S20	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}.
Q92539	LPIN2	S125	ochoa	Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2)	Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the endoplasmic reticulum membrane. Plays important roles in controlling the metabolism of fatty acids at different levels. Also acts as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism. {ECO:0000250\|UniProtKB:Q99PI5}.
Q92545	TMEM131	S1619	ochoa	Transmembrane protein 131 (Protein RW1)	Collagen binding transmembrane protein involved in collagen secretion by recruiting the ER-to-Golgi transport complex TRAPPIII (PubMed:32095531). May play a role in the immune response to viral infection. {ECO:0000250, ECO:0000269\|PubMed:32095531}.
Q92574	TSC1	S505	ochoa	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92574	TSC1	S515	ochoa	Hamartin (Tuberous sclerosis 1 protein)	Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155). {ECO:0000250\|UniProtKB:Q9Z136, ECO:0000269\|PubMed:10585443, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:16464865, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:33215753, ECO:0000269\|PubMed:9242607}.
Q92585	MAML1	S321	ochoa	Mastermind-like protein 1 (Mam-1)	Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions. {ECO:0000269\|PubMed:11101851, ECO:0000269\|PubMed:11390662, ECO:0000269\|PubMed:12050117, ECO:0000269\|PubMed:15546612, ECO:0000269\|PubMed:17317671}.
Q92597	NDRG1	S326	ochoa	Protein NDRG1 (Differentiation-related gene 1 protein) (DRG-1) (N-myc downstream-regulated gene 1 protein) (Nickel-specific induction protein Cap43) (Reducing agents and tunicamycin-responsive protein) (RTP) (Rit42)	Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy. {ECO:0000269\|PubMed:15247272, ECO:0000269\|PubMed:15377670, ECO:0000269\|PubMed:17786215, ECO:0000269\|PubMed:9766676}.
Q92614	MYO18A	S132	ochoa	Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)	May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250\|UniProtKB:Q9JMH9, ECO:0000269\|PubMed:16087679, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:19837035, ECO:0000269\|PubMed:21123169, ECO:0000269\|PubMed:23345592, ECO:0000269\|PubMed:25965346, ECO:0000269\|PubMed:27467939}.
Q92614	MYO18A	S2031	ochoa	Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)	May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592). Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity). Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly enhances natural killer cell cytotoxicity (PubMed:27467939). {ECO:0000250\|UniProtKB:Q9JMH9, ECO:0000269\|PubMed:16087679, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:19837035, ECO:0000269\|PubMed:21123169, ECO:0000269\|PubMed:23345592, ECO:0000269\|PubMed:25965346, ECO:0000269\|PubMed:27467939}.
Q92619	ARHGAP45	S619	ochoa	Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1 (mHag HA-1)]	Contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, also contains N-terminally a BAR-domin which is able to play an autoinhibitory effect on this RhoGAP activity. {ECO:0000269\|PubMed:24086303}.; FUNCTION: Precursor of the histocompatibility antigen HA-1. More generally, minor histocompatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocompatibility antigen in HLA-matched sibling marrow transplants. Specifically, mismatching for mHag HA-1 which is recognized as immunodominant, is shown to be associated with the development of severe GVHD after HLA-identical BMT. HA-1 is presented to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte (CTL) reactivity against hematologic malignancies after treatment by HLA-identical allogenic BMT. It induces cell recognition and lysis by CTL. {ECO:0000269\|PubMed:12601144, ECO:0000269\|PubMed:8260714, ECO:0000269\|PubMed:8532022, ECO:0000269\|PubMed:9798702}.
Q92974	ARHGEF2	S127	ochoa	Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40)	Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250\|UniProtKB:Q60875, ECO:0000250\|UniProtKB:Q865S3, ECO:0000269\|PubMed:19043560, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:28453519, ECO:0000269\|PubMed:9857026}.
Q92974	ARHGEF2	S133	ochoa	Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (Microtubule-regulated Rho-GEF) (Proliferating cell nucleolar antigen p40)	Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250\|UniProtKB:Q60875, ECO:0000250\|UniProtKB:Q865S3, ECO:0000269\|PubMed:19043560, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:28453519, ECO:0000269\|PubMed:9857026}.
Q92994	BRF1	S432	ochoa	Transcription factor IIIB 90 kDa subunit (TFIIIB90) (hTFIIIB90) (B-related factor 1) (BRF-1) (hBRF) (TAF3B2) (TATA box-binding protein-associated factor, RNA polymerase III, subunit 2)	General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.
Q92997	DVL3	S566	psp	Segment polarity protein dishevelled homolog DVL-3 (Dishevelled-3) (DSH homolog 3)	Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000250\|UniProtKB:Q61062}.
Q92997	DVL3	S633	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}.
Q93074	MED12	S552	ochoa	Mediator of RNA polymerase II transcription subunit 12 (Activator-recruited cofactor 240 kDa component) (ARC240) (CAG repeat protein 45) (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway. {ECO:0000269\|PubMed:16565090, ECO:0000269\|PubMed:16595664, ECO:0000269\|PubMed:17000779}.
Q969V6	MRTFA	S146	ochoa	Myocardin-related transcription factor A (MRTF-A) (MKL/myocardin-like protein 1) (Megakaryoblastic leukemia 1 protein) (Megakaryocytic acute leukemia protein)	Transcription coactivator that associates with the serum response factor (SRF) transcription factor to control expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration (PubMed:26224645). The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. MRTFA binds G-actin via its RPEL repeats, regulating activity of the MRTFA-SRF complex. Activity is also regulated by filamentous actin (F-actin) in the nucleus. {ECO:0000250\|UniProtKB:Q8K4J6, ECO:0000269\|PubMed:26224645}.
Q96B97	SH3KBP1	S493	ochoa	SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)	Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may be inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Has an essential role in the stimulation of B cell activation (PubMed:29636373). {ECO:0000250, ECO:0000269\|PubMed:11894095, ECO:0000269\|PubMed:11894096, ECO:0000269\|PubMed:12177062, ECO:0000269\|PubMed:12734385, ECO:0000269\|PubMed:12771190, ECO:0000269\|PubMed:15090612, ECO:0000269\|PubMed:15707590, ECO:0000269\|PubMed:16177060, ECO:0000269\|PubMed:16256071, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:29636373}.
Q96C24	SYTL4	S199	ochoa	Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin)	Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). {ECO:0000250}.
Q96C24	SYTL4	S201	ochoa	Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin)	Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). {ECO:0000250}.
Q96CP6	GRAMD1A	S257	ochoa	Protein Aster-A (GRAM domain-containing protein 1A)	Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity). May play a role in tumor progression (By similarity). Plays a role in autophagy regulation and is required for biogenesis of the autophagosome (PubMed:31222192). This function in autophagy requires its cholesterol-transfer activity (PubMed:31222192). {ECO:0000250\|UniProtKB:Q8VEF1, ECO:0000269\|PubMed:31222192}.
Q96E39	RBMXL1	S277	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96E39	RBMXL1	S316	ochoa	RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)	RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.
Q96EB6	SIRT1	S159	ochoa	NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]	NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17290224, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21947282, PubMed:22274616, PubMed:22918831, PubMed:24415752, PubMed:24824780, PubMed:29681526, PubMed:29765047, PubMed:30409912). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (PubMed:15469825). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (PubMed:14976264, PubMed:14980222, PubMed:15152190). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (PubMed:15205477). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (By similarity). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (PubMed:21504832). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:19188449). Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (PubMed:20375098). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (By similarity). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (PubMed:18004385, PubMed:21504832). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (PubMed:18004385, PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672523, PubMed:12006491, PubMed:22542455). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (By similarity). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (PubMed:19364925, PubMed:21807113). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (PubMed:14976264, PubMed:14980222, PubMed:21841822). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (PubMed:15126506). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (PubMed:15152190). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17283066, PubMed:17620057, PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15692560). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (PubMed:12535671). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (PubMed:17505061). Represses HNF1A-mediated transcription (By similarity). Required for the repression of ESRRG by CREBZF (PubMed:19690166). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (PubMed:20817729, PubMed:29765047). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (By similarity). Deacetylates p300/EP300 and PRMT1 (By similarity). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:21701047). Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (PubMed:17290224, PubMed:20817729). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (PubMed:15205477, PubMed:16998810, PubMed:17334224, PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (PubMed:15205477, PubMed:17334224, PubMed:20097625). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (PubMed:32538779). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (PubMed:19934257). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (PubMed:32034146). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (PubMed:21775285). Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (PubMed:18687677, PubMed:20203304). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (PubMed:21890893). Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (PubMed:22274616). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (By similarity). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (By similarity). Protects cardiomyocytes against palmitate-induced apoptosis (By similarity). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (By similarity). Involved in the regulation of centrosome duplication: deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (PubMed:31722219). Deacetylates NDC80/HEC1 (PubMed:30409912). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein delactylation, depropionylation and decrotonylation (PubMed:28497810, PubMed:38512451). Mediates depropionylation of Osterix (SP7) (By similarity). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (PubMed:28497810). Mediates protein delactylation of TEAD1 and YAP1 (PubMed:38512451). {ECO:0000250\|UniProtKB:Q923E4, ECO:0000269\|PubMed:11672523, ECO:0000269\|PubMed:12006491, ECO:0000269\|PubMed:12535671, ECO:0000269\|PubMed:14976264, ECO:0000269\|PubMed:14980222, ECO:0000269\|PubMed:15126506, ECO:0000269\|PubMed:15152190, ECO:0000269\|PubMed:15205477, ECO:0000269\|PubMed:15469825, ECO:0000269\|PubMed:15692560, ECO:0000269\|PubMed:16079181, ECO:0000269\|PubMed:16166628, ECO:0000269\|PubMed:16892051, ECO:0000269\|PubMed:16998810, ECO:0000269\|PubMed:17283066, ECO:0000269\|PubMed:17290224, ECO:0000269\|PubMed:17334224, ECO:0000269\|PubMed:17505061, ECO:0000269\|PubMed:17612497, ECO:0000269\|PubMed:17620057, ECO:0000269\|PubMed:17936707, ECO:0000269\|PubMed:18203716, ECO:0000269\|PubMed:18296641, ECO:0000269\|PubMed:18485871, ECO:0000269\|PubMed:18662546, ECO:0000269\|PubMed:18687677, ECO:0000269\|PubMed:19188449, ECO:0000269\|PubMed:19220062, ECO:0000269\|PubMed:19364925, ECO:0000269\|PubMed:19690166, ECO:0000269\|PubMed:19934257, ECO:0000269\|PubMed:20097625, ECO:0000269\|PubMed:20100829, ECO:0000269\|PubMed:20203304, ECO:0000269\|PubMed:20375098, ECO:0000269\|PubMed:20620956, ECO:0000269\|PubMed:20670893, ECO:0000269\|PubMed:20817729, ECO:0000269\|PubMed:20955178, ECO:0000269\|PubMed:21149730, ECO:0000269\|PubMed:21245319, ECO:0000269\|PubMed:21471201, ECO:0000269\|PubMed:21504832, ECO:0000269\|PubMed:21555002, ECO:0000269\|PubMed:21698133, ECO:0000269\|PubMed:21701047, ECO:0000269\|PubMed:21775285, ECO:0000269\|PubMed:21807113, ECO:0000269\|PubMed:21841822, ECO:0000269\|PubMed:21890893, ECO:0000269\|PubMed:21947282, ECO:0000269\|PubMed:22274616, ECO:0000269\|PubMed:22542455, ECO:0000269\|PubMed:22918831, ECO:0000269\|PubMed:23142079, ECO:0000269\|PubMed:24415752, ECO:0000269\|PubMed:24824780, ECO:0000269\|PubMed:28497810, ECO:0000269\|PubMed:29681526, ECO:0000269\|PubMed:29765047, ECO:0000269\|PubMed:30193097, ECO:0000269\|PubMed:30409912, ECO:0000269\|PubMed:31722219, ECO:0000269\|PubMed:32034146, ECO:0000269\|PubMed:32538779, ECO:0000269\|PubMed:38512451}.; FUNCTION: [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. {ECO:0000269\|PubMed:20975832}.; FUNCTION: [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000269\|PubMed:21987377}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. {ECO:0000269\|PubMed:18329615}.
Q96EY7	PTCD3	S671	ochoa	Small ribosomal subunit protein mS39 (28S ribosomal protein S39, mitochondrial) (MRP-S39) (Pentatricopeptide repeat domain-containing protein 3, mitochondrial) (Transformation-related gene 15 protein) (TRG-15)	Mitochondrial RNA-binding protein that has a role in mitochondrial translation. {ECO:0000269\|PubMed:19427859}.
Q96F86	EDC3	S138	ochoa	Enhancer of mRNA-decapping protein 3 (LSM16 homolog) (YjeF N-terminal domain-containing protein 2) (YjeF_N2) (hYjeF_N2) (YjeF domain-containing protein 1)	Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis. {ECO:0000269\|PubMed:16364915, ECO:0000269\|PubMed:17533573, ECO:0000269\|PubMed:18678652, ECO:0000269\|PubMed:25701870}.
Q96HP0	DOCK6	S872	ochoa	Dedicator of cytokinesis protein 6	Acts as a guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity). {ECO:0000250, ECO:0000269\|PubMed:17196961}.
Q96JM3	CHAMP1	S366	ochoa	Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)	Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269\|PubMed:21063390}.
Q96JM3	CHAMP1	S372	ochoa	Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)	Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269\|PubMed:21063390}.
Q96JM3	CHAMP1	S462	ochoa	Chromosome alignment-maintaining phosphoprotein 1 (Zinc finger protein 828)	Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269\|PubMed:21063390}.
Q96JY6	PDLIM2	S117	ochoa	PDZ and LIM domain protein 2 (PDZ-LIM protein mystique)	Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269\|PubMed:15659642}.
Q96KP1	EXOC2	S416	ochoa	Exocyst complex component 2 (Exocyst complex component Sec5)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269\|PubMed:12459492, ECO:0000269\|PubMed:32639540}.
Q96KP1	EXOC2	S422	ochoa	Exocyst complex component 2 (Exocyst complex component Sec5)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269\|PubMed:12459492, ECO:0000269\|PubMed:32639540}.
Q96L73	NSD1	S965	ochoa	Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.357) (Androgen receptor coactivator 267 kDa protein) (Androgen receptor-associated protein of 267 kDa) (H3-K36-HMTase) (Lysine N-methyltransferase 3B) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)	Histone methyltransferase that dimethylates Lys-36 of histone H3 (H3K36me2). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context. {ECO:0000269\|PubMed:21196496}.
Q96MU7	YTHDC1	S308	ochoa	YTH domain-containing protein 1 (Splicing factor YT521) (YT521-B)	Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). {ECO:0000250\|UniProtKB:E9Q5K9, ECO:0000269\|PubMed:20167602, ECO:0000269\|PubMed:25242552, ECO:0000269\|PubMed:26318451, ECO:0000269\|PubMed:26876937, ECO:0000269\|PubMed:27602518, ECO:0000269\|PubMed:28984244, ECO:0000269\|PubMed:32663306}.
Q96N67	DOCK7	S888	ochoa	Dedicator of cytokinesis protein 7	Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250\|UniProtKB:Q8R1A4, ECO:0000269\|PubMed:16982419, ECO:0000269\|PubMed:29467281}.
Q96P48	ARAP1	S624	ochoa	Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (Centaurin-delta-2) (Cnt-d2)	Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members (PubMed:11804590, PubMed:19666464). Activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding and, to a lesser extent, by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) binding (PubMed:11804590). Has a preference for ARF1 and ARF5 (PubMed:11804590, PubMed:19666464). Positively regulates the ring size of circular dorsal ruffles and promotes macropinocytosis (PubMed:22573888). Acts as a bridging factor in osteoclasts to control actin and membrane dynamics (By similarity). Regulates the condensing of osteoclast podosomes into sealing zones which segregate the bone-facing membrane from other membrane domains and are required for osteoclast resorption activity (By similarity). Also regulates recruitment of the AP-3 complex to endosomal membranes and trafficking of lysosomal membrane proteins to the ruffled membrane border of osteoclasts to modulate bone resorption (By similarity). Regulates the endocytic trafficking of EGFR (PubMed:18764928, PubMed:18939958, PubMed:21275903). Regulates the incorporation of CD63 and CD9 into multivesicular bodies (PubMed:38682696). Required in the retinal pigment epithelium (RPE) for photoreceptor survival due to its role in promoting RPE phagocytosis (By similarity). {ECO:0000250\|UniProtKB:Q4LDD4, ECO:0000269\|PubMed:11804590, ECO:0000269\|PubMed:18764928, ECO:0000269\|PubMed:18939958, ECO:0000269\|PubMed:19666464, ECO:0000269\|PubMed:21275903, ECO:0000269\|PubMed:22573888, ECO:0000269\|PubMed:38682696}.
Q96PY5	FMNL2	S169	ochoa	Formin-like protein 2 (Formin homology 2 domain-containing protein 2)	Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics. {ECO:0000269\|PubMed:21834987}.
Q96Q45	TMEM237	S96	ochoa	Transmembrane protein 237 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein)	Component of the transition zone in primary cilia. Required for ciliogenesis. {ECO:0000269\|PubMed:22152675}.
Q96QD8	SLC38A2	S19	ochoa	Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Protein 40-9-1) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)	Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10930503, PubMed:15774260, PubMed:15922329, PubMed:16621798). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (PubMed:10930503, PubMed:15774260). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250\|UniProtKB:Q8CFE6, ECO:0000250\|UniProtKB:Q9JHE5, ECO:0000269\|PubMed:10930503, ECO:0000269\|PubMed:15774260, ECO:0000269\|PubMed:15922329, ECO:0000269\|PubMed:16621798}.
Q96QT4	TRPM7	S1386	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}.
Q96RG2	PASK	S106	ochoa	PAS domain-containing serine/threonine-protein kinase (PAS-kinase) (PASKIN) (hPASK) (EC 2.7.11.1)	Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. {ECO:0000269\|PubMed:16275910, ECO:0000269\|PubMed:17052199, ECO:0000269\|PubMed:17595531, ECO:0000269\|PubMed:20943661, ECO:0000269\|PubMed:21181396, ECO:0000269\|PubMed:21418524}.
Q96RG2	PASK	S939	ochoa	PAS domain-containing serine/threonine-protein kinase (PAS-kinase) (PASKIN) (hPASK) (EC 2.7.11.1)	Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. {ECO:0000269\|PubMed:16275910, ECO:0000269\|PubMed:17052199, ECO:0000269\|PubMed:17595531, ECO:0000269\|PubMed:20943661, ECO:0000269\|PubMed:21181396, ECO:0000269\|PubMed:21418524}.
Q96RT1	ERBIN	S1072	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96RT1	ERBIN	S1158	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96S38	RPS6KC1	S640	ochoa	Ribosomal protein S6 kinase delta-1 (S6K-delta-1) (EC 2.7.11.1) (52 kDa ribosomal protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein) (SPHK1-binding protein)	May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role in the recruitment of PRDX3 to early endosomes (PubMed:15750338). {ECO:0000269\|PubMed:12077123, ECO:0000269\|PubMed:15750338}.
Q96SD1	DCLRE1C	S645	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}.
Q96SU4	OSBPL9	S307	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S314	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S315	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S319	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q96SU4	OSBPL9	S338	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q99081	TCF12	S63	ochoa	Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)	Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3') (By similarity). May be involved in the functional network that regulates the development of the GnRH axis (PubMed:32620954). {ECO:0000250\|UniProtKB:Q61286, ECO:0000269\|PubMed:32620954}.
Q99081	TCF12	S69	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}.
Q99501	GAS2L1	S348	ochoa	GAS2-like protein 1 (GAS2-related protein on chromosome 22) (Growth arrest-specific protein 2-like 1)	Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). {ECO:0000269\|PubMed:12584248, ECO:0000269\|PubMed:24706950}.
Q99575	POP1	S65	ochoa	Ribonucleases P/MRP protein subunit POP1 (hPOP1)	Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:8918471). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269\|PubMed:28115465, ECO:0000269\|PubMed:30454648, ECO:0000269\|PubMed:8918471}.
Q99590	SCAF11	S1104	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99614	TTC1	S265	ochoa	Tetratricopeptide repeat protein 1 (TPR repeat protein 1)	None
Q99640	PKMYT1	S469	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}.
Q99666	RGPD5	S1471	ochoa	RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63)	None
Q99666	RGPD5	S1582	ochoa	RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63)	None
Q99683	MAP3K5	S1224	ochoa	Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269\|PubMed:10411906, ECO:0000269\|PubMed:10688666, ECO:0000269\|PubMed:10849426, ECO:0000269\|PubMed:11029458, ECO:0000269\|PubMed:11154276, ECO:0000269\|PubMed:11689443, ECO:0000269\|PubMed:11920685, ECO:0000269\|PubMed:14688258, ECO:0000269\|PubMed:14749717, ECO:0000269\|PubMed:15023544, ECO:0000269\|PubMed:16129676, ECO:0000269\|PubMed:17220297, ECO:0000269\|PubMed:23102700, ECO:0000269\|PubMed:26095851, ECO:0000269\|PubMed:8940179, ECO:0000269\|PubMed:8974401, ECO:0000269\|PubMed:9564042, ECO:0000269\|PubMed:9774977}.
Q9BQ52	ELAC2	S205	ochoa	Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Heredity prostate cancer protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2)	Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (PubMed:21593607). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly (PubMed:24703694). {ECO:0000269\|PubMed:21593607, ECO:0000269\|PubMed:24703694}.
Q9BQ89	FAM110A	S243	ochoa	Protein FAM110A	None
Q9BQA9	CYBC1	S168	ochoa	Cytochrome b-245 chaperone 1 (Essential for reactive oxygen species protein) (Eros)	Functions as a chaperone necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 heterodimer (PubMed:30361506). Controls the phagocyte respiratory burst and is essential for innate immunity (By similarity). {ECO:0000250\|UniProtKB:Q3TYS2, ECO:0000269\|PubMed:30361506}.
Q9BQE9	BCL7B	S108	ochoa	B-cell CLL/lymphoma 7 protein family member B (allergen Hom s 3)	Positive regulator of apoptosis. Plays a role in the Wnt signaling pathway, negatively regulating the expression of Wnt signaling components CTNNB1 and HMGA1 (PubMed:25569233). Involved in cell cycle progression, maintenance of the nuclear structure and stem cell differentiation (PubMed:25569233). May play a role in lung tumor development or progression (By similarity). {ECO:0000250\|UniProtKB:Q921K9, ECO:0000269\|PubMed:25569233}.
Q9BST9	RTKN	S232	ochoa	Rhotekin	Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures. {ECO:0000269\|PubMed:10940294, ECO:0000269\|PubMed:15480428, ECO:0000269\|PubMed:16007136}.
Q9BT25	HAUS8	S129	psp	HAUS augmin-like complex subunit 8 (HEC1/NDC80-interacting centrosome-associated protein 1) (Sarcoma antigen NY-SAR-48)	Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269\|PubMed:18362163, ECO:0000269\|PubMed:19369198, ECO:0000269\|PubMed:19427217}.
Q9BWG6	SCNM1	S173	ochoa	Sodium channel modifier 1	As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:36084634). Plays a role in the regulation of primary cilia length and Hedgehog signaling (PubMed:36084634). {ECO:0000269\|PubMed:36084634}.
Q9BX66	SORBS1	S76	ochoa	Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP)	Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity). {ECO:0000250\|UniProtKB:Q62417}.
Q9BXB4	OSBPL11	S32	ochoa	Oxysterol-binding protein-related protein 11 (ORP-11) (OSBP-related protein 11)	Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:23028956, ECO:0000269\|PubMed:39106189}.
Q9BXF6	RAB11FIP5	S244	ochoa	Rab11 family-interacting protein 5 (Rab11-FIP5) (Gamma-SNAP-associated factor 1) (Gaf-1) (Phosphoprotein pp75) (Rab11-interacting protein Rip11)	Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269\|PubMed:11163216, ECO:0000269\|PubMed:20717956}.
Q9BXF6	RAB11FIP5	S357	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}.
Q9BXK1	KLF16	S99	ochoa	Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Novel Sp1-like zinc finger transcription factor 2) (Transcription factor BTEB4) (Transcription factor NSLP2)	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.
Q9BXK1	KLF16	S224	ochoa	Krueppel-like factor 16 (Basic transcription element-binding protein 4) (BTE-binding protein 4) (Novel Sp1-like zinc finger transcription factor 2) (Transcription factor BTEB4) (Transcription factor NSLP2)	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.
Q9BY11	PACSIN1	S339	ochoa	Protein kinase C and casein kinase substrate in neurons protein 1 (Syndapin-1)	Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Binds to membranes via its F-BAR domain and mediates membrane tubulation. {ECO:0000250, ECO:0000269\|PubMed:19549836, ECO:0000269\|PubMed:22573331, ECO:0000269\|PubMed:23236520}.
Q9BY89	KIAA1671	S1598	ochoa	Uncharacterized protein KIAA1671	None
Q9BZF1	OSBPL8	S89	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}.
Q9C0B5	ZDHHC5	Y352	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S415	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S422	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0B5	ZDHHC5	S448	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9C0C2	TNKS1BP1	S872	ochoa	182 kDa tankyrase-1-binding protein	None
Q9C0D5	TANC1	S1652	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1668	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1671	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D6	FHDC1	S650	ochoa	FH2 domain-containing protein 1 (Inverted formin-1)	Microtubule-associated formin which regulates both actin and microtubule dynamics. Induces microtubule acetylation and stabilization and actin stress fiber formation (PubMed:18815276). Regulates Golgi ribbon formation (PubMed:26564798). Required for normal cilia assembly. Early in cilia assembly, may assist in the maturation and positioning of the centrosome/basal body, and once cilia assembly has initiated, may also promote cilia elongation by inhibiting disassembly (PubMed:29742020). {ECO:0000269\|PubMed:18815276, ECO:0000269\|PubMed:26564798, ECO:0000269\|PubMed:29742020}.
Q9C0K0	BCL11B	S483	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}.
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}.
Q9H089	LSG1	S271	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}.
Q9H0H5	RACGAP1	S154	ochoa	Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269\|PubMed:10979956, ECO:0000269\|PubMed:11085985, ECO:0000269\|PubMed:11278976, ECO:0000269\|PubMed:11782313, ECO:0000269\|PubMed:14729465, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16129829, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:18511905, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19468302, ECO:0000269\|PubMed:23235882, ECO:0000269\|PubMed:9497316}.
Q9H1A4	ANAPC1	S333	ochoa	Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
Q9H1A4	ANAPC1	S362	ochoa	Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
Q9H1K0	RBSN	S222	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H201	EPN3	S179	ochoa	Epsin-3 (EPS-15-interacting protein 3)	None
Q9H201	EPN3	S182	ochoa	Epsin-3 (EPS-15-interacting protein 3)	None
Q9H3Q1	CDC42EP4	S64	ochoa	Cdc42 effector protein 4 (Binder of Rho GTPases 4)	Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Q9H3Q1	CDC42EP4	S70	ochoa	Cdc42 effector protein 4 (Binder of Rho GTPases 4)	Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Q9H4A4	RNPEP	S19	ochoa	Aminopeptidase B (AP-B) (EC 3.4.11.6) (Arginine aminopeptidase) (Arginyl aminopeptidase)	Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}.
Q9H4L5	OSBPL3	S320	ochoa	Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)	Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269\|PubMed:16143324, ECO:0000269\|PubMed:17428193, ECO:0000269\|PubMed:18270267, ECO:0000269\|PubMed:25447204}.
Q9H4X1	RGCC	S65	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H4X1	RGCC	S69	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H6S3	EPS8L2	S449	ochoa	Epidermal growth factor receptor kinase substrate 8-like protein 2 (EPS8-like protein 2) (Epidermal growth factor receptor pathway substrate 8-related protein 2) (EPS8-related protein 2)	Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. In the cochlea, is required for stereocilia maintenance in adult hair cells (By similarity). {ECO:0000250\|UniProtKB:Q99K30, ECO:0000269\|PubMed:14565974}.
Q9H6U6	BCAS3	S480	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6U6	BCAS3	S886	ochoa	BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3) (GAOB1)	Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). {ECO:0000250\|UniProtKB:Q8CCN5, ECO:0000269\|PubMed:17505058, ECO:0000269\|PubMed:33499712}.
Q9H6W3	RIOX1	S60	ochoa	Ribosomal oxygenase 1 (60S ribosomal protein L8 histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Myc-associated protein with JmjC domain) (Nucleolar protein 66) (hsNO66) (Ribosomal oxygenase NO66) (ROX)	Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (PubMed:23103944). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2) (By similarity). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis (PubMed:23103944). Participates in MYC-induced transcriptional activation (PubMed:17308053). {ECO:0000250\|UniProtKB:Q9JJF3, ECO:0000269\|PubMed:17308053, ECO:0000269\|PubMed:23103944}.
Q9H8V3	ECT2	S858	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}.
Q9H992	MARCHF7	S358	ochoa	E3 ubiquitin-protein ligase MARCHF7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING finger protein 177) (RING-type E3 ubiquitin transferase MARCHF7)	E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:16868077). May be involved in T-cell proliferation by regulating LIF secretion (By similarity). May play a role in lysosome homeostasis (PubMed:31270356). Promotes 'Lys-6', 'Lys-11' and 'Lys-63'-linked mixed polyubiquitination on ATG14 leading to the inhibition of autophagy by impairing the interaction between ATG14 and STX7 (PubMed:37632749). Participates in the dopamine-mediated negative regulation of the NLRP3 inflammasome by promoting its uibiquitination and subsequent degradation (PubMed:25594175). {ECO:0000250\|UniProtKB:Q9WV66, ECO:0000269\|PubMed:16868077, ECO:0000269\|PubMed:25594175, ECO:0000269\|PubMed:31270356, ECO:0000269\|PubMed:37632749}.
Q9H9A7	RMI1	S265	ochoa	RecQ-mediated genome instability protein 1 (BLM-associated protein of 75 kDa) (BLAP75) (FAAP75)	Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability. {ECO:0000269\|PubMed:15775963, ECO:0000269\|PubMed:16537486, ECO:0000269\|PubMed:16595695}.
Q9HAW4	CLSPN	S764	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}.
Q9HAW4	CLSPN	S823	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}.
Q9NPI6	DCP1A	S180	ochoa	mRNA-decapping enzyme 1A (EC 3.6.1.62) (Smad4-interacting transcriptional co-activator) (Transcription factor SMIF)	Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:12417715). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12417715). Contributes to the transactivation of target genes after stimulation by TGFB1 (PubMed:11836524). Essential for embryonic development (PubMed:33813271). {ECO:0000269\|PubMed:11836524, ECO:0000269\|PubMed:12417715, ECO:0000269\|PubMed:33813271}.
Q9NR48	ASH1L	S1671	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NRR5	UBQLN4	S308	ochoa	Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75)	Regulator of protein degradation that mediates the proteasomal targeting of misfolded, mislocalized or accumulated proteins (PubMed:15280365, PubMed:27113755, PubMed:29666234, PubMed:30612738). Acts by binding polyubiquitin chains of target proteins via its UBA domain and by interacting with subunits of the proteasome via its ubiquitin-like domain (PubMed:15280365, PubMed:27113755, PubMed:30612738). Key regulator of DNA repair that represses homologous recombination repair: in response to DNA damage, recruited to sites of DNA damage following phosphorylation by ATM and acts by binding and removing ubiquitinated MRE11 from damaged chromatin, leading to MRE11 degradation by the proteasome (PubMed:30612738). MRE11 degradation prevents homologous recombination repair, redirecting double-strand break repair toward non-homologous end joining (NHEJ) (PubMed:30612738). Specifically recognizes and binds mislocalized transmembrane-containing proteins and targets them to proteasomal degradation (PubMed:27113755). Collaborates with DESI1/POST in the export of ubiquitinated proteins from the nucleus to the cytoplasm (PubMed:29666234). Also plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery (PubMed:23459205). Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:23459205). {ECO:0000250\|UniProtKB:Q99NB8, ECO:0000269\|PubMed:15280365, ECO:0000269\|PubMed:23459205, ECO:0000269\|PubMed:27113755, ECO:0000269\|PubMed:29666234, ECO:0000269\|PubMed:30612738}.
Q9NTI5	PDS5B	S1156	ochoa	Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3)	Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269\|PubMed:10963680, ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19696148}.
Q9NV70	EXOC1	S463	ochoa	Exocyst complex component 1 (Exocyst complex component Sec3)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; FUNCTION: (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269\|PubMed:19889084}.
Q9NV70	EXOC1	S481	ochoa	Exocyst complex component 1 (Exocyst complex component Sec3)	Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.; FUNCTION: (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269\|PubMed:19889084}.
Q9NWQ8	PAG1	S333	ochoa	Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 (Csk-binding protein) (Transmembrane adapter protein PAG) (Transmembrane phosphoprotein Cbp)	Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. {ECO:0000269\|PubMed:10790433}.
Q9NY59	SMPD3	S173	ochoa	Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II)	Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). {ECO:0000250\|UniProtKB:O35049, ECO:0000250\|UniProtKB:Q9JJY3, ECO:0000269\|PubMed:10823942, ECO:0000269\|PubMed:14741383, ECO:0000269\|PubMed:15051724}.
Q9NY59	SMPD3	S291	ochoa	Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II)	Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). {ECO:0000250\|UniProtKB:O35049, ECO:0000250\|UniProtKB:Q9JJY3, ECO:0000269\|PubMed:10823942, ECO:0000269\|PubMed:14741383, ECO:0000269\|PubMed:15051724}.
Q9NYF8	BCLAF1	S196	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYF8	BCLAF1	S262	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYP9	MIS18A	S26	ochoa	Protein Mis18-alpha (FAPP1-associated protein 1)	Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269\|PubMed:17199038}.
Q9NYV4	CDK12	S251	ochoa	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q9NYV6	RRN3	S626	ochoa	RNA polymerase I-specific transcription initiation factor RRN3 (Transcription initiation factor IA) (TIF-IA)	Required for efficient transcription initiation by RNA polymerase I (Pol I). Required for the formation of the competent pre-initiation complex (PIC). {ECO:0000250, ECO:0000269\|PubMed:10758157, ECO:0000269\|PubMed:11250903, ECO:0000269\|PubMed:11265758, ECO:0000269\|PubMed:15805466}.
Q9NZB2	FAM120A	S450	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZM3	ITSN2	S216	ochoa	Intersectin-2 (SH3 domain-containing protein 1B) (SH3P18) (SH3P18-like WASP-associated protein)	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:23999003}.
Q9P0K7	RAI14	S286	ochoa	Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14)	Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier. {ECO:0000250\|UniProtKB:Q5U312}.
Q9P0L2	MARK1	S393	ochoa	Serine/threonine-protein kinase MARK1 (EC 2.7.11.1) (EC 2.7.11.26) (MAP/microtubule affinity-regulating kinase 1) (PAR1 homolog c) (Par-1c) (Par1c)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:17573348, ECO:0000269\|PubMed:23666762}.
Q9P0U3	SENP1	S149	ochoa	Sentrin-specific protease 1 (EC 3.4.22.-) (Sentrin/SUMO-specific protease SENP1)	Protease that catalyzes two essential functions in the SUMO pathway (PubMed:10652325, PubMed:15199155, PubMed:15487983, PubMed:16253240, PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed:15487983). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:15199155, PubMed:16253240, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). Deconjugates SUMO1 from HIPK2 (PubMed:16253240). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (PubMed:15199155, PubMed:21829689). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (PubMed:23160374). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Inhibits N(6)-methyladenosine (m6A) RNA methylation by mediating SUMO1 deconjugation from METTL3 and ALKBH5: METTL3 inhibits the m6A RNA methyltransferase activity, while ALKBH5 desumoylation promotes m6A demethylation (PubMed:29506078, PubMed:34048572, PubMed:37257451). Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032). Deconjugates SUMO1 from GPS2 (PubMed:24943844). {ECO:0000269\|PubMed:10652325, ECO:0000269\|PubMed:15199155, ECO:0000269\|PubMed:15487983, ECO:0000269\|PubMed:16253240, ECO:0000269\|PubMed:16553580, ECO:0000269\|PubMed:21829689, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:23160374, ECO:0000269\|PubMed:24943844, ECO:0000269\|PubMed:25406032, ECO:0000269\|PubMed:29506078, ECO:0000269\|PubMed:34048572, ECO:0000269\|PubMed:37257451}.
Q9P0V3	SH3BP4	S241	ochoa	SH3 domain-binding protein 4 (EH-binding protein 10) (Transferrin receptor-trafficking protein)	May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy. {ECO:0000269\|PubMed:16325581, ECO:0000269\|PubMed:22575674}.
Q9P1T7	MDFIC	S128	ochoa	MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (hIC)	Required to control the activity of various transcription factors through their sequestration in the cytoplasm. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm and inhibits their transcriptional activation (By similarity). Modulates the expression from cellular promoters. Binds to the axin complex, resulting in an increase in the level of free beta-catenin (PubMed:12192039). Affects axin regulation of the WNT and JNK signaling pathways (PubMed:12192039). Involved in the development of lymphatic vessel valves (By similarity). Required to promote lymphatic endothelial cell migration, in a process that involves down-regulation of integrin beta 1 activation and control of cell adhesion to the extracellular matrix (PubMed:35235341). Regulates the activity of mechanosensitive Piezo channel (PubMed:37590348). {ECO:0000250\|UniProtKB:Q8BX65, ECO:0000269\|PubMed:12192039, ECO:0000269\|PubMed:35235341, ECO:0000269\|PubMed:37590348}.; FUNCTION: (Microbial infection) Modulates the expression from viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta (PubMed:12944466, PubMed:16260749, Ref.6). Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR (PubMed:10671520). {ECO:0000269\|PubMed:10671520, ECO:0000269\|PubMed:12944466, ECO:0000269\|PubMed:16260749, ECO:0000269\|Ref.6}.
Q9P1Y5	CAMSAP3	S341	ochoa	Calmodulin-regulated spectrin-associated protein 3 (Protein Nezha)	Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19041755, PubMed:23169647). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (PubMed:24486153). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153). In addition, it also reduces the velocity of microtubule polymerization (PubMed:24486153). Required for the biogenesis and the maintenance of zonula adherens by anchoring the minus-end of microtubules to zonula adherens and by recruiting the kinesin KIFC3 to those junctional sites (PubMed:19041755). Required for orienting the apical-to-basal polarity of microtubules in epithelial cells: acts by tethering non-centrosomal microtubules to the apical cortex, leading to their longitudinal orientation (PubMed:26715742, PubMed:27802168). Plays a key role in early embryos, which lack centrosomes: accumulates at the microtubule bridges that connect pairs of cells and enables the formation of a non-centrosomal microtubule-organizing center that directs intracellular transport in the early embryo (By similarity). Couples non-centrosomal microtubules with actin: interaction with MACF1 at the minus ends of non-centrosomal microtubules, tethers the microtubules to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). Plays a key role in the generation of non-centrosomal microtubules by accumulating in the pericentrosomal region and cooperating with KATNA1 to release non-centrosomal microtubules from the centrosome (PubMed:28386021). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (PubMed:28089391). Through interaction with AKAP9, involved in translocation of Golgi vesicles in epithelial cells, where microtubules are mainly non-centrosomal (PubMed:28089391). Plays an important role in motile cilia function by facilitatating proper orientation of basal bodies and formation of central microtubule pairs in motile cilia (By similarity). {ECO:0000250\|UniProtKB:Q80VC9, ECO:0000269\|PubMed:19041755, ECO:0000269\|PubMed:23169647, ECO:0000269\|PubMed:24486153, ECO:0000269\|PubMed:26715742, ECO:0000269\|PubMed:27693509, ECO:0000269\|PubMed:27802168, ECO:0000269\|PubMed:28089391, ECO:0000269\|PubMed:28386021}.
Q9P206	NHSL3	S559	ochoa	NHS-like protein 3	Able to directly activate the TNF-NFkappaB signaling pathway. {ECO:0000269\|PubMed:32854746}.
Q9P219	CCDC88C	S1571	ochoa	Protein Daple (Coiled-coil domain-containing protein 88C) (Dvl-associating protein with a high frequency of leucine residues) (hDaple) (Hook-related protein 2) (HkRP2)	Required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling (PubMed:26126266). Binds to ligand-activated Wnt receptor FZD7, displacing DVL1 from the FZD7 receptor and leading to inhibition of canonical Wnt signaling (PubMed:26126266). Acts as a non-receptor guanine nucleotide exchange factor by also binding to guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits, leading to their activation (PubMed:26126266). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex, triggering non-canonical Wnt responses such as activation of RAC1 and PI3K-AKT signaling (PubMed:26126266). Promotes apical constriction of cells via ARHGEF18 (PubMed:30948426). {ECO:0000269\|PubMed:26126266, ECO:0000269\|PubMed:30948426}.
Q9P246	STIM2	S599	ochoa	Stromal interaction molecule 2	Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx. {ECO:0000269\|PubMed:16005298, ECO:0000269\|PubMed:16860747, ECO:0000269\|PubMed:17905723, ECO:0000269\|PubMed:18160041, ECO:0000269\|PubMed:21217057, ECO:0000269\|PubMed:22464749, ECO:0000269\|PubMed:23359669}.
Q9P270	SLAIN2	S247	ochoa	SLAIN motif-containing protein 2	Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269\|PubMed:21646404}.
Q9P275	USP36	S602	ochoa	Ubiquitin carboxyl-terminal hydrolase 36 (EC 2.3.2.-) (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)	Deubiquitinase essential for the regulation of nucleolar structure and function (PubMed:19208757, PubMed:22902402, PubMed:29273634). Required for cell and organism viability (PubMed:19208757, PubMed:22902402, PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:19208757, PubMed:22902402, PubMed:29273634, PubMed:36912080). Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (PubMed:29274341). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (PubMed:25775507). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (PubMed:25775507). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (PubMed:27445338). Deubiquitinates SOD2, regulates SOD2 protein stability (PubMed:21268071). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (PubMed:22622177). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (PubMed:35989368). Acts as a SUMO ligase to promote EXOSC10 sumoylation critical for the nucleolar RNA exosome function in rRNA processing (PubMed:36912080). Binds to pre-rRNAs (PubMed:36912080). {ECO:0000269\|PubMed:19208757, ECO:0000269\|PubMed:21268071, ECO:0000269\|PubMed:22622177, ECO:0000269\|PubMed:22902402, ECO:0000269\|PubMed:25775507, ECO:0000269\|PubMed:27445338, ECO:0000269\|PubMed:29273634, ECO:0000269\|PubMed:29274341, ECO:0000269\|PubMed:35989368, ECO:0000269\|PubMed:36912080}.
Q9P2N6	KANSL3	S525	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}.
Q9P2Q2	FRMD4A	S946	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9UBC2	EPS15L1	S241	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S707	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBC2	EPS15L1	S708	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBW5	BIN2	S253	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}.
Q9UDT6	CLIP2	S24	ochoa	CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2) (Williams-Beuren syndrome chromosomal region 3 protein) (Williams-Beuren syndrome chromosomal region 4 protein)	Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}.
Q9UDT6	CLIP2	S163	ochoa	CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2) (Williams-Beuren syndrome chromosomal region 3 protein) (Williams-Beuren syndrome chromosomal region 4 protein)	Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}.
Q9UER7	DAXX	S405	ochoa	Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)	Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269\|PubMed:12140263, ECO:0000269\|PubMed:14990586, ECO:0000269\|PubMed:15016915, ECO:0000269\|PubMed:15364927, ECO:0000269\|PubMed:16845383, ECO:0000269\|PubMed:17081986, ECO:0000269\|PubMed:17942542, ECO:0000269\|PubMed:20504901, ECO:0000269\|PubMed:20651253, ECO:0000269\|PubMed:23222847, ECO:0000269\|PubMed:24200965, ECO:0000269\|PubMed:24530302}.
Q9UGP4	LIMD1	S233	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UGP4	LIMD1	S343	ochoa	LIM domain-containing protein 1	Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269\|PubMed:15542589, ECO:0000269\|PubMed:20303269, ECO:0000269\|PubMed:20616046, ECO:0000269\|PubMed:21834987, ECO:0000269\|PubMed:22286099}.
Q9UHB6	LIMA1	S326	ochoa	LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)	Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250\|UniProtKB:Q9ERG0, ECO:0000269\|PubMed:12566430, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:33999101}.
Q9UHC7	MKRN1	S126	ochoa	E3 ubiquitin-protein ligase makorin-1 (EC 2.3.2.27) (RING finger protein 61) (RING-type E3 ubiquitin transferase makorin-1)	E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II-dependent transcription. {ECO:0000269\|PubMed:16785614, ECO:0000269\|PubMed:19536131}.
Q9UHF7	TRPS1	S1056	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}.
Q9UI08	EVL	S331	ochoa	Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
Q9UID3	VPS51	S643	ochoa	Vacuolar protein sorting-associated protein 51 homolog (Another new gene 2 protein) (Protein fat-free homolog)	Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN (PubMed:20685960). Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269\|PubMed:20685960, ECO:0000269\|PubMed:25799061}.
Q9UID3	VPS51	S653	ochoa	Vacuolar protein sorting-associated protein 51 homolog (Another new gene 2 protein) (Protein fat-free homolog)	Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN (PubMed:20685960). Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269\|PubMed:20685960, ECO:0000269\|PubMed:25799061}.
Q9UJD0	RIMS3	S104	ochoa	Regulating synaptic membrane exocytosis protein 3 (Nim3) (RIM3 gamma) (Rab-3-interacting molecule 3) (RIM 3)	Regulates synaptic membrane exocytosis. {ECO:0000250}.
Q9UJF2	RASAL2	S918	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9UJK0	TSR3	S254	ochoa	18S rRNA aminocarboxypropyltransferase (EC 2.5.1.157) (20S S rRNA accumulation protein 3 homolog) (HsTsr3)	Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) in 18S rRNA (Probable). It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (Probable). {ECO:0000305\|PubMed:27084949}.
Q9UK61	TASOR	S1200	ochoa	Protein TASOR (CTCL tumor antigen se89-1) (Retinoblastoma-associated protein RAP140) (Transgene activation suppressor protein)	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Plays a crucial role in early embryonic development (By similarity). Involved in the organization of spindle poles and spindle apparatus assembly during zygotic division (By similarity). Plays an important role in maintaining epiblast fitness or potency (By similarity). {ECO:0000250\|UniProtKB:Q69ZR9, ECO:0000269\|PubMed:26022416, ECO:0000269\|PubMed:28581500, ECO:0000269\|PubMed:29211708, ECO:0000269\|PubMed:30487602}.
Q9UKE5	TNIK	S720	ochoa	TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)	Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). {ECO:0000269\|PubMed:10521462, ECO:0000269\|PubMed:15342639, ECO:0000269\|PubMed:19061864, ECO:0000269\|PubMed:19816403, ECO:0000269\|PubMed:20159449, ECO:0000269\|PubMed:21690388, ECO:0000269\|PubMed:26437443}.
Q9UKI8	TLK1	S74	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S93	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKI8	TLK1	S176	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9UKK3	PARP4	S1511	ochoa	Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP)	Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. {ECO:0000269\|PubMed:25043379}.
Q9ULH0	KIDINS220	S1349	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}.
Q9ULH0	KIDINS220	S1352	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}.
Q9ULH0	KIDINS220	S1411	ochoa	Kinase D-interacting substrate of 220 kDa (Ankyrin repeat-rich membrane-spanning protein)	Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269\|PubMed:18089783}.
Q9ULH1	ASAP1	S733	ochoa	Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879). {ECO:0000250, ECO:0000269\|PubMed:20393563, ECO:0000269\|PubMed:25673879}.
Q9ULT8	HECTD1	S1380	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	S1509	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	S1519	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	S465	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}.
Q9UMS6	SYNPO2	S767	ochoa	Synaptopodin-2 (Genethonin-2) (Myopodin)	Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks in an isoform-specific manner (PubMed:23225103, PubMed:24005909). At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines. Involved in autophagosome formation. May play a role in chaperone-assisted selective autophagy (CASA) involved in Z lines maintenance in striated muscle under mechanical tension; may link the client-processing CASA chaperone machinery to a membrane-tethering and fusion complex providing autophagosome membranes (By similarity). Involved in regulation of cell migration (PubMed:22915763, PubMed:25883213). May be a tumor suppressor (PubMed:16885336). {ECO:0000250\|UniProtKB:D4A702, ECO:0000250\|UniProtKB:Q91YE8, ECO:0000269\|PubMed:22915763, ECO:0000269\|PubMed:23225103, ECO:0000269\|PubMed:24005909, ECO:0000269\|PubMed:25883213, ECO:0000305\|PubMed:16885336, ECO:0000305\|PubMed:20554076}.; FUNCTION: [Isoform 1]: Involved in regulation of cell migration. Can induce formation of thick, irregular actin bundles in the cell body. {ECO:0000269\|PubMed:22915763, ECO:0000269\|PubMed:24005909}.; FUNCTION: [Isoform 2]: Involved in regulation of cell migration. Can induce long, well-organized actin bundles frequently orientated in parallel along the long axis of the cell showing characteristics of contractile ventral stress fibers. {ECO:0000269\|PubMed:22915763, ECO:0000269\|PubMed:24005909}.; FUNCTION: [Isoform 3]: Involved in regulation of cell migration. Can induce an amorphous actin meshwork throughout the cell body containing a mixture of long and short, randomly organized thick and thin actin bundles. {ECO:0000269\|PubMed:22915763, ECO:0000269\|PubMed:24005909}.; FUNCTION: [Isoform 4]: Can induce long, well-organized actin bundles frequently orientated in parallel along the long axis of the cell showing characteristics of contractile ventral stress fibers. {ECO:0000269\|PubMed:24005909}.; FUNCTION: [Isoform 5]: Involved in regulation of cell migration in part dependent on the Rho-ROCK cascade; can promote formation of nascent focal adhesions, actin bundles at the leading cell edge and lamellipodia (PubMed:22915763, PubMed:25883213). Can induce formation of thick, irregular actin bundles in the cell body; the induced actin network is associated with enhanced cell migration in vitro. {ECO:0000269\|PubMed:22915763, ECO:0000269\|PubMed:24005909, ECO:0000269\|PubMed:25883213}.
Q9UMX1	SUFU	S342	ochoa\|psp	Suppressor of fused homolog (SUFUH)	Negative regulator in the hedgehog/smoothened signaling pathway (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:12068298, PubMed:12975309, PubMed:15367681, PubMed:22365972, PubMed:24217340, PubMed:24311597, PubMed:27234298, PubMed:28965847). Down-regulates GLI1-mediated transactivation of target genes (PubMed:15367681, PubMed:24217340, PubMed:24311597). Down-regulates GLI2-mediated transactivation of target genes (PubMed:24217340, PubMed:24311597). Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:24217340). Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:24217340). Negative regulator of beta-catenin signaling (By similarity). Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full-length form of GLI3 (GLI3FL) (PubMed:24311597, PubMed:28965847). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state (PubMed:24311597, PubMed:28965847). Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R (PubMed:24311597, PubMed:28965847). When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A) (PubMed:24311597, PubMed:28965847). Required for normal embryonic development (By similarity). Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity). {ECO:0000250\|UniProtKB:Q9Z0P7, ECO:0000269\|PubMed:10559945, ECO:0000269\|PubMed:10564661, ECO:0000269\|PubMed:10806483, ECO:0000269\|PubMed:12068298, ECO:0000269\|PubMed:12975309, ECO:0000269\|PubMed:15367681, ECO:0000269\|PubMed:22365972, ECO:0000269\|PubMed:24217340, ECO:0000269\|PubMed:24311597, ECO:0000269\|PubMed:27234298, ECO:0000269\|PubMed:28965847}.
Q9UMZ2	SYNRG	S1075	ochoa	Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin)	Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269\|PubMed:15758025, ECO:0000305\|PubMed:12538641}.
Q9UN36	NDRG2	S328	ochoa	Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Syld709613)	Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. {ECO:0000269\|PubMed:12845671, ECO:0000269\|PubMed:16103061, ECO:0000269\|PubMed:21247902}.
Q9UNZ2	NSFL1C	S262	ochoa	NSFL1 cofactor p47 (UBX domain-containing protein 2C) (p97 cofactor p47)	Reduces the ATPase activity of VCP (By similarity). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro) (PubMed:15498563). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation during mitosis (PubMed:23649807). {ECO:0000250\|UniProtKB:O35987, ECO:0000269\|PubMed:15498563, ECO:0000269\|PubMed:23649807}.
Q9UP95	SLC12A4	S37	ochoa	Solute carrier family 12 member 4 (Electroneutral potassium-chloride cotransporter 1) (Erythroid K-Cl cotransporter 1) (hKCC1)	Mediates electroneutral potassium-chloride cotransport when activated by cell swelling (PubMed:35759661). May contribute to cell volume homeostasis in single cells (PubMed:10913127, PubMed:34031912). May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). {ECO:0000250\|UniProtKB:Q9JIS8, ECO:0000269\|PubMed:10913127, ECO:0000269\|PubMed:34031912, ECO:0000269\|PubMed:35759661}.; FUNCTION: [Isoform 4]: No transporter activity. {ECO:0000269\|PubMed:11551954}.
Q9UPN3	MACF1	S1112	ochoa	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPN3	MACF1	S7278	ochoa	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPN3	MACF1	S7282	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}.
Q9UPZ3	HPS5	S429	ochoa	BLOC-2 complex member HPS5 (Alpha-integrin-binding protein 63) (Hermansky-Pudlak syndrome 5 protein) (Ruby-eye protein 2 homolog) (Ru2)	May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269\|PubMed:15296495, ECO:0000269\|PubMed:17301833}.
Q9UQ35	SRRM2	S892	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1014	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1032	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1069	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1093	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1122	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2111	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2388	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S2684	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ80	PA2G4	S34	psp	Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1)	May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250\|UniProtKB:P50580, ECO:0000250\|UniProtKB:Q6AYD3, ECO:0000269\|PubMed:11268000, ECO:0000269\|PubMed:12682367, ECO:0000269\|PubMed:15064750, ECO:0000269\|PubMed:15583694, ECO:0000269\|PubMed:16832058}.
Q9UQE7	SMC3	S1067	ochoa\|psp	Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP)	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269\|PubMed:11076961, ECO:0000269\|PubMed:19907496}.
Q9Y250	LZTS1	S178	ochoa	Leucine zipper putative tumor suppressor 1 (F37/esophageal cancer-related gene-coding leucine-zipper motif) (Fez1)	Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor. {ECO:0000269\|PubMed:10097140, ECO:0000269\|PubMed:11464283, ECO:0000269\|PubMed:11504921}.
Q9Y294	ASF1A	S165	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}.
Q9Y2H0	DLGAP4	S601	ochoa	Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)	May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Q9Y2H0	DLGAP4	S606	ochoa	Disks large-associated protein 4 (DAP-4) (PSD-95/SAP90-binding protein 4) (SAP90/PSD-95-associated protein 4) (SAPAP-4)	May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Q9Y2K9	STXBP5L	S812	psp	Syntaxin-binding protein 5-like (Lethal(2) giant larvae protein homolog 4) (Tomosyn-2)	Plays a role in vesicle trafficking and exocytosis inhibition. In pancreatic beta-cells, inhibits insulin secretion probably by interacting with and regulating STX1A and STX4, key t-SNARE proteins involved in the fusion of insulin granules to the plasma membrane. Also plays a role in neurotransmitter release by inhibiting basal acetylcholine release from axon terminals and by preventing synaptic fatigue upon repetitive stimulation (By similarity). Promotes as well axonal outgrowth (PubMed:25504045). {ECO:0000250\|UniProtKB:Q5DQR4, ECO:0000269\|PubMed:25504045}.
Q9Y2L5	TRAPPC8	S259	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}.
Q9Y2U5	MAP3K2	S302	ochoa	Mitogen-activated protein kinase kinase kinase 2 (EC 2.7.11.25) (MAPK/ERK kinase kinase 2) (MEK kinase 2) (MEKK 2)	Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. {ECO:0000250, ECO:0000269\|PubMed:10713157, ECO:0000269\|PubMed:16001074}.
Q9Y2W1	THRAP3	S207	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y2X7	GIT1	S561	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y446	PKP3	Y210	ochoa	Plakophilin-3	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:24124604). Required for the localization of DSG2, DSP and PKP2 to mature desmosome junctions (PubMed:20859650). May also play a role in the maintenance of DSG3 protein abundance in keratinocytes (By similarity). Required for the formation of DSP-containing desmosome precursors in the cytoplasm during desmosome assembly (PubMed:25208567). Also regulates the accumulation of CDH1 to mature desmosome junctions, via cAMP-dependent signaling and its interaction with activated RAP1A (PubMed:25208567). Positively regulates the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with FXR1, may also regulate the protein abundance of DSP via the same mechanism (PubMed:25225333). May also regulate the protein abundance of the desmosome component PKP1 (By similarity). Required for the organization of desmosome junctions at intercellular borders between basal keratinocytes of the epidermis, as a result plays a role in maintenance of the dermal barrier and regulation of the dermal inflammatory response (By similarity). Required during epidermal keratinocyte differentiation for cell adherence at tricellular cell-cell contacts, via regulation of the timely formation of adherens junctions and desmosomes in a calcium-dependent manner, and may also play a role in the organization of the intracellular actin fiber belt (By similarity). Acts as a negative regulator of the inflammatory response in hematopoietic cells of the skin and intestine, via modulation of proinflammatory cytokine production (By similarity). Important for epithelial barrier maintenance in the intestine to reduce intestinal permeability, thereby plays a role in protection from intestinal-derived endotoxemia (By similarity). Required for the development of hair follicles, via a role in the regulation of inner root sheaf length, correct alignment and anterior-posterior polarity of hair follicles (By similarity). Promotes proliferation and cell-cycle G1/S phase transition of keratinocytes (By similarity). Promotes E2F1-driven transcription of G1/S phase promoting genes by acting to release E2F1 from its inhibitory interaction with RB1, via sequestering RB1 and CDKN1A to the cytoplasm and thereby increasing CDK4- and CDK6-driven phosphorylation of RB1 (By similarity). May act as a scaffold protein to facilitate MAPK phosphorylation of RPS6KA protein family members and subsequently promote downstream EGFR signaling (By similarity). May play a role in the positive regulation of transcription of Wnt-mediated TCF-responsive target genes (PubMed:34058472). {ECO:0000250\|UniProtKB:Q9QY23, ECO:0000269\|PubMed:20859650, ECO:0000269\|PubMed:24124604, ECO:0000269\|PubMed:25208567, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:34058472}.
Q9Y450	HBS1L	S215	ochoa	HBS1-like protein (EC 3.6.5.-) (ERFS)	GTPase component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:21448132, PubMed:23667253, PubMed:27863242). The Pelota-HBS1L complex recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (PubMed:27863242). Following mRNA extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L complex promotes recruitment of ABCE1, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132, PubMed:32006463). {ECO:0000269\|PubMed:21448132, ECO:0000269\|PubMed:23667253, ECO:0000269\|PubMed:27863242, ECO:0000269\|PubMed:32006463}.
Q9Y4F5	CEP170B	S1356	ochoa	Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B)	Plays a role in microtubule organization. {ECO:0000250\|UniProtKB:Q5SW79}.
Q9Y4G8	RAPGEF2	S1244	psp	Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)	Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Also acts as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10548487, PubMed:10608844, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Also provides inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269\|PubMed:10548487, ECO:0000269\|PubMed:10608844, ECO:0000269\|PubMed:10608883, ECO:0000269\|PubMed:10801446, ECO:0000269\|PubMed:10934204, ECO:0000269\|PubMed:11359771, ECO:0000269\|PubMed:12391161, ECO:0000269\|PubMed:16272156, ECO:0000269\|PubMed:17724123, ECO:0000269\|PubMed:21840392, ECO:0000269\|PubMed:23800469}.
Q9Y4H2	IRS2	S669	psp	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
Q9Y4H2	IRS2	S1154	ochoa	Insulin receptor substrate 2 (IRS-2)	Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239). {ECO:0000250\|UniProtKB:P35570, ECO:0000269\|PubMed:15316008, ECO:0000269\|PubMed:19109239, ECO:0000269\|PubMed:24616100, ECO:0000269\|PubMed:25879670, ECO:0000269\|PubMed:32554797}.
Q9Y5M8	SRPRB	S209	ochoa	Signal recognition particle receptor subunit beta (SR-beta) (Protein APMCF1)	Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity). {ECO:0000250\|UniProtKB:P47758}.
Q9Y5P4	CERT1	S125	ochoa	Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11)	Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269\|PubMed:14685229, ECO:0000269\|PubMed:17591919, ECO:0000269\|PubMed:18184806, ECO:0000269\|PubMed:20036255}.
Q9Y5S2	CDC42BPB	S1673	ochoa	Serine/threonine-protein kinase MRCK beta (EC 2.7.11.1) (CDC42-binding protein kinase beta) (CDC42BP-beta) (DMPK-like beta) (Myotonic dystrophy kinase-related CDC42-binding kinase beta) (MRCK beta) (Myotonic dystrophy protein kinase-like beta)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250\|UniProtKB:Q7TT50, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:21949762}.
Q9Y5S2	CDC42BPB	S1680	ochoa\|psp	Serine/threonine-protein kinase MRCK beta (EC 2.7.11.1) (CDC42-binding protein kinase beta) (CDC42BP-beta) (DMPK-like beta) (Myotonic dystrophy kinase-related CDC42-binding kinase beta) (MRCK beta) (Myotonic dystrophy protein kinase-like beta)	Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250\|UniProtKB:Q7TT50, ECO:0000269\|PubMed:18854160, ECO:0000269\|PubMed:21457715, ECO:0000269\|PubMed:21949762}.
Q9Y608	LRRFIP2	S314	ochoa	Leucine-rich repeat flightless-interacting protein 2 (LRR FLII-interacting protein 2)	May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269\|PubMed:15677333, ECO:0000269\|PubMed:19265123}.
Q9Y6D5	ARFGEF2	S614	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2)	Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269\|PubMed:12051703, ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15385626, ECO:0000269\|PubMed:16477018, ECO:0000269\|PubMed:17276987, ECO:0000269\|PubMed:18625701, ECO:0000269\|PubMed:20360857}.
Q9Y6D6	ARFGEF1	S664	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S670	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6G9	DYNC1LI1	S405	ochoa	Cytoplasmic dynein 1 light intermediate chain 1 (LIC1) (Dynein light chain A) (DLC-A) (Dynein light intermediate chain 1, cytosolic) (DLIC-1)	Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. Forms a functional Rab11/RAB11FIP3/dynein complex onto endosomal membrane that regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endosomal recycling compartment (ERC) (PubMed:20026645). {ECO:0000269\|PubMed:19229290, ECO:0000269\|PubMed:20026645}.
Q9Y6N7	ROBO1	S1602	ochoa	Roundabout homolog 1 (Deleted in U twenty twenty) (H-Robo-1)	Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity). {ECO:0000250\|UniProtKB:O89026, ECO:0000269\|PubMed:10102268, ECO:0000269\|PubMed:24560577, ECO:0000269\|PubMed:26529257, ECO:0000305}.
Q15007	WTAP	S271	Sugiyama	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}.
Q15007	WTAP	S278	Sugiyama	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}.
O14757	CHEK1	S291	EPSD\|PSP\|Sugiyama	Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758). {ECO:0000250\|UniProtKB:O35280, ECO:0000269\|PubMed:10673501, ECO:0000269\|PubMed:11535615, ECO:0000269\|PubMed:12399544, ECO:0000269\|PubMed:12446774, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:12676583, ECO:0000269\|PubMed:12676925, ECO:0000269\|PubMed:12759351, ECO:0000269\|PubMed:12955071, ECO:0000269\|PubMed:14559997, ECO:0000269\|PubMed:14681206, ECO:0000269\|PubMed:14988723, ECO:0000269\|PubMed:15311285, ECO:0000269\|PubMed:15650047, ECO:0000269\|PubMed:15659650, ECO:0000269\|PubMed:15665856, ECO:0000269\|PubMed:16511572, ECO:0000269\|PubMed:17296736, ECO:0000269\|PubMed:17380128, ECO:0000269\|PubMed:18451105, ECO:0000269\|PubMed:18728393, ECO:0000269\|PubMed:19734889, ECO:0000269\|PubMed:20090422, ECO:0000269\|PubMed:31316063, ECO:0000269\|PubMed:32357935, ECO:0000269\|PubMed:33108758, ECO:0000269\|PubMed:9278511}.; FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition. {ECO:0000269\|PubMed:22184239}.
O14920	IKBKB	S682	SIGNOR\|ELM\|EPSD	Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697). {ECO:0000250\|UniProtKB:O88351, ECO:0000269\|PubMed:11297557, ECO:0000269\|PubMed:14673179, ECO:0000269\|PubMed:15084260, ECO:0000269\|PubMed:17213322, ECO:0000269\|PubMed:19716809, ECO:0000269\|PubMed:20410276, ECO:0000269\|PubMed:20434986, ECO:0000269\|PubMed:20797629, ECO:0000269\|PubMed:21138416, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:30337470, ECO:0000269\|PubMed:32209697, ECO:0000269\|PubMed:38621137, ECO:0000269\|PubMed:9346484}.
O15143	ARPC1B	S323	Sugiyama	Actin-related protein 2/3 complex subunit 1B (Arp2/3 complex 41 kDa subunit) (p41-ARC)	Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:11741539, PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269\|PubMed:11741539, ECO:0000269\|PubMed:29925947, ECO:0000269\|PubMed:9230079}.
Q7Z460	CLASP1	S548	Sugiyama	CLIP-associating protein 1 (Cytoplasmic linker-associated protein 1) (Multiple asters homolog 1) (Protein Orbit homolog 1) (hOrbit1)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:12837247, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864}.
Q7Z5J4	RAI1	Y335	Sugiyama	Retinoic acid-induced protein 1	Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation. {ECO:0000269\|PubMed:22578325}.
O94804	STK10	S444	Sugiyama	Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269\|PubMed:11903060, ECO:0000269\|PubMed:12639966, ECO:0000269\|PubMed:19255442}.
Q9UQ35	SRRM2	S172	Sugiyama	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
P35368	ADRA1B	S396	SIGNOR\|iPTMNet\|EPSD	Alpha-1B adrenergic receptor (Alpha-1B adrenoreceptor) (Alpha-1B adrenoceptor)	This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269\|PubMed:18802028, ECO:0000269\|PubMed:22120526}.
Q9H6T3	RPAP3	S503	Sugiyama	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}.
Q9Y478	PRKAB1	S170	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).
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).
Q9NYV4	CDK12	Y246	Sugiyama	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q15642	TRIP10	S288	Sugiyama	Cdc42-interacting protein 4 (Protein Felic) (Salt tolerant protein) (hSTP) (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10)	Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269\|PubMed:11069762, ECO:0000269\|PubMed:16318909, ECO:0000269\|PubMed:16326391}.
Q14671	PUM1	S175	Sugiyama	Pumilio homolog 1 (HsPUM) (Pumilio-1)	Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:18328718, PubMed:21397187, PubMed:21572425, PubMed:21653694). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517, PubMed:29474920). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000250\|UniProtKB:Q80U78, ECO:0000269\|PubMed:18328718, ECO:0000269\|PubMed:18776931, ECO:0000269\|PubMed:20818387, ECO:0000269\|PubMed:20860814, ECO:0000269\|PubMed:21397187, ECO:0000269\|PubMed:21572425, ECO:0000269\|PubMed:21653694, ECO:0000269\|PubMed:22345517, ECO:0000269\|PubMed:22955276, ECO:0000269\|PubMed:25340845, ECO:0000269\|PubMed:25768905, ECO:0000269\|PubMed:26724866, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:29474920}.
O95425	SVIL	S228	Sugiyama	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95817	BAG3	S184	Sugiyama	BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)	Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269\|PubMed:10597216, ECO:0000269\|PubMed:24318877, ECO:0000269\|PubMed:26159920, ECO:0000269\|PubMed:27474739, ECO:0000269\|PubMed:27884606, ECO:0000269\|PubMed:30559338, ECO:0000269\|PubMed:9873016}.
Q9HBH9	MKNK2	S442	Sugiyama	MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2)	Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal. {ECO:0000269\|PubMed:11154262, ECO:0000269\|PubMed:11463832, ECO:0000269\|PubMed:12897141, ECO:0000269\|PubMed:16111636, ECO:0000269\|PubMed:17965020, ECO:0000269\|PubMed:18299328, ECO:0000269\|PubMed:20823271, ECO:0000269\|PubMed:20927323, ECO:0000269\|PubMed:21149447}.
Q9P0L2	MARK1	S383	Sugiyama	Serine/threonine-protein kinase MARK1 (EC 2.7.11.1) (EC 2.7.11.26) (MAP/microtubule affinity-regulating kinase 1) (PAR1 homolog c) (Par-1c) (Par1c)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:17573348, ECO:0000269\|PubMed:23666762}.
A0A0C4DFX4	None	S243	ochoa	Snf2 related CREBBP activator protein	None
O14545	TRAFD1	S479	ochoa	TRAF-type zinc finger domain-containing protein 1 (Protein FLN29)	Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity). {ECO:0000250, ECO:0000269\|PubMed:16221674}.
O14770	MEIS2	S196	ochoa	Homeobox protein Meis2 (Meis1-related protein 1)	Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription. {ECO:0000269\|PubMed:10764806, ECO:0000269\|PubMed:11279116, ECO:0000269\|PubMed:21746878}.
O15068	MCF2L	S965	ochoa	Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein)	Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42 (PubMed:15157669). {ECO:0000250\|UniProtKB:Q63406, ECO:0000269\|PubMed:15157669}.; FUNCTION: [Isoform 3]: Does not catalyze guanine nucleotide exchange on CDC42 (PubMed:15157669). {ECO:0000269\|PubMed:15157669}.
O15439	ABCC4	S657	ochoa	ATP-binding cassette sub-family C member 4 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (MRP/cMOAT-related ABC transporter) (Multi-specific organic anion transporter B) (MOAT-B) (Multidrug resistance-associated protein 4)	ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins (PubMed:11856762, PubMed:12523936, PubMed:12835412, PubMed:12883481, PubMed:15364914, PubMed:15454390, PubMed:16282361, PubMed:17959747, PubMed:18300232, PubMed:26721430). Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4 (PubMed:17959747). Mediates the cotransport of bile acids with reduced glutathione (GSH) (PubMed:12523936, PubMed:12883481, PubMed:16282361). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (PubMed:11856762, PubMed:12105214, PubMed:15454390, PubMed:17344354, PubMed:18300232). Confers resistance to anticancer agents such as methotrexate (PubMed:11106685). {ECO:0000269\|PubMed:11106685, ECO:0000269\|PubMed:11856762, ECO:0000269\|PubMed:12105214, ECO:0000269\|PubMed:12523936, ECO:0000269\|PubMed:12835412, ECO:0000269\|PubMed:12883481, ECO:0000269\|PubMed:15364914, ECO:0000269\|PubMed:15454390, ECO:0000269\|PubMed:16282361, ECO:0000269\|PubMed:17344354, ECO:0000269\|PubMed:17959747, ECO:0000269\|PubMed:18300232, ECO:0000269\|PubMed:26721430}.
O43353	RIPK2	S349	ochoa	Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)	Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269\|PubMed:14638696, ECO:0000269\|PubMed:17054981, ECO:0000269\|PubMed:17562858, ECO:0000269\|PubMed:18079694, ECO:0000269\|PubMed:21123652, ECO:0000269\|PubMed:21887730, ECO:0000269\|PubMed:22607974, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:28545134, ECO:0000269\|PubMed:28656966, ECO:0000269\|PubMed:29452636, ECO:0000269\|PubMed:30026309, ECO:0000269\|PubMed:30279485, ECO:0000269\|PubMed:30478312, ECO:0000269\|PubMed:9575181, ECO:0000269\|PubMed:9642260}.
O43491	EPB41L2	S47	ochoa	Band 4.1-like protein 2 (Erythrocyte membrane protein band 4.1-like 2) (Generally expressed protein 4.1) (4.1G)	Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127). {ECO:0000269\|PubMed:23870127}.
O60307	MAST3	S927	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60315	ZEB2	S352	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}.
O75044	SRGAP2	S852	ochoa	SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)	Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons (PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and inhibitory synapse density through its RAC1-specific GTPase activating activity, while it promotes maturation of both excitatory and inhibitory synapses through its ability to bind to the postsynaptic scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic protein GPHN at inhibitory synapses (By similarity). Mechanistically, acts by binding and deforming membranes, thereby regulating actin dynamics to regulate cell migration and differentiation (PubMed:27373832). Promotes cell repulsion and contact inhibition of locomotion: localizes to protrusions with curved edges and controls the duration of RAC1 activity in contact protrusions (By similarity). In non-neuronal cells, may also play a role in cell migration by regulating the formation of lamellipodia and filopodia (PubMed:20810653, PubMed:21148482). {ECO:0000250\|UniProtKB:Q91Z67, ECO:0000269\|PubMed:20810653, ECO:0000269\|PubMed:21148482, ECO:0000269\|PubMed:22559944, ECO:0000269\|PubMed:27373832, ECO:0000269\|PubMed:28333212}.
O75122	CLASP2	S360	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	S453	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75122	CLASP2	Y1019	ochoa	CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)	Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269\|PubMed:11290329, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16824950, ECO:0000269\|PubMed:16866869, ECO:0000269\|PubMed:16914514, ECO:0000269\|PubMed:17543864, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:26003921}.
O75410	TACC1	S44	ochoa	Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1)	Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways (PubMed:20078863). Might promote the nuclear localization of the receptors (PubMed:20078863). Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. {ECO:0000269\|PubMed:20078863}.
O76080	ZFAND5	S48	ochoa	AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216)	Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Also inhibits tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269\|PubMed:14754897}.
O94880	PHF14	S290	ochoa	PHD finger protein 14	Histone-binding protein (PubMed:23688586). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity). {ECO:0000250\|UniProtKB:A0A286Y9D1, ECO:0000250\|UniProtKB:Q9D4H9, ECO:0000269\|PubMed:23688586}.
O94913	PCF11	S174	ochoa	Pre-mRNA cleavage complex 2 protein Pcf11 (Pre-mRNA cleavage complex II protein Pcf11)	Component of pre-mRNA cleavage complex II, which promotes transcription termination by RNA polymerase II. {ECO:0000269\|PubMed:11060040, ECO:0000269\|PubMed:29196535}.
O95208	EPN2	S172	ochoa	Epsin-2 (EPS-15-interacting protein 2)	Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269\|PubMed:10567358}.
P00519	ABL1	S708	ochoa	Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)	Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 also acts as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250\|UniProtKB:P00520, ECO:0000269\|PubMed:10391250, ECO:0000269\|PubMed:11971963, ECO:0000269\|PubMed:12379650, ECO:0000269\|PubMed:12531427, ECO:0000269\|PubMed:12672821, ECO:0000269\|PubMed:15031292, ECO:0000269\|PubMed:15556646, ECO:0000269\|PubMed:15657060, ECO:0000269\|PubMed:15886098, ECO:0000269\|PubMed:16424036, ECO:0000269\|PubMed:16678104, ECO:0000269\|PubMed:16943190, ECO:0000269\|PubMed:17306540, ECO:0000269\|PubMed:17623672, ECO:0000269\|PubMed:18328268, ECO:0000269\|PubMed:18945674, ECO:0000269\|PubMed:19891780, ECO:0000269\|PubMed:20357770, ECO:0000269\|PubMed:20417104, ECO:0000269\|PubMed:22810897, ECO:0000269\|PubMed:28428613, ECO:0000269\|PubMed:9037071, ECO:0000269\|PubMed:9144171, ECO:0000269\|PubMed:9461559}.
P00519	ABL1	S710	ochoa	Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)	Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 also acts as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250\|UniProtKB:P00520, ECO:0000269\|PubMed:10391250, ECO:0000269\|PubMed:11971963, ECO:0000269\|PubMed:12379650, ECO:0000269\|PubMed:12531427, ECO:0000269\|PubMed:12672821, ECO:0000269\|PubMed:15031292, ECO:0000269\|PubMed:15556646, ECO:0000269\|PubMed:15657060, ECO:0000269\|PubMed:15886098, ECO:0000269\|PubMed:16424036, ECO:0000269\|PubMed:16678104, ECO:0000269\|PubMed:16943190, ECO:0000269\|PubMed:17306540, ECO:0000269\|PubMed:17623672, ECO:0000269\|PubMed:18328268, ECO:0000269\|PubMed:18945674, ECO:0000269\|PubMed:19891780, ECO:0000269\|PubMed:20357770, ECO:0000269\|PubMed:20417104, ECO:0000269\|PubMed:22810897, ECO:0000269\|PubMed:28428613, ECO:0000269\|PubMed:9037071, ECO:0000269\|PubMed:9144171, ECO:0000269\|PubMed:9461559}.
P04792	HSPB1	S74	ochoa	Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Heat shock protein family B member 1) (Stress-responsive protein 27) (SRP27)	Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742). {ECO:0000269\|PubMed:10383393, ECO:0000269\|PubMed:19166925, ECO:0000269\|PubMed:20178975, ECO:0000269\|PubMed:23728742}.
P07814	EPRS1	S990	psp	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P08138	NGFR	S303	ochoa\|psp	Tumor necrosis factor receptor superfamily member 16 (Gp80-LNGFR) (Low affinity neurotrophin receptor p75NTR) (Low-affinity nerve growth factor receptor) (NGF receptor) (Low-affinity nerve growth factor receptor p75NGFR) (Low-affinity nerve growth factor receptor p75NGR) (p75 ICD) (CD antigen CD271)	Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells. Plays a role in the inactivation of RHOA (PubMed:26646181). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCmgetaN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138). Together with BFAR negatively regulates NF-kappa-B and JNK-related signaling pathways (PubMed:22566094). {ECO:0000250, ECO:0000250\|UniProtKB:Q9Z0W1, ECO:0000269\|PubMed:14966521, ECO:0000269\|PubMed:23785138, ECO:0000269\|PubMed:24908487, ECO:0000269\|PubMed:26646181, ECO:0000269\|PubMed:3022937}.
P08172	CHRM2	S282	psp	Muscarinic acetylcholine receptor M2	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269\|PubMed:24256733, ECO:0000269\|PubMed:3443095}.
P11166	SLC2A1	S465	ochoa	Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1) (HepG2 glucose transporter)	Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:10227690, PubMed:10954735, PubMed:18245775, PubMed:19449892, PubMed:25982116, PubMed:27078104, PubMed:32860739). Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (PubMed:18245775, PubMed:19449892). Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain (PubMed:10227690). In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors (By similarity). Required for mesendoderm differentiation (By similarity). {ECO:0000250\|UniProtKB:P17809, ECO:0000250\|UniProtKB:P46896, ECO:0000269\|PubMed:10227690, ECO:0000269\|PubMed:10954735, ECO:0000269\|PubMed:18245775, ECO:0000269\|PubMed:19449892, ECO:0000269\|PubMed:25982116, ECO:0000269\|PubMed:27078104, ECO:0000269\|PubMed:32860739}.
P11277	SPTB	S2117	psp	Spectrin beta chain, erythrocytic (Beta-I spectrin)	Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
P15884	TCF4	Y332	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P15924	DSP	S2598	ochoa	Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)	Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250\|UniProtKB:F1LMV6}.
P17812	CTPS1	Y567	ochoa	CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1)	This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000269\|PubMed:16179339, ECO:0000269\|PubMed:24870241}.
P20700	LMNB1	S396	ochoa	Lamin-B1	Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28716252, PubMed:32910914). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:28716252, PubMed:32910914). {ECO:0000269\|PubMed:28716252, ECO:0000269\|PubMed:32910914}.
P27694	RPA1	S384	ochoa\|psp	Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (Single-stranded DNA-binding protein) [Cleaved into: Replication protein A 70 kDa DNA-binding subunit, N-terminally processed]	As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (PubMed:17596542, PubMed:27723717, PubMed:27723720). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Also plays a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. Plays a role in telomere maintenance (PubMed:17959650, PubMed:34767620). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). RPA stimulates 5'-3' helicase activity of the BRIP1/FANCJ (PubMed:17596542). {ECO:0000269\|PubMed:12791985, ECO:0000269\|PubMed:17596542, ECO:0000269\|PubMed:17765923, ECO:0000269\|PubMed:17959650, ECO:0000269\|PubMed:19116208, ECO:0000269\|PubMed:19996105, ECO:0000269\|PubMed:24332808, ECO:0000269\|PubMed:27723717, ECO:0000269\|PubMed:27723720, ECO:0000269\|PubMed:34767620, ECO:0000269\|PubMed:7697716, ECO:0000269\|PubMed:7700386, ECO:0000269\|PubMed:9430682, ECO:0000269\|PubMed:9765279}.
P29590	PML	S504	ochoa	Protein PML (E3 SUMO-protein ligase PML) (EC 2.3.2.-) (Promyelocytic leukemia protein) (RING finger protein 71) (RING-type E3 SUMO transferase PML) (Tripartite motif-containing protein 19) (TRIM19)	Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Inhibits EIF4E-mediated mRNA nuclear export by reducing EIF4E affinity for the 5' 7-methylguanosine (m7G) cap of target mRNAs (PubMed:11500381, PubMed:11575918, PubMed:18391071). Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration. {ECO:0000269\|PubMed:11500381, ECO:0000269\|PubMed:11575918, ECO:0000269\|PubMed:18391071}.; FUNCTION: Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response (PubMed:20972456, PubMed:28250117). Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity (PubMed:20972456, PubMed:28250117). {ECO:0000269\|PubMed:20972456, ECO:0000269\|PubMed:28250117}.
P30622	CLIP1	S304	ochoa	CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 1) (Cytoplasmic linker protein 170 alpha-2) (CLIP-170) (Reed-Sternberg intermediate filament-associated protein) (Restin)	Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269\|PubMed:12433698, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:17889670}.
P31629	HIVEP2	S809	ochoa	Transcription factor HIVEP2 (Human immunodeficiency virus type I enhancer-binding protein 2) (HIV-EP2) (MHC-binding protein 2) (MBP-2)	This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
P42345	MTOR	S2442	psp	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}.
P42858	HTT	S411	ochoa	Huntingtin (Huntington disease protein) (HD protein) [Cleaved into: Huntingtin, myristoylated N-terminal fragment]	[Huntingtin]: May play a role in microtubule-mediated transport or vesicle function.; FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the formation of autophagic vesicles. {ECO:0000269\|PubMed:24459296}.
P46821	MAP1B	S1248	ochoa	Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1]	Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269\|PubMed:18195017, ECO:0000269\|PubMed:33268592}.
P46821	MAP1B	S1793	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}.
P46937	YAP1	S397	ochoa\|psp	Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)	Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533). {ECO:0000250\|UniProtKB:P46938, ECO:0000269\|PubMed:16772533, ECO:0000269\|PubMed:17974916, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:18280240, ECO:0000269\|PubMed:18579750, ECO:0000269\|PubMed:21364637, ECO:0000269\|PubMed:25778702, ECO:0000269\|PubMed:25849865, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:30447097, ECO:0000269\|PubMed:34404733}.; FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.; FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269\|PubMed:12807903}.
P49023	PXN	S250	ochoa\|psp	Paxillin	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion. {ECO:0000269\|PubMed:25015296}.
P49790	NUP153	S209	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49815	TSC2	S1375	ochoa	Tuberin (Tuberous sclerosis 2 protein)	Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:35772404). Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12820960, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:33436626). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:35772404). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 (By similarity). {ECO:0000250\|UniProtKB:P49816, ECO:0000269\|PubMed:12172553, ECO:0000269\|PubMed:12271141, ECO:0000269\|PubMed:12820960, ECO:0000269\|PubMed:12842888, ECO:0000269\|PubMed:12906785, ECO:0000269\|PubMed:15340059, ECO:0000269\|PubMed:22819219, ECO:0000269\|PubMed:24529379, ECO:0000269\|PubMed:28215400, ECO:0000269\|PubMed:33436626, ECO:0000269\|PubMed:35772404}.
P49916	LIG3	S230	ochoa	DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotide synthase [ATP] 3)	Isoform 3 functions as a heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as a DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269\|PubMed:10207110, ECO:0000269\|PubMed:24674627}.
P50851	LRBA	S1064	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}.
P53396	ACLY	S451	ochoa\|psp	ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (ACL) (Citrate cleavage enzyme)	Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism. {ECO:0000269\|PubMed:10653665, ECO:0000269\|PubMed:1371749, ECO:0000269\|PubMed:19286649, ECO:0000269\|PubMed:23932781, ECO:0000269\|PubMed:39881208, ECO:0000269\|PubMed:9116495}.
P54725	RAD23A	S128	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P54725	RAD23A	S136	ochoa	UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269\|PubMed:20614012}.
P57682	KLF3	S70	ochoa	Krueppel-like factor 3 (Basic krueppel-like factor) (CACCC-box-binding protein BKLF) (TEF-2)	Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis (By similarity). {ECO:0000250}.
P98198	ATP8B2	S1175	ochoa	Phospholipid-transporting ATPase ID (EC 7.6.2.1) (ATPase class I type 8B member 2) (P4-ATPase flippase complex alpha subunit ATP8B2)	Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. May contribute to the maintenance of membrane lipid asymmetry. {ECO:0000269\|PubMed:25315773}.
Q00653	NFKB2	S707	psp	Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. {ECO:0000269\|PubMed:7925301}.
Q01974	ROR2	S860	ochoa	Tyrosine-protein kinase transmembrane receptor ROR2 (EC 2.7.10.1) (Neurotrophic tyrosine kinase, receptor-related 2)	Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation (PubMed:17717073). In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443). {ECO:0000250\|UniProtKB:Q9Z138, ECO:0000269\|PubMed:17717073, ECO:0000269\|PubMed:25029443}.
Q03111	MLLT1	S315	ochoa	Protein ENL (YEATS domain-containing protein 1)	Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948). Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated (PubMed:27105114). Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20) (PubMed:27105114). {ECO:0000269\|PubMed:20159561, ECO:0000269\|PubMed:20471948, ECO:0000269\|PubMed:27105114}.; FUNCTION: Acts as a key chromatin reader in acute myeloid leukemia by recognizing and binding to acetylated histones via its YEATS domain, thereby regulating oncogenic gene transcription. {ECO:0000269\|PubMed:28241139, ECO:0000269\|PubMed:28241141}.
Q03164	KMT2A	S3517	ochoa	Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.364) (ALL-1) (CXXC-type zinc finger protein 7) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]	Histone methyltransferase that plays an essential role in early development and hematopoiesis (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:26886794). Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac) (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:24235145, PubMed:26886794). Catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:12453419, PubMed:15960975, PubMed:19187761, PubMed:19556245, PubMed:20677832, PubMed:21220120, PubMed:25561738, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9' (PubMed:19187761). Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20010842, PubMed:20677832). Promotes PPP1R15A-induced apoptosis (PubMed:10490642). Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-BMAL1 heterodimer (By similarity). Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-BMAL1 to chromatin (By similarity). Also has auto-methylation activity on Cys-3882 in absence of histone H3 substrate (PubMed:24235145). {ECO:0000250\|UniProtKB:P55200, ECO:0000269\|PubMed:10490642, ECO:0000269\|PubMed:12453419, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:19187761, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20010842, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:24235145, ECO:0000269\|PubMed:26886794, ECO:0000305\|PubMed:20677832}.
Q08170	SRSF4	S450	ochoa	Serine/arginine-rich splicing factor 4 (Pre-mRNA-splicing factor SRP75) (SRP001LB) (Splicing factor, arginine/serine-rich 4)	Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269\|PubMed:15009664}.
Q08999	RBL2	S965	ochoa	Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)	Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor.
Q08AD1	CAMSAP2	S1011	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}.
Q12986	NFX1	S142	ochoa	Transcriptional repressor NF-X1 (EC 2.3.2.-) (Nuclear transcription factor, X box-binding protein 1)	Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269\|PubMed:10500182, ECO:0000269\|PubMed:15371341, ECO:0000269\|PubMed:17267499}.
Q13131	PRKAA1	S486	ochoa\|psp	5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)	Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943). {ECO:0000250\|UniProtKB:P54645, ECO:0000250\|UniProtKB:Q5EG47, ECO:0000269\|PubMed:11518699, ECO:0000269\|PubMed:11554766, ECO:0000269\|PubMed:12519745, ECO:0000269\|PubMed:14651849, ECO:0000269\|PubMed:15866171, ECO:0000269\|PubMed:17486097, ECO:0000269\|PubMed:17711846, ECO:0000269\|PubMed:18184930, ECO:0000269\|PubMed:18439900, ECO:0000269\|PubMed:20074060, ECO:0000269\|PubMed:20160076, ECO:0000269\|PubMed:21205641, ECO:0000269\|PubMed:24563466, ECO:0000269\|PubMed:28561066, ECO:0000269\|PubMed:32029622, ECO:0000269\|PubMed:34077757, ECO:0000269\|PubMed:36367943, ECO:0000269\|PubMed:36732624, ECO:0000269\|PubMed:37079666, ECO:0000269\|PubMed:37821951, ECO:0000303\|PubMed:17307971, ECO:0000303\|PubMed:17712357}.
Q13136	PPFIA1	S234	ochoa	Liprin-alpha-1 (LAR-interacting protein 1) (LIP-1) (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1) (PTPRF-interacting protein alpha-1)	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269\|PubMed:7796809}.
Q13247	SRSF6	S291	ochoa	Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6)	Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269\|PubMed:12549914, ECO:0000269\|PubMed:15009664, ECO:0000269\|PubMed:22767602, ECO:0000269\|PubMed:24440982}.
Q13315	ATM	S1883	ochoa	Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated) (A-T mutated)	Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15064416, PubMed:15448695, PubMed:15456891, PubMed:15790808, PubMed:15916964, PubMed:17923702, PubMed:21757780, PubMed:24534091, PubMed:35076389, PubMed:9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15448695, PubMed:15456891, PubMed:15916964, PubMed:17923702, PubMed:24534091, PubMed:9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, FBXO46, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:10550055, PubMed:10766245, PubMed:10802669, PubMed:10839545, PubMed:10910365, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:21757780, PubMed:24534091, PubMed:26240375, PubMed:26774286, PubMed:30171069, PubMed:30612738, PubMed:30886146, PubMed:30952868, PubMed:38128537, PubMed:9733515, PubMed:9843217). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (PubMed:19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed:15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed:15448695). Also involved in pexophagy by mediating phosphorylation of PEX5: translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed:26344566). {ECO:0000250\|UniProtKB:Q62388, ECO:0000269\|PubMed:10550055, ECO:0000269\|PubMed:10766245, ECO:0000269\|PubMed:10802669, ECO:0000269\|PubMed:10839545, ECO:0000269\|PubMed:10910365, ECO:0000269\|PubMed:10973490, ECO:0000269\|PubMed:11375976, ECO:0000269\|PubMed:12086603, ECO:0000269\|PubMed:12556884, ECO:0000269\|PubMed:14871926, ECO:0000269\|PubMed:15448695, ECO:0000269\|PubMed:15456891, ECO:0000269\|PubMed:15916964, ECO:0000269\|PubMed:16086026, ECO:0000269\|PubMed:16858402, ECO:0000269\|PubMed:17923702, ECO:0000269\|PubMed:19431188, ECO:0000269\|PubMed:19965871, ECO:0000269\|PubMed:21757780, ECO:0000269\|PubMed:24534091, ECO:0000269\|PubMed:26240375, ECO:0000269\|PubMed:26344566, ECO:0000269\|PubMed:26774286, ECO:0000269\|PubMed:29203878, ECO:0000269\|PubMed:30171069, ECO:0000269\|PubMed:30612738, ECO:0000269\|PubMed:30886146, ECO:0000269\|PubMed:30952868, ECO:0000269\|PubMed:35076389, ECO:0000269\|PubMed:38128537, ECO:0000269\|PubMed:9733514, ECO:0000269\|PubMed:9733515, ECO:0000269\|PubMed:9843217}.
Q13501	SQSTM1	S276	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}.
Q13620	CUL4B	S70	ochoa	Cullin-4B (CUL-4B)	Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269\|PubMed:14578910, ECO:0000269\|PubMed:16322693, ECO:0000269\|PubMed:16678110, ECO:0000269\|PubMed:18235224, ECO:0000269\|PubMed:18593899, ECO:0000269\|PubMed:19801544, ECO:0000269\|PubMed:22118460, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:29779948, ECO:0000269\|PubMed:30166453, ECO:0000269\|PubMed:33854232, ECO:0000269\|PubMed:33854239}.
Q13796	SHROOM2	S185	ochoa	Protein Shroom2 (Apical-like protein) (Protein APXL)	May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). {ECO:0000250}.
Q13835	PKP1	S225	ochoa	Plakophilin-1 (Band 6 protein) (B6P)	A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:23444369). Plays a role in desmosome protein expression regulation and localization to the desmosomal plaque, thereby maintaining cell sheet integrity and anchorage of desmosomes to intermediate filaments (PubMed:10852826, PubMed:23444369). Required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes in response to mechanical strain, via the formation of an interaction complex composed of DSG3, YAP1, PKP1 and YWHAG (PubMed:31835537). Positively regulates differentiation of keratinocytes, potentially via promoting localization of DSG1 at desmosome cell junctions (By similarity). Required for calcium-independent development and maturation of desmosome plaques specifically at lateral cell-cell contacts in differentiating keratinocytes (By similarity). Plays a role in the maintenance of DSG3 protein abundance, DSG3 clustering and localization of these clusters to the cell membrane in keratinocytes (By similarity). May also promote keratinocyte proliferation and morphogenesis during postnatal development (PubMed:9326952). Required for tight junction inside-out transepidermal barrier function of the skin (By similarity). Promotes Wnt-mediated proliferation and differentiation of ameloblasts, via facilitating TJP1/ZO-1 localization to tight junctions (By similarity). Binds single-stranded DNA (ssDNA), and may thereby play a role in sensing DNA damage and promoting cell survival (PubMed:20613778). Positively regulates cap-dependent translation and as a result cell proliferation, via recruitment of EIF4A1 to the initiation complex and promotion of EIF4A1 ATPase activity (PubMed:20156963, PubMed:23444369). Regulates the mRNA stability and protein abundance of desmosome components PKP2, PKP3, DSC2 and DSP, potentially via its interaction with FXR1 (PubMed:25225333). {ECO:0000250\|UniProtKB:P97350, ECO:0000269\|PubMed:10852826, ECO:0000269\|PubMed:20156963, ECO:0000269\|PubMed:20613778, ECO:0000269\|PubMed:23444369, ECO:0000269\|PubMed:25225333, ECO:0000269\|PubMed:31835537, ECO:0000269\|PubMed:9326952}.
Q14432	PDE3A	S400	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}.
Q14677	CLINT1	S312	ochoa	Clathrin interactor 1 (Clathrin-interacting protein localized in the trans-Golgi region) (Clint) (Enthoprotin) (Epsin-4) (Epsin-related protein) (EpsinR)	Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269\|PubMed:12429846, ECO:0000269\|PubMed:12538641}.
Q14683	SMC1A	S956	ochoa	Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Sb1.8)	Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269\|PubMed:11877377}.
Q15648	MED1	S663	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q15648	MED1	S1439	ochoa	Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269\|PubMed:10406464, ECO:0000269\|PubMed:11867769, ECO:0000269\|PubMed:12037571, ECO:0000269\|PubMed:12218053, ECO:0000269\|PubMed:12556447, ECO:0000269\|PubMed:14636573, ECO:0000269\|PubMed:15340084, ECO:0000269\|PubMed:15471764, ECO:0000269\|PubMed:15989967, ECO:0000269\|PubMed:16574658, ECO:0000269\|PubMed:24245781, ECO:0000269\|PubMed:9653119}.
Q2M1P5	KIF7	S458	ochoa	Kinesin-like protein KIF7	Essential for hedgehog signaling regulation: acts both as a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250\|UniProtKB:B7ZNG0, ECO:0000269\|PubMed:21633164}.
Q3V6T2	CCDC88A	S1417	ochoa\|psp	Girdin (Akt phosphorylation enhancer) (APE) (Coiled-coil domain-containing protein 88A) (G alpha-interacting vesicle-associated protein) (GIV) (Girders of actin filament) (Hook-related protein 1) (HkRP1)	Bifunctional modulator of guanine nucleotide-binding proteins (G proteins) (PubMed:19211784, PubMed:27621449). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits (PubMed:19211784, PubMed:21954290, PubMed:23509302, PubMed:25187647). Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS (PubMed:27621449). Essential for cell migration (PubMed:16139227, PubMed:19211784, PubMed:20462955, PubMed:21954290). Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration (PubMed:20462955). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB (PubMed:19211784). Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed:21954290). Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation (PubMed:27621449). Essential for the integrity of the actin cytoskeleton (PubMed:16139227, PubMed:19211784). Required for formation of actin stress fibers and lamellipodia (PubMed:15882442). May be involved in membrane sorting in the early endosome (PubMed:15882442). Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed:27623382). {ECO:0000250\|UniProtKB:Q5SNZ0, ECO:0000269\|PubMed:15882442, ECO:0000269\|PubMed:16139227, ECO:0000269\|PubMed:19211784, ECO:0000269\|PubMed:20462955, ECO:0000269\|PubMed:21954290, ECO:0000269\|PubMed:23509302, ECO:0000269\|PubMed:25187647, ECO:0000269\|PubMed:27621449, ECO:0000269\|PubMed:27623382}.
Q5JSZ5	PRRC2B	S1679	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5PRF9	SAMD4B	S271	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	S245	ochoa	Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2)	Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269\|PubMed:12786946, ECO:0000269\|PubMed:15047147, ECO:0000269\|PubMed:34516797}.
Q5SW79	CEP170	S871	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5T1M5	FKBP15	S295	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5VT52	RPRD2	S777	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q6P4Q7	CNNM4	S652	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}.
Q6P6C2	ALKBH5	S363	ochoa	RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5)	Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178, PubMed:34048572, PubMed:36944332, PubMed:37257451, PubMed:37369679). Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178). Demethylation of m6A mRNA affects mRNA processing, translation and export (PubMed:23177736, PubMed:34048572, PubMed:36944332, PubMed:37257451). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity). Involved in paraspeckle assembly, a nuclear membraneless organelle, by undergoing liquid-liquid phase separation (PubMed:37369679, PubMed:37474102). Paraspeckle assembly is coupled with m6A demethylation of RNAs, such as NEAT1 non-coding RNA (PubMed:37474102). Also acts as a negative regulator of T-cell development: inhibits gamma-delta T-cell proliferation via demethylation of JAG1 and NOTCH2 transcripts (By similarity). Inhibits regulatory T-cell (Treg) recruitment by mediating demethylation and destabilization of CCL28 mRNAs (By similarity). {ECO:0000250\|UniProtKB:Q3TSG4, ECO:0000269\|PubMed:21264265, ECO:0000269\|PubMed:23177736, ECO:0000269\|PubMed:24489119, ECO:0000269\|PubMed:24616105, ECO:0000269\|PubMed:24778178, ECO:0000269\|PubMed:34048572, ECO:0000269\|PubMed:36944332, ECO:0000269\|PubMed:37257451, ECO:0000269\|PubMed:37369679, ECO:0000269\|PubMed:37474102}.
Q6R327	RICTOR	S1211	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}.
Q6SZW1	SARM1	S703	ochoa	NAD(+) hydrolase SARM1 (NADase SARM1) (hSARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and Armadillo repeat protein) (Sterile alpha and TIR motif-containing protein 1) (Sterile alpha motif domain-containing protein 2) (MyD88-5) (SAM domain-containing protein 2) (Tir-1 homolog) (HsTIR)	NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (PubMed:25908823, PubMed:27671644, PubMed:28334607). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (PubMed:15123841, PubMed:16964262, PubMed:20306472, PubMed:25908823). Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction (PubMed:25908823, PubMed:28334607, PubMed:30333228, PubMed:31128467, PubMed:31439792, PubMed:31439793, PubMed:32049506, PubMed:32828421, PubMed:33053563). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:29395922). Can activate neuronal cell death in response to stress (PubMed:20306472). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (PubMed:16964262). {ECO:0000250\|UniProtKB:Q6PDS3, ECO:0000269\|PubMed:15123841, ECO:0000269\|PubMed:16964262, ECO:0000269\|PubMed:20306472, ECO:0000269\|PubMed:25908823, ECO:0000269\|PubMed:27671644, ECO:0000269\|PubMed:28334607, ECO:0000269\|PubMed:29395922, ECO:0000269\|PubMed:30333228, ECO:0000269\|PubMed:31128467, ECO:0000269\|PubMed:31439792, ECO:0000269\|PubMed:31439793, ECO:0000269\|PubMed:32049506, ECO:0000269\|PubMed:32828421, ECO:0000269\|PubMed:33053563}.
Q6XZF7	DNMBP	S1419	ochoa	Dynamin-binding protein (Scaffold protein Tuba)	Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250\|UniProtKB:E2RP94, ECO:0000250\|UniProtKB:Q6TXD4, ECO:0000269\|PubMed:17015620, ECO:0000269\|PubMed:19767742, ECO:0000269\|PubMed:20479467}.
Q6ZRS2	SRCAP	S262	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q7KZI7	MARK2	S390	ochoa	Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)	Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269\|PubMed:11433294, ECO:0000269\|PubMed:12429843, ECO:0000269\|PubMed:14976552, ECO:0000269\|PubMed:15158914, ECO:0000269\|PubMed:15324659, ECO:0000269\|PubMed:15365179, ECO:0000269\|PubMed:16775013, ECO:0000269\|PubMed:16980613, ECO:0000269\|PubMed:18626018, ECO:0000269\|PubMed:20194617, ECO:0000269\|PubMed:23666762}.
Q7L2J0	MEPCE	S334	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}.
Q7Z6E9	RBBP6	S688	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6E9	RBBP6	S1262	ochoa	E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding Q protein 1) (RBQ-1) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)	E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome (PubMed:18851979). May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth (By similarity). Regulates DNA-replication and the stability of chromosomal common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein stability and abundance via ubiquitination and proteasomal degradation, and ZBTB38 in turn negatively regulates the expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). {ECO:0000250\|UniProtKB:P97868, ECO:0000269\|PubMed:18851979, ECO:0000269\|PubMed:24726359}.; FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus replication probably by impairing the vp30-NP interaction, and thus viral transcription. {ECO:0000269\|PubMed:30550789}.
Q7Z6Z7	HUWE1	S2526	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}.
Q86TI0	TBC1D1	S565	ochoa\|psp	TBC1 domain family member 1	May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity). {ECO:0000250}.
Q86VP3	PACS2	S694	ochoa	Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein)	Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:15692567}.
Q86W92	PPFIBP1	Y353	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}.
Q8IWB9	TEX2	S736	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}.
Q8IZE3	SCYL3	S513	ochoa	Protein-associating with the carboxyl-terminal domain of ezrin (Ezrin-binding protein PACE-1) (SCY1-like protein 3)	May play a role in regulating cell adhesion/migration complexes in migrating cells. {ECO:0000269\|PubMed:12651155}.
Q8IZH2	XRN1	S1645	ochoa	5'-3' exoribonuclease 1 (EC 3.1.13.-) (Strand-exchange protein 1 homolog)	Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250\|UniProtKB:P97789, ECO:0000269\|PubMed:18172165}.
Q8N488	RYBP	S203	ochoa	RING1 and YY1-binding protein (Apoptin-associating protein 1) (APAP-1) (Death effector domain-associated factor) (DED-associated factor) (YY1 and E4TF1-associated factor 1)	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:25519132). Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (By similarity). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (PubMed:19098711). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis (PubMed:14765135, PubMed:27060496). May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (PubMed:11953439). May bind to DNA (By similarity). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3 (PubMed:27748911). {ECO:0000250\|UniProtKB:Q8CCI5, ECO:0000269\|PubMed:11953439, ECO:0000269\|PubMed:14765135, ECO:0000269\|PubMed:19098711, ECO:0000269\|PubMed:27060496, ECO:0000269\|PubMed:27748911}.
Q8N684	CPSF7	S409	ochoa	Cleavage and polyadenylation specificity factor subunit 7 (Cleavage and polyadenylation specificity factor 59 kDa subunit) (CPSF 59 kDa subunit) (Cleavage factor Im complex 59 kDa subunit) (CFIm59) (Pre-mRNA cleavage factor Im 59 kDa subunit)	Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:17024186, PubMed:29276085, PubMed:8626397). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:17024186, PubMed:8626397). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF7 activates directly the mRNA 3'-processing machinery (PubMed:29276085). Binds to pA signals in RNA substrates (PubMed:17024186, PubMed:8626397). {ECO:0000269\|PubMed:17024186, ECO:0000269\|PubMed:20695905, ECO:0000269\|PubMed:23187700, ECO:0000269\|PubMed:29276085, ECO:0000269\|PubMed:8626397}.
Q8NDF8	TENT4B	S48	ochoa	Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)	Terminal nucleotidyltransferase that catalyzes preferentially the transfer of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:21788334, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro) (PubMed:21788334, PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation (PubMed:22442037). {ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:21788334, ECO:0000269\|PubMed:21855801, ECO:0000269\|PubMed:22442037, ECO:0000269\|PubMed:25049417, ECO:0000269\|PubMed:28383716, ECO:0000269\|PubMed:30026317}.
Q8NHH9	ATL2	S27	ochoa	Atlastin-2 (ATL-2) (EC 3.6.5.-) (ADP-ribosylation factor-like protein 6-interacting protein 2)	Atlastin-2 (ATL2) is a membrane-anchored GTPase that mediates the GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the continuous ER network. It facilitates the formation of three-way junctions where ER tubules intersect (PubMed:18270207, PubMed:19665976, PubMed:22065636, PubMed:27619977, PubMed:34817557). Two atlastin-2 on neighboring ER tubules bind GTP and form loose homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon GTP hydrolysis, the 3HB regions tighten, pulling the membranes together to drive their fusion. After fusion, the homodimer disassembles upon release of inorganic phosphate (Pi). Subsequently, GDP dissociates, resetting the monomers to a conformation ready for a new fusion cycle (By similarity). {ECO:0000250\|UniProtKB:Q8WXF7, ECO:0000269\|PubMed:18270207, ECO:0000269\|PubMed:19665976, ECO:0000269\|PubMed:22065636, ECO:0000269\|PubMed:27619977, ECO:0000269\|PubMed:34817557}.
Q8NHV4	NEDD1	S558	psp	Protein NEDD1 (Neural precursor cell expressed developmentally down-regulated protein 1) (NEDD-1)	Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269\|PubMed:19029337, ECO:0000269\|PubMed:19509060}.
Q8NI08	NCOA7	S171	ochoa	Nuclear receptor coactivator 7 (140 kDa estrogen receptor-associated protein) (Estrogen nuclear receptor coactivator 1)	Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269\|PubMed:11971969}.
Q8NI27	THOC2	S1211	ochoa	THO complex subunit 2 (Tho2) (hTREX120)	Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. {ECO:0000269\|PubMed:11979277, ECO:0000269\|PubMed:15833825, ECO:0000269\|PubMed:15998806, ECO:0000269\|PubMed:17190602, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23222130, ECO:0000269\|PubMed:33191911}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269\|PubMed:18974867}.
Q8TED9	AFAP1L1	S143	ochoa	Actin filament-associated protein 1-like 1 (AFAP1-like protein 1)	May be involved in podosome and invadosome formation. {ECO:0000269\|PubMed:21333378}.
Q8TEV9	SMCR8	S394	ochoa	Guanine nucleotide exchange protein SMCR8 (Smith-Magenis syndrome chromosomal region candidate gene 8 protein)	Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:20562859, PubMed:27103069, PubMed:27193190, PubMed:27559131, PubMed:27617292, PubMed:28195531, PubMed:32303654). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation (PubMed:20562859, PubMed:27103069, PubMed:27617292, PubMed:28195531). The C9orf72-SMCR8 complex also acts as a negative regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and inhibiting its protein kinase activity (PubMed:27617292, PubMed:28195531). As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro (PubMed:32303654). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131, PubMed:28195531). In addition to its activity in the cytoplasm within the C9orf72-SMCR8 complex, SMCR8 also localizes in the nucleus, where it associates with chromatin and negatively regulates expression of suppresses ULK1 and WIPI2 genes (PubMed:28195531). {ECO:0000269\|PubMed:20562859, ECO:0000269\|PubMed:27103069, ECO:0000269\|PubMed:27193190, ECO:0000269\|PubMed:27559131, ECO:0000269\|PubMed:27617292, ECO:0000269\|PubMed:28195531, ECO:0000269\|PubMed:32303654}.
Q8WWI1	LMO7	S1591	ochoa	LIM domain only protein 7 (LMO-7) (F-box only protein 20) (LOMP)	None
Q8WXG6	MADD	S692	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q8WXG6	MADD	S701	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q96D71	REPS1	S117	ochoa	RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1)	May coordinate the cellular actions of activated EGF receptors and Ral-GTPases. {ECO:0000250}.
Q96F86	EDC3	S140	ochoa	Enhancer of mRNA-decapping protein 3 (LSM16 homolog) (YjeF N-terminal domain-containing protein 2) (YjeF_N2) (hYjeF_N2) (YjeF domain-containing protein 1)	Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis. {ECO:0000269\|PubMed:16364915, ECO:0000269\|PubMed:17533573, ECO:0000269\|PubMed:18678652, ECO:0000269\|PubMed:25701870}.
Q96FA3	PELI1	S70	psp	E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (Pellino-related intracellular-signaling molecule) (RING-type E3 ubiquitin transferase pellino homolog 1)	E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:12496252, PubMed:17675297, PubMed:29883609, PubMed:30952868). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6 (PubMed:12496252, PubMed:17675297). Acts as a positive regulator of inflammatory response in microglia through activation of NF-kappa-B and MAP kinase (By similarity). Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (PubMed:12496252, PubMed:17675297). Conjugates 'Lys-63'-linked ubiquitin chains to the adapter protein ASC/PYCARD, which in turn is crucial for NLRP3 inflammasome activation (PubMed:34706239). Mediates 'Lys-48'-linked polyubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation; preferentially recognizes and mediates the degradation of the 'Thr-182' phosphorylated form of RIPK3 (PubMed:29883609). Negatively regulates necroptosis by reducing RIPK3 expression (PubMed:29883609). Mediates 'Lys-63'-linked ubiquitination of RIPK1 (PubMed:29883609). Following phosphorylation by ATM, catalyzes 'Lys-63'-linked ubiquitination of NBN, promoting DNA repair via homologous recombination (PubMed:30952868). Negatively regulates activation of the metabolic mTORC1 signaling pathway by mediating 'Lys-63'-linked ubiquitination of mTORC1-inhibitory protein TSC1 and thereby promoting TSC1/TSC2 complex stability (PubMed:33215753). {ECO:0000250\|UniProtKB:Q8C669, ECO:0000269\|PubMed:12496252, ECO:0000269\|PubMed:17675297, ECO:0000269\|PubMed:29883609, ECO:0000269\|PubMed:30952868, ECO:0000269\|PubMed:33215753}.
Q96K76	USP47	S956	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}.
Q96RT1	ERBIN	S659	ochoa	Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)	Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269\|PubMed:10878805, ECO:0000269\|PubMed:16203728}.
Q96S59	RANBP9	S477	ochoa	Ran-binding protein 9 (RanBP9) (BPM-L) (BPM90) (Ran-binding protein M) (RanBPM) (RanBP7)	May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Acts as a mediator of cell spreading and actin cytoskeleton rearrangement (PubMed:18710924). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). May be involved in signaling of ITGB2/LFA-1 and other integrins (PubMed:14722085). Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway (PubMed:12147692). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation (PubMed:12361945, PubMed:18222118). Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity (PubMed:15558019). Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA. {ECO:0000269\|PubMed:12147692, ECO:0000269\|PubMed:12361945, ECO:0000269\|PubMed:14500717, ECO:0000269\|PubMed:14722085, ECO:0000269\|PubMed:15381419, ECO:0000269\|PubMed:15558019, ECO:0000269\|PubMed:18222118, ECO:0000269\|PubMed:18710924, ECO:0000269\|PubMed:29911972, ECO:0000305}.
Q96SU4	OSBPL9	S317	ochoa	Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9)	Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269\|PubMed:39106189}.
Q99504	EYA3	S256	ochoa	Protein phosphatase EYA3 (EC 3.1.3.48) (Eyes absent homolog 3)	Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1 (PubMed:19234442, PubMed:19351884). Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity (By similarity). May be involved in development of the eye. {ECO:0000250\|UniProtKB:P97480, ECO:0000269\|PubMed:19234442, ECO:0000269\|PubMed:19351884}.
Q99569	PKP4	S143	ochoa	Plakophilin-4 (p0071)	Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques. {ECO:0000269\|PubMed:17115030}.
Q99590	SCAF11	S392	ochoa	Protein SCAF11 (CTD-associated SR protein 11) (Renal carcinoma antigen NY-REN-40) (SC35-interacting protein 1) (SR-related and CTD-associated factor 11) (SRSF2-interacting protein) (Serine/arginine-rich splicing factor 2-interacting protein) (Splicing factor, arginine/serine-rich 2-interacting protein) (Splicing regulatory protein 129) (SRrp129)	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269\|PubMed:9447963}.
Q99700	ATXN2	S857	ochoa	Ataxin-2 (Spinocerebellar ataxia type 2 protein) (Trinucleotide repeat-containing gene 13 protein)	Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269\|PubMed:18602463}.
Q99755	PIP5K1A	S467	ochoa	Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha)	Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:21477596, PubMed:22942276, PubMed:8955136). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (PubMed:19158393, PubMed:20660631). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (PubMed:22942276). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup (By similarity). Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (PubMed:19158393). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane (PubMed:20660631). Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (PubMed:18288197). {ECO:0000250\|UniProtKB:P70182, ECO:0000269\|PubMed:18288197, ECO:0000269\|PubMed:19158393, ECO:0000269\|PubMed:20660631, ECO:0000269\|PubMed:21477596, ECO:0000269\|PubMed:22942276, ECO:0000269\|PubMed:8955136}.
Q9BTC0	DIDO1	S1026	ochoa	Death-inducer obliterator 1 (DIO-1) (hDido1) (Death-associated transcription factor 1) (DATF-1)	Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development. {ECO:0000250, ECO:0000269\|PubMed:16127461}.; FUNCTION: [Isoform 2]: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes. {ECO:0000269\|PubMed:16127461}.
Q9BV36	MLPH	S256	ochoa	Melanophilin (Exophilin-3) (Slp homolog lacking C2 domains a) (SlaC2-a) (Synaptotagmin-like protein 2a)	Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. {ECO:0000269\|PubMed:12062444}.
Q9C0A6	SETD5	S1125	ochoa	Histone-lysine N-methyltransferase SETD5 (EC 2.1.1.359) (EC 2.1.1.367) (SET domain-containing protein 5)	Chromatin regulator required for brain development: acts as a regulator of RNA elongation rate, thereby regulating neural stem cell (NSC) proliferation and synaptic transmission. May act by mediating trimethylation of 'Lys-36' of histone H3 (H3K36me3), which is essential to allow on-time RNA elongation dynamics. Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. The relevance of histone methyltransferase activity is however subject to discussion. {ECO:0000250\|UniProtKB:Q5XJV7}.
Q9C0D0	PHACTR1	S177	ochoa	Phosphatase and actin regulator 1	Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity (PubMed:21798305, PubMed:21939755). Involved in the regulation of cortical neuron migration and dendrite arborization (By similarity). {ECO:0000250\|UniProtKB:Q2M3X8, ECO:0000269\|PubMed:21798305, ECO:0000269\|PubMed:21939755}.
Q9H4A3	WNK1	S1289	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4X1	RGCC	S67	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9HB90	RRAGC	S376	ochoa	Ras-related GTP-binding protein C (Rag C) (RagC) (EC 3.6.5.-) (GTPase-interacting protein 2) (TIB929)	Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade (PubMed:20381137, PubMed:24095279, PubMed:27234373, PubMed:31601708, PubMed:31601764, PubMed:32612235, PubMed:34071043, PubMed:36697823, PubMed:37057673). Forms heterodimeric Rag complexes with RagA/RRAGA or RagB/RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form: RagC/RRAGC is in its active form when GDP-bound RagC/RRAGC forms a complex with GTP-bound RagA/RRAGA (or RagB/RRAGB) and in an inactive form when GTP-bound RagC/RRAGC heterodimerizes with GDP-bound RagA/RRAGA (or RagB/RRAGB) (PubMed:24095279, PubMed:31601708, PubMed:31601764, PubMed:32868926). In its GDP-bound active form, promotes the recruitment of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB (PubMed:20381137, PubMed:24095279, PubMed:27234373, PubMed:32612235, PubMed:36697823). This is a crucial step in the activation of the MTOR signaling cascade by amino acids (PubMed:20381137, PubMed:24095279, PubMed:27234373). Also plays a central role in the non-canonical mTORC1 complex, which acts independently of RHEB and specifically mediates phosphorylation of MiT/TFE factors TFEB and TFE3: GDP-bound RagC/RRAGC mediates recruitment of MiT/TFE factors TFEB and TFE3 (PubMed:32612235, PubMed:36697823). {ECO:0000269\|PubMed:20381137, ECO:0000269\|PubMed:24095279, ECO:0000269\|PubMed:27234373, ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:32612235, ECO:0000269\|PubMed:32868926, ECO:0000269\|PubMed:34071043, ECO:0000269\|PubMed:36697823, ECO:0000269\|PubMed:37057673}.
Q9NR48	ASH1L	S1681	ochoa	Histone-lysine N-methyltransferase ASH1L (EC 2.1.1.359) (EC 2.1.1.367) (ASH1-like protein) (huASH1) (Absent small and homeotic disks protein 1 homolog) (Lysine N-methyltransferase 2H)	Histone methyltransferase specifically trimethylating 'Lys-36' of histone H3 forming H3K36me3 (PubMed:21239497). Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). The physiological significance of the H3K9me1 activity is unclear (By similarity). {ECO:0000250\|UniProtKB:Q99MY8, ECO:0000269\|PubMed:21239497}.
Q9NRA8	EIF4ENIF1	S345	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NWH9	SLTM	S543	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}.
Q9NY27	PPP4R2	S216	ochoa	Serine/threonine-protein phosphatase 4 regulatory subunit 2	Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. {ECO:0000269\|PubMed:10769191, ECO:0000269\|PubMed:12668731, ECO:0000269\|PubMed:18614045, ECO:0000269\|PubMed:20154705}.
Q9NYF8	BCLAF1	S264	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYV4	CDK12	S241	ochoa	Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cdc2-related kinase, arginine/serine-rich) (CrkRS) (Cell division cycle 2-related protein kinase 7) (CDC2-related protein kinase 7) (Cell division protein kinase 12) (hCDK12)	Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269\|PubMed:11683387, ECO:0000269\|PubMed:19651820, ECO:0000269\|PubMed:20952539, ECO:0000269\|PubMed:22012619, ECO:0000269\|PubMed:24662513}.
Q9NZB2	FAM120A	S434	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZB2	FAM120A	S1067	ochoa	Constitutive coactivator of PPAR-gamma-like protein 1 (Oxidative stress-associated SRC activator) (Protein FAM120A)	Component of the oxidative stress-induced survival signaling. May regulate the activation of SRC family protein kinases (PubMed:19015244). May act as a scaffolding protein enabling SRC family protein kinases to phosphorylate and activate PI3-kinase (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 protein (PubMed:19015244). {ECO:0000269\|PubMed:19015244}.
Q9NZM3	ITSN2	S210	ochoa	Intersectin-2 (SH3 domain-containing protein 1B) (SH3P18) (SH3P18-like WASP-associated protein)	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:23999003}.
Q9P219	CCDC88C	S1572	ochoa	Protein Daple (Coiled-coil domain-containing protein 88C) (Dvl-associating protein with a high frequency of leucine residues) (hDaple) (Hook-related protein 2) (HkRP2)	Required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling (PubMed:26126266). Binds to ligand-activated Wnt receptor FZD7, displacing DVL1 from the FZD7 receptor and leading to inhibition of canonical Wnt signaling (PubMed:26126266). Acts as a non-receptor guanine nucleotide exchange factor by also binding to guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits, leading to their activation (PubMed:26126266). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex, triggering non-canonical Wnt responses such as activation of RAC1 and PI3K-AKT signaling (PubMed:26126266). Promotes apical constriction of cells via ARHGEF18 (PubMed:30948426). {ECO:0000269\|PubMed:26126266, ECO:0000269\|PubMed:30948426}.
Q9UBC2	EPS15L1	S238	ochoa	Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein) (Eps15R)	Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:22648170, ECO:0000269\|PubMed:9407958}.
Q9UBF9	MYOT	S225	ochoa	Myotilin (57 kDa cytoskeletal protein) (Myofibrillar titin-like Ig domains protein) (Titin immunoglobulin domain protein)	Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells. {ECO:0000269\|PubMed:12499399}.
Q9UBW5	BIN2	S282	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}.
Q9UGU0	TCF20	S1361	ochoa	Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Protein AR1) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein)	Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. {ECO:0000269\|PubMed:10995766}.
Q9UI08	EVL	S337	ochoa	Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
Q9UK76	JPT1	S79	ochoa	Jupiter microtubule associated homolog 1 (Androgen-regulated protein 2) (Hematological and neurological expressed 1 protein) [Cleaved into: Jupiter microtubule associated homolog 1, N-terminally processed]	Modulates negatively AKT-mediated GSK3B signaling (PubMed:21323578, PubMed:22155408). Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions (PubMed:25169422). Plays a role in the regulation of cell cycle and cell adhesion (PubMed:25169422, PubMed:25450365). Has an inhibitory role on AR-signaling pathway through the induction of receptor proteasomal degradation (PubMed:22155408). {ECO:0000269\|PubMed:21323578, ECO:0000269\|PubMed:22155408, ECO:0000269\|PubMed:25169422, ECO:0000269\|PubMed:25450365}.
Q9UKI8	TLK1	S97	ochoa	Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1)	Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. {ECO:0000269\|PubMed:10523312, ECO:0000269\|PubMed:10588641, ECO:0000269\|PubMed:11314006, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:12660173, ECO:0000269\|PubMed:9427565}.
Q9ULU4	ZMYND8	S478	ochoa	MYND-type zinc finger-containing chromatin reader ZMYND8 (Cutaneous T-cell lymphoma-associated antigen se14-3) (CTCL-associated antigen se14-3) (Protein kinase C-binding protein 1) (Rack7) (Transcription coregulator ZMYND8) (Zinc finger MYND domain-containing protein 8)	Chromatin reader that recognizes dual histone modifications such as histone H3.1 dimethylated at 'Lys-36' and histone H4 acetylated at 'Lys-16' (H3.1K36me2-H4K16ac) and histone H3 methylated at 'Lys-4' and histone H4 acetylated at 'Lys-14' (H3K4me1-H3K14ac) (PubMed:26655721, PubMed:27477906, PubMed:31965980, PubMed:36064715). May act as a transcriptional corepressor for KDM5D by recognizing the dual histone signature H3K4me1-H3K14ac (PubMed:27477906). May also act as a transcriptional corepressor for KDM5C and EZH2 (PubMed:33323928). Recognizes acetylated histone H4 and recruits the NuRD chromatin remodeling complex to damaged chromatin for transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309, PubMed:27732854, PubMed:30134174). Also activates transcription elongation by RNA polymerase II through recruiting the P-TEFb complex to target promoters (PubMed:26655721, PubMed:30134174). Localizes to H3.1K36me2-H4K16ac marks at all-trans-retinoic acid (ATRA)-responsive genes and positively regulates their expression (PubMed:26655721). Promotes neuronal differentiation by associating with regulatory regions within the MAPT gene, to enhance transcription of a protein-coding MAPT isoform and suppress the non-coding MAPT213 isoform (PubMed:30134174, PubMed:35916866, PubMed:36064715). Suppresses breast cancer, and prostate cancer cell invasion and metastasis (PubMed:27477906, PubMed:31965980, PubMed:33323928). {ECO:0000269\|PubMed:25593309, ECO:0000269\|PubMed:26655721, ECO:0000269\|PubMed:27477906, ECO:0000269\|PubMed:27732854, ECO:0000269\|PubMed:30134174, ECO:0000269\|PubMed:31965980, ECO:0000269\|PubMed:33323928, ECO:0000269\|PubMed:35916866, ECO:0000269\|PubMed:36064715}.
Q9UQ35	SRRM2	S902	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1073	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1132	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1375	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQ35	SRRM2	S1542	ochoa	Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)	Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269\|PubMed:19854871, ECO:0000269\|PubMed:28076346, ECO:0000269\|PubMed:28502770, ECO:0000269\|PubMed:29301961, ECO:0000269\|PubMed:29360106, ECO:0000269\|PubMed:29361316, ECO:0000269\|PubMed:30705154, ECO:0000269\|PubMed:9531537, ECO:0000305\|PubMed:33509932}.
Q9UQE7	SMC3	S1077	ochoa	Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Basement membrane-associated chondroitin proteoglycan) (Bamacan) (Chondroitin sulfate proteoglycan 6) (Chromosome-associated polypeptide) (hCAP)	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269\|PubMed:11076961, ECO:0000269\|PubMed:19907496}.
Q9UQR0	SCML2	S582	ochoa	Sex comb on midleg-like protein 2	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.
Q9Y2L6	FRMD4B	S766	ochoa	FERM domain-containing protein 4B (GRP1-binding protein GRSP1)	Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex. Plays a redundant role with FRMD4A in epithelial polarization. {ECO:0000250\|UniProtKB:Q920B0}.
Q9Y2W1	THRAP3	S211	ochoa	Thyroid hormone receptor-associated protein 3 (BCLAF1 and THRAP3 family member 2) (Thyroid hormone receptor-associated protein complex 150 kDa component) (Trap150)	Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269\|PubMed:20123736, ECO:0000269\|PubMed:20932480, ECO:0000269\|PubMed:22424773, ECO:0000269\|PubMed:23525231, ECO:0000269\|PubMed:24043798}.
Q9Y3R5	DOP1B	S1183	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y6D6	ARFGEF1	Y662	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6D6	ARFGEF1	S672	ochoa	Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)	Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269\|PubMed:12571360, ECO:0000269\|PubMed:15644318, ECO:0000269\|PubMed:17227842, ECO:0000269\|PubMed:20360857, ECO:0000269\|PubMed:22084092}.
Q9Y6Y8	SEC23IP	S126	ochoa	SEC23-interacting protein (p125)	Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P). {ECO:0000269\|PubMed:10400679, ECO:0000269\|PubMed:15623529, ECO:0000269\|PubMed:22922100}.
Q9H3H1	TRIT1	S431	Sugiyama	tRNA dimethylallyltransferase (EC 2.5.1.75) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (hGRO1) (tRNA isopentenyltransferase 1) (IPTase)	Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i6A37) (PubMed:11111046, PubMed:24126054, PubMed:24901367, PubMed:34774131). Mediates modification of a limited subset of tRNAs: tRNA(Ser)(AGA), tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial modification of the selenocysteine tRNA(Ser)(UCA) (PubMed:24126054). TRIT1 is therefore required for selenoprotein expression (PubMed:24126054). {ECO:0000269\|PubMed:11111046, ECO:0000269\|PubMed:24126054, ECO:0000269\|PubMed:24901367, ECO:0000269\|PubMed:34774131}.
Q86W92	PPFIBP1	S630	Sugiyama	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}.
P53355	DAPK1	S313	GPS6	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.
A7KAX9	ARHGAP32	S2021	ochoa	Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (GTPase regulator interacting with TrkA) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)	GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269\|PubMed:12446789, ECO:0000269\|PubMed:12454018, ECO:0000269\|PubMed:12531901, ECO:0000269\|PubMed:12788081, ECO:0000269\|PubMed:12819203, ECO:0000269\|PubMed:12857875, ECO:0000269\|PubMed:17663722}.
A8MT19	RHPN2P1	S495	ochoa	Putative rhophilin-2-like protein RHPN2P1 (Rhophilin-2 pseudogene 1)	None
O00192	ARVCF	S335	ochoa	Splicing regulator ARVCF (Armadillo repeat protein deleted in velo-cardio-facial syndrome)	Contributes to the regulation of alternative splicing of pre-mRNAs. {ECO:0000269\|PubMed:24644279}.
O00267	SUPT5H	S763	ochoa	Transcription elongation factor SPT5 (hSPT5) (DRB sensitivity-inducing factor 160 kDa subunit) (DSIF p160) (DRB sensitivity-inducing factor large subunit) (DSIF large subunit) (Tat-cotransactivator 1 protein) (Tat-CT1 protein)	Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A (PubMed:10075709, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter (PubMed:10075709, PubMed:10199401, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II (PubMed:16214896). TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme (PubMed:16214896). Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (PubMed:16214896). Following phosphorylation by CDK9, DSIF can also positively regulate transcriptional elongation (PubMed:16427012). Required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat (PubMed:10393184, PubMed:10454543, PubMed:11809800, PubMed:9514752). DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences (PubMed:11112772, PubMed:14701750). {ECO:0000269\|PubMed:10075709, ECO:0000269\|PubMed:10199401, ECO:0000269\|PubMed:10393184, ECO:0000269\|PubMed:10421630, ECO:0000269\|PubMed:10454543, ECO:0000269\|PubMed:10757782, ECO:0000269\|PubMed:10912001, ECO:0000269\|PubMed:11112772, ECO:0000269\|PubMed:11553615, ECO:0000269\|PubMed:11809800, ECO:0000269\|PubMed:12653964, ECO:0000269\|PubMed:12718890, ECO:0000269\|PubMed:14701750, ECO:0000269\|PubMed:15136722, ECO:0000269\|PubMed:15380072, ECO:0000269\|PubMed:16214896, ECO:0000269\|PubMed:16427012, ECO:0000269\|PubMed:9450929, ECO:0000269\|PubMed:9514752, ECO:0000269\|PubMed:9857195}.
O15013	ARHGEF10	S1285	ochoa	Rho guanine nucleotide exchange factor 10	May play a role in developmental myelination of peripheral nerves. {ECO:0000269\|PubMed:14508709}.
O15049	N4BP3	S200	ochoa	NEDD4-binding protein 3 (N4BP3)	Plays a positive role in the antiviral innate immune signaling pathway. Mechanistically, interacts with MAVS and functions as a positive regulator to promote 'Lys-63'-linked polyubiquitination of MAVS and thus strengthens the interaction between MAVS and TRAF2 (PubMed:34880843). Also plays a role in axon and dendrite arborization during cranial nerve development. May also be important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (By similarity). {ECO:0000250\|UniProtKB:A0A1L8GXY6, ECO:0000269\|PubMed:34880843}.
O15164	TRIM24	S654	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15211	RGL2	S578	ochoa	Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) (RalGDS-like factor) (Ras-associated protein RAB2L)	Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity). {ECO:0000250}.
O15265	ATXN7	S207	ochoa	Ataxin-7 (Spinocerebellar ataxia type 7 protein)	Acts as a component of the SAGA (aka STAGA) transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of SAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Probably involved in tethering the deubiquitination module within the SAGA complex (PubMed:24493646). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). Involved in neurodegeneration (PubMed:9288099). {ECO:0000269\|PubMed:15932940, ECO:0000269\|PubMed:18206972, ECO:0000269\|PubMed:22100762, ECO:0000269\|PubMed:24493646, ECO:0000269\|PubMed:9288099}.
O15439	ABCC4	S655	ochoa	ATP-binding cassette sub-family C member 4 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (MRP/cMOAT-related ABC transporter) (Multi-specific organic anion transporter B) (MOAT-B) (Multidrug resistance-associated protein 4)	ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins (PubMed:11856762, PubMed:12523936, PubMed:12835412, PubMed:12883481, PubMed:15364914, PubMed:15454390, PubMed:16282361, PubMed:17959747, PubMed:18300232, PubMed:26721430). Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4 (PubMed:17959747). Mediates the cotransport of bile acids with reduced glutathione (GSH) (PubMed:12523936, PubMed:12883481, PubMed:16282361). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (PubMed:11856762, PubMed:12105214, PubMed:15454390, PubMed:17344354, PubMed:18300232). Confers resistance to anticancer agents such as methotrexate (PubMed:11106685). {ECO:0000269\|PubMed:11106685, ECO:0000269\|PubMed:11856762, ECO:0000269\|PubMed:12105214, ECO:0000269\|PubMed:12523936, ECO:0000269\|PubMed:12835412, ECO:0000269\|PubMed:12883481, ECO:0000269\|PubMed:15364914, ECO:0000269\|PubMed:15454390, ECO:0000269\|PubMed:16282361, ECO:0000269\|PubMed:17344354, ECO:0000269\|PubMed:17959747, ECO:0000269\|PubMed:18300232, ECO:0000269\|PubMed:26721430}.
O15551	CLDN3	S199	ochoa	Claudin-3 (Clostridium perfringens enterotoxin receptor 2) (CPE-R 2) (CPE-receptor 2) (Rat ventral prostate.1 protein homolog) (hRVP1)	Barrier-forming claudin. Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269\|PubMed:36008380}.
O43166	SIPA1L1	S1117	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}.
O43581	SYT7	S103	ochoa	Synaptotagmin-7 (IPCA-7) (Prostate cancer-associated protein 7) (Synaptotagmin VII) (SytVII)	Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory and synaptic vesicles through Ca(2+) and phospholipid binding to the C2 domain (By similarity). Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). SYT7 binds Ca(2+) with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of the plasma membrane repair (PubMed:11342594). Ca(2+)-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (By similarity). Ca(2+)-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (By similarity). In case of infection, involved in participates cell invasion by Trypanosoma cruzi via Ca(2+)-triggered lysosomal exocytosis (PubMed:11342594, PubMed:15811535). Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes (By similarity). Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca(2+) into the axon terminal after spike generation, increasing the release probability of neurotransmitters (By similarity). Probably mediates synaptic facilitation by directly increasing the probability of release (By similarity). May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca(2+) and by forming a complex with calmodulin (By similarity). Also acts as a regulator of Ca(2+)-dependent insulin and glucagon secretion in beta-cells (By similarity). Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (By similarity). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (By similarity). {ECO:0000250\|UniProtKB:Q62747, ECO:0000250\|UniProtKB:Q9R0N7, ECO:0000269\|PubMed:11342594, ECO:0000269\|PubMed:15811535}.
O60381	HBP1	S372	psp	HMG box-containing protein 1 (HMG box transcription factor 1) (High mobility group box transcription factor 1)	Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4. {ECO:0000269\|PubMed:10562551, ECO:0000269\|PubMed:10958660, ECO:0000269\|PubMed:11500377}.
O60825	PFKFB2	S473	ochoa	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)]	Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269\|PubMed:11069105}.
O60861	GAS7	S152	ochoa	Growth arrest-specific protein 7 (GAS-7)	May play a role in promoting maturation and morphological differentiation of cerebellar neurons.
O60885	BRD4	S488	psp	Bromodomain-containing protein 4 (Protein HUNK1)	Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). {ECO:0000250\|UniProtKB:Q9ESU6, ECO:0000269\|PubMed:16109376, ECO:0000269\|PubMed:16109377, ECO:0000269\|PubMed:19103749, ECO:0000269\|PubMed:19596240, ECO:0000269\|PubMed:22334664, ECO:0000269\|PubMed:22509028, ECO:0000269\|PubMed:23086925, ECO:0000269\|PubMed:23317504, ECO:0000269\|PubMed:23589332, ECO:0000269\|PubMed:24360279, ECO:0000269\|PubMed:29176719}.; FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation. {ECO:0000269\|PubMed:23728299}.
O75369	FLNB	S2486	ochoa	Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)	Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
O75396	SEC22B	S164	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}.
O75410	TACC1	S305	ochoa	Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1)	Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways (PubMed:20078863). Might promote the nuclear localization of the receptors (PubMed:20078863). Likely involved in the processes that promote cell division prior to the formation of differentiated tissues. {ECO:0000269\|PubMed:20078863}.
O75427	LRCH4	S307	ochoa	Leucine-rich repeat and calponin homology domain-containing protein 4 (Leucine-rich repeat neuronal protein 4) (Leucine-rich neuronal protein)	Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance. {ECO:0000250\|UniProtKB:Q921G6}.
O76094	SRP72	S610	ochoa	Signal recognition particle subunit SRP72 (SRP72) (Signal recognition particle 72 kDa protein)	Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:34020957). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (PubMed:34020957). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68 (PubMed:21073748, PubMed:27899666). Can bind 7SL RNA with low affinity (PubMed:21073748, PubMed:27899666). The SRP complex possibly participates in the elongation arrest function (By similarity). {ECO:0000250\|UniProtKB:P38688, ECO:0000269\|PubMed:21073748, ECO:0000269\|PubMed:27899666, ECO:0000269\|PubMed:34020957}.
O94915	FRYL	S1970	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}.
O95292	VAPB	S146	ochoa	Vesicle-associated membrane protein-associated protein B/C (VAMP-B/VAMP-C) (VAMP-associated protein B/C) (VAP-B/VAP-C)	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). Interacts with STARD3 in a FFAT motif phosphorylation dependent manner (PubMed:33124732). Via interaction with WDR44 participates in neosynthesized protein export (PubMed:32344433). Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity (PubMed:16891305, PubMed:20940299). Involved in cellular calcium homeostasis regulation (PubMed:22131369). {ECO:0000269\|PubMed:16891305, ECO:0000269\|PubMed:20940299, ECO:0000269\|PubMed:22131369, ECO:0000269\|PubMed:32344433, ECO:0000269\|PubMed:33124732}.
O95425	SVIL	S253	ochoa	Supervillin (Archvillin) (p205/p250)	[Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269\|PubMed:12711699, ECO:0000269\|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250\|UniProtKB:O46385}.
O95639	CPSF4	S201	ochoa	Cleavage and polyadenylation specificity factor subunit 4 (Cleavage and polyadenylation specificity factor 30 kDa subunit) (CPSF 30 kDa subunit) (NS1 effector domain-binding protein 1) (Neb-1) (No arches homolog)	Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U). {ECO:0000269\|PubMed:14749727, ECO:0000269\|PubMed:9224719}.
P07814	EPRS1	Y872	ochoa	Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]	Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:3290852, PubMed:37212275). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:15479637, PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000269\|PubMed:15479637, ECO:0000269\|PubMed:23071094, ECO:0000269\|PubMed:23263184, ECO:0000269\|PubMed:24100331, ECO:0000269\|PubMed:28178239, ECO:0000269\|PubMed:29576217, ECO:0000269\|PubMed:3290852, ECO:0000269\|PubMed:37212275}.
P08238	HSP90AB1	S460	ochoa	Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3)	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269\|PubMed:16478993, ECO:0000269\|PubMed:18239673, ECO:0000269\|PubMed:19696785, ECO:0000269\|PubMed:20353823, ECO:0000269\|PubMed:24613385, ECO:0000269\|PubMed:32272059, ECO:0000303\|PubMed:25973397, ECO:0000303\|PubMed:26991466, ECO:0000303\|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269\|PubMed:21949862, ECO:0000305\|PubMed:22066472}.
P11137	MAP2	S1790	ochoa	Microtubule-associated protein 2 (MAP-2)	The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
P11532	DMD	S3613	ochoa	Dystrophin	Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000250\|UniProtKB:P11531, ECO:0000269\|PubMed:16710609}.
P13804	ETFA	S172	ochoa	Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF)	Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:10356313, PubMed:15159392, PubMed:15975918, PubMed:27499296, PubMed:9334218). It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:9334218). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism (PubMed:12815589, PubMed:1430199, PubMed:1882842). {ECO:0000269\|PubMed:10356313, ECO:0000269\|PubMed:12815589, ECO:0000269\|PubMed:1430199, ECO:0000269\|PubMed:15159392, ECO:0000269\|PubMed:15975918, ECO:0000269\|PubMed:27499296, ECO:0000269\|PubMed:9334218, ECO:0000303\|PubMed:17941859, ECO:0000305\|PubMed:1882842}.
P15884	TCF4	S188	ochoa	Transcription factor 4 (TCF-4) (Class B basic helix-loop-helix protein 19) (bHLHb19) (Immunoglobulin transcription factor 2) (ITF-2) (SL3-3 enhancer factor 2) (SEF-2)	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'. {ECO:0000250}.
P17302	GJA1	S262	ochoa\|psp	Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein)	Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity). {ECO:0000250\|UniProtKB:P08050, ECO:0000250\|UniProtKB:P23242}.
P18583	SON	S1585	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}.
P22087	FBL	S116	ochoa	rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (34 kDa nucleolar scleroderma antigen) (Histone-glutamine methyltransferase) (U6 snRNA 2'-O-methyltransferase fibrillarin)	S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins (PubMed:24352239, PubMed:30540930, PubMed:32017898). Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:30540930). Site specificity is provided by a guide RNA that base pairs with the substrate (By similarity). Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity). Probably catalyzes 2'-O-methylation of U6 snRNAs in box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239, PubMed:30540930). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250\|UniProtKB:P15646, ECO:0000269\|PubMed:24352239, ECO:0000269\|PubMed:30540930, ECO:0000269\|PubMed:32017898, ECO:0000269\|PubMed:34516797}.
P25054	APC	S1032	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}.
P29401	TKT	S295	ochoa	Transketolase (TK) (EC 2.2.1.1)	Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. {ECO:0000269\|PubMed:27259054}.
P36507	MAP2K2	S216	ochoa\|psp	Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)	Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). {ECO:0000250\|UniProtKB:Q63932, ECO:0000269\|PubMed:29433126}.
P42566	EPS15	S670	ochoa	Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)	Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269\|PubMed:16903783, ECO:0000269\|PubMed:18362181, ECO:0000269\|PubMed:19458185, ECO:0000269\|PubMed:22648170}.
P43243	MATR3	S501	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	S174	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	S1679	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}.
P46531	NOTCH1	S2513	psp	Neurogenic locus notch homolog protein 1 (Notch 1) (hN1) (Translocation-associated notch protein TAN-1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]	Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000269\|PubMed:20616313}.
P49790	NUP153	S164	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P49790	NUP153	S172	ochoa	Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)	Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269\|PubMed:12802065, ECO:0000269\|PubMed:15229283, ECO:0000269\|PubMed:22253824}.; FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269\|PubMed:23523133, ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:29997211}.; FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269\|PubMed:24130490, ECO:0000269\|PubMed:31913756}.
P50552	VASP	T315	ochoa	Vasodilator-stimulated phosphoprotein (VASP)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. {ECO:0000269\|PubMed:10087267, ECO:0000269\|PubMed:10438535, ECO:0000269\|PubMed:15939738, ECO:0000269\|PubMed:17082196, ECO:0000269\|PubMed:18559661}.
P50851	LRBA	S1076	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}.
P54296	MYOM2	S52	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.
P57679	EVC	S71	ochoa	EvC complex member EVC (DWF-1) (Ellis-van Creveld syndrome protein)	Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling. Involved in endochondral growth and skeletal development. {ECO:0000250\|UniProtKB:P57680}.
P78332	RBM6	S370	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.
P78559	MAP1A	S1190	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.
Q02750	MAP2K1	S212	ochoa\|psp	Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (MKK1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. {ECO:0000269\|PubMed:14737111, ECO:0000269\|PubMed:17101779, ECO:0000269\|PubMed:29433126}.
Q02952	AKAP12	S732	ochoa\|psp	A-kinase anchor protein 12 (AKAP-12) (A-kinase anchor protein 250 kDa) (AKAP 250) (Gravin) (Myasthenia gravis autoantigen)	Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Q05209	PTPN12	S507	ochoa	Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1)	Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). {ECO:0000269\|PubMed:17329398, ECO:0000269\|PubMed:18559503, ECO:0000269\|PubMed:27134172}.
Q08357	SLC20A2	S424	ochoa	Sodium-dependent phosphate transporter 2 (Gibbon ape leukemia virus receptor 2) (GLVR-2) (Phosphate transporter 2) (PiT-2) (Pit2) (hPit2) (Solute carrier family 20 member 2)	Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:12205090, PubMed:15955065, PubMed:16790504, PubMed:17494632, PubMed:22327515, PubMed:28722801, PubMed:30704756). Plays a critical role in the determination of bone quality and strength by providing phosphate for bone mineralization (By similarity). Required to maintain normal cerebrospinal fluid phosphate levels (By similarity). Mediates phosphate-induced calcification of vascular smooth muscle cells (VCMCs) and can functionally compensate for loss of SLC20A1 in VCMCs (By similarity). {ECO:0000250\|UniProtKB:Q80UP8, ECO:0000269\|PubMed:12205090, ECO:0000269\|PubMed:15955065, ECO:0000269\|PubMed:16790504, ECO:0000269\|PubMed:17494632, ECO:0000269\|PubMed:22327515, ECO:0000269\|PubMed:28722801, ECO:0000269\|PubMed:30704756}.; FUNCTION: (Microbial infection) Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. {ECO:0000269\|PubMed:11435563, ECO:0000269\|PubMed:12205090, ECO:0000269\|PubMed:15955065, ECO:0000269\|PubMed:8302848}.
Q13427	PPIG	S677	ochoa	Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (CASP10) (Clk-associating RS-cyclophilin) (CARS-Cyp) (CARS-cyclophilin) (SR-cyclophilin) (SR-cyp) (SRcyp) (Cyclophilin G) (Rotamase G)	PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. {ECO:0000269\|PubMed:20676357}.
Q13428	TCOF1	S1191	ochoa	Treacle protein (Treacher Collins syndrome protein)	Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269\|PubMed:12777385, ECO:0000269\|PubMed:26399832}.
Q13501	SQSTM1	S266	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}.
Q13613	MTMR1	S647	ochoa	Phosphatidylinositol-3-phosphate phosphatase MTMR1 (EC 3.1.3.-) (Myotubularin-related protein 1) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95)	Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate, generating phosphatidylinositol (PubMed:11733541, PubMed:27018598). Could also dephosphorylate phosphatidylinositol 3,5-bisphosphate to produce phosphatidylinositol 5-phosphate (PubMed:27018598). {ECO:0000269\|PubMed:11733541, ECO:0000269\|PubMed:27018598}.
Q14149	MORC3	S550	ochoa	MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)	Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696). Binds RNA in vitro (PubMed:11927593). Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034). {ECO:0000269\|PubMed:11927593, ECO:0000269\|PubMed:17332504, ECO:0000269\|PubMed:20501696, ECO:0000269\|PubMed:26933034, ECO:0000269\|PubMed:27440897, ECO:0000269\|PubMed:34759314}.; FUNCTION: (Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269\|PubMed:26202233}.
Q14674	ESPL1	S1528	ochoa	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}.
Q14980	NUMA1	S190	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q14980	NUMA1	S1862	ochoa	Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)	Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity). {ECO:0000250\|UniProtKB:E9Q7G0, ECO:0000269\|PubMed:11163243, ECO:0000269\|PubMed:11229403, ECO:0000269\|PubMed:11956313, ECO:0000269\|PubMed:12445386, ECO:0000269\|PubMed:16076287, ECO:0000269\|PubMed:17172455, ECO:0000269\|PubMed:19255246, ECO:0000269\|PubMed:22327364, ECO:0000269\|PubMed:23027904, ECO:0000269\|PubMed:23870127, ECO:0000269\|PubMed:23921553, ECO:0000269\|PubMed:24109598, ECO:0000269\|PubMed:24371089, ECO:0000269\|PubMed:24996901, ECO:0000269\|PubMed:25657325, ECO:0000269\|PubMed:26195665, ECO:0000269\|PubMed:26765568, ECO:0000269\|PubMed:27462074, ECO:0000269\|PubMed:7769006, ECO:0000305\|PubMed:10075938, ECO:0000305\|PubMed:21816348}.
Q15036	SNX17	S325	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}.
Q29RF7	PDS5A	S1223	ochoa	Sister chromatid cohesion protein PDS5 homolog A (Cell proliferation-inducing gene 54 protein) (Sister chromatid cohesion protein 112) (SCC-112)	Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269\|PubMed:15855230, ECO:0000269\|PubMed:19907496}.
Q2KJY2	KIF26B	S1762	ochoa	Kinesin-like protein KIF26B	Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.
Q2M1P5	KIF7	S456	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}.
Q5QJE6	DNTTIP2	S82	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}.
Q5T4S7	UBR4	S1752	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}.
Q5THJ4	VPS13D	S1699	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	S1189	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}.
Q5VT52	RPRD2	S899	ochoa	Regulation of nuclear pre-mRNA domain-containing protein 2	None
Q5W0B1	OBI1	S561	ochoa	ORC ubiquitin ligase 1 (OBI1) (EC 2.3.2.27) (RING finger protein 219)	E3 ubiquitin ligase essential for DNA replication origin activation during S phase (PubMed:31160578). Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-phase (PubMed:31160578). {ECO:0000269\|PubMed:31160578}.
Q68DQ2	CRYBG3	S340	ochoa	Very large A-kinase anchor protein (vlAKAP) (Beta/gamma crystallin domain-containing protein 3)	[Isoform vlAKAP]: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269\|PubMed:25097019}.
Q69YH5	CDCA2	S608	ochoa	Cell division cycle-associated protein 2 (Recruits PP1 onto mitotic chromatin at anaphase protein) (Repo-Man)	Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates. {ECO:0000269\|PubMed:16492807, ECO:0000269\|PubMed:16998479}.
Q6NYC8	PPP1R18	S203	ochoa	Phostensin (Protein phosphatase 1 F-actin cytoskeleton-targeting subunit) (Protein phosphatase 1 regulatory subunit 18)	[Isoform 1]: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000269\|PubMed:24434620}.; FUNCTION: [Isoform 4]: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000269\|PubMed:17374523}.
Q6NZY4	ZCCHC8	S591	ochoa	Zinc finger CCHC domain-containing protein 8 (TRAMP-like complex RNA-binding factor ZCCHC8)	Scaffolding subunit of the trimeric nuclear exosome targeting (NEXT) complex that is involved in the surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed:27871484). NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. May be involved in pre-mRNA splicing (Probable). It is required for 3'-end maturation of telomerase RNA component (TERC), TERC 3'-end targeting to the nuclear RNA exosome, and for telomerase function (PubMed:31488579). {ECO:0000269\|PubMed:27871484, ECO:0000269\|PubMed:31488579, ECO:0000305\|PubMed:16263084}.
Q6P996	PDXDC1	S714	ochoa	Pyridoxal-dependent decarboxylase domain-containing protein 1 (EC 4.1.1.-)	None
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}.
Q6VMQ6	ATF7IP	S473	ochoa	Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621)	Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Required for HUSH-mediated heterochromatin formation and gene silencing (PubMed:27732843). Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1 (PubMed:12665582). Stabilizes SETDB1, is required to stimulate histone methyltransferase activity of SETDB1 and facilitates the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) (PubMed:14536086, PubMed:27732843). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells (PubMed:19106100). {ECO:0000269\|PubMed:12665582, ECO:0000269\|PubMed:14536086, ECO:0000269\|PubMed:19106100, ECO:0000269\|PubMed:27732843}.
Q6ZUJ8	PIK3AP1	S562	ochoa	Phosphoinositide 3-kinase adapter protein 1 (B-cell adapter for phosphoinositide 3-kinase) (B-cell phosphoinositide 3-kinase adapter protein 1)	Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. {ECO:0000269\|PubMed:15893754}.
Q765P7	MTSS2	S332	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	S30	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}.
Q7Z2Z1	TICRR	S1420	ochoa	Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein)	Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269\|PubMed:20116089}.
Q7Z6Z7	HUWE1	S2917	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}.
Q8IUC4	RHPN2	S598	ochoa	Rhophilin-2 (76 kDa RhoB effector protein) (GTP-Rho-binding protein 2) (p76RBE)	Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity. {ECO:0000269\|PubMed:12221077}.
Q8IVT5	KSR1	S184	ochoa	Kinase suppressor of Ras 1 (EC 2.7.11.1)	Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (By similarity). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (PubMed:29433126). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (By similarity). Its kinase activity is unsure (By similarity). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (By similarity). {ECO:0000250\|UniProtKB:Q61097, ECO:0000269\|PubMed:29433126}.
Q8N122	RPTOR	S711	ochoa\|psp	Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein)	Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity). {ECO:0000250\|UniProtKB:Q8K4Q0, ECO:0000269\|PubMed:12150925, ECO:0000269\|PubMed:12150926, ECO:0000269\|PubMed:12747827, ECO:0000269\|PubMed:24403073, ECO:0000269\|PubMed:26588989, ECO:0000269\|PubMed:32561715, ECO:0000269\|PubMed:37541260}.
Q8N1G2	CMTR1	S28	ochoa	Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap methyltransferase 1) (Cap1 2'O-ribose methyltransferase 1) (MTr1) (hMTr1) (FtsJ methyltransferase domain-containing protein 2) (Interferon-stimulated gene 95 kDa protein) (ISG95)	S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269\|PubMed:18533109, ECO:0000269\|PubMed:20713356, ECO:0000269\|PubMed:21310715}.
Q8N5G2	MACO1	S337	ochoa	Macoilin (Macoilin-1) (Transmembrane protein 57)	Plays a role in the regulation of neuronal activity. {ECO:0000269\|PubMed:21589894}.
Q8N6T3	ARFGAP1	S150	ochoa	ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)	GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). {ECO:0000250}.
Q8NF91	SYNE1	S8664	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}.
Q8NFC6	BOD1L1	S2954	ochoa	Biorientation of chromosomes in cell division protein 1-like 1	Component of the fork protection machinery required to protect stalled/damaged replication forks from uncontrolled DNA2-dependent resection. Acts by stabilizing RAD51 at stalled replication forks and protecting RAD51 nucleofilaments from the antirecombinogenic activities of FBH1 and BLM (PubMed:26166705, PubMed:29937342). Does not regulate spindle orientation (PubMed:26166705). {ECO:0000269\|PubMed:26166705, ECO:0000269\|PubMed:29937342}.
Q8NFG4	FLCN	S62	ochoa\|psp	Folliculin (BHD skin lesion fibrofolliculoma protein) (Birt-Hogg-Dube syndrome protein)	Multi-functional protein, involved in both the cellular response to amino acid availability and in the regulation of glycolysis (PubMed:17028174, PubMed:18663353, PubMed:21209915, PubMed:24081491, PubMed:24095279, PubMed:31672913, PubMed:31704029, PubMed:32612235, PubMed:34381247, PubMed:36103527, PubMed:37079666). GTPase-activating protein that plays a key role in the cellular response to amino acid availability through regulation of the non-canonical mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3 (PubMed:17028174, PubMed:18663353, PubMed:21209915, PubMed:24081491, PubMed:24095279, PubMed:24448649, PubMed:31672913, PubMed:31704029, PubMed:32612235, PubMed:36103527, PubMed:37079666). Activates mTORC1 by acting as a GTPase-activating protein: specifically stimulates GTP hydrolysis by RagC/RRAGC or RagD/RRAGD, promoting the conversion to the GDP-bound state of RagC/RRAGC or RagD/RRAGD, and thereby activating the kinase activity of mTORC1 (PubMed:24095279, PubMed:31672913, PubMed:31704029, PubMed:32612235, PubMed:37079666). The GTPase-activating activity is inhibited during starvation and activated in presence of nutrients (PubMed:31672913, PubMed:32612235). Acts as a key component for non-canonical mTORC1-dependent control of the MiT/TFE factors TFEB and TFE3, while it is not involved in mTORC1-dependent phosphorylation of canonical RPS6KB1/S6K1 and EIF4EBP1/4E-BP1 (PubMed:21209915, PubMed:24081491, PubMed:31672913, PubMed:32612235). In low-amino acid conditions, the lysosomal folliculin complex (LFC) is formed on the membrane of lysosomes, which inhibits the GTPase-activating activity of FLCN, inactivates mTORC1 and maximizes nuclear translocation of TFEB and TFE3 (PubMed:31672913). Upon amino acid restimulation, RagA/RRAGA (or RagB/RRAGB) nucleotide exchange promotes disassembly of the LFC complex and liberates the GTPase-activating activity of FLCN, leading to activation of mTORC1 and subsequent cytoplasmic retention of TFEB and TFE3 (PubMed:31672913). Indirectly acts as a positive regulator of Wnt signaling by promoting mTOR-dependent cytoplasmic retention of MiT/TFE factor TFE3 (PubMed:31272105). Required for the exit of hematopoietic stem cell from pluripotency by promoting mTOR-dependent cytoplasmic retention of TFE3, thereby increasing Wnt signaling (PubMed:30733432). Acts as an inhibitor of browning of adipose tissue by regulating mTOR-dependent cytoplasmic retention of TFE3 (By similarity). Involved in the control of embryonic stem cells differentiation; together with LAMTOR1 it is necessary to recruit and activate RagC/RRAGC and RagD/RRAGD at the lysosomes, and to induce exit of embryonic stem cells from pluripotency via non-canonical, mTOR-independent TFE3 inactivation (By similarity). In response to flow stress, regulates STK11/LKB1 accumulation and mTORC1 activation through primary cilia: may act by recruiting STK11/LKB1 to primary cilia for activation of AMPK resided at basal bodies, causing mTORC1 down-regulation (PubMed:27072130). Together with FNIP1 and/or FNIP2, regulates autophagy: following phosphorylation by ULK1, interacts with GABARAP and promotes autophagy (PubMed:25126726). Required for starvation-induced perinuclear clustering of lysosomes by promoting association of RILP with its effector RAB34 (PubMed:27113757). Regulates glycolysis by binding to lactate dehydrogenase LDHA, acting as an uncompetitive inhibitor (PubMed:34381247). {ECO:0000250\|UniProtKB:Q8QZS3, ECO:0000269\|PubMed:17028174, ECO:0000269\|PubMed:18663353, ECO:0000269\|PubMed:21209915, ECO:0000269\|PubMed:24081491, ECO:0000269\|PubMed:24095279, ECO:0000269\|PubMed:24448649, ECO:0000269\|PubMed:25126726, ECO:0000269\|PubMed:27072130, ECO:0000269\|PubMed:27113757, ECO:0000269\|PubMed:30733432, ECO:0000269\|PubMed:31272105, ECO:0000269\|PubMed:31672913, ECO:0000269\|PubMed:31704029, ECO:0000269\|PubMed:32612235, ECO:0000269\|PubMed:34381247, ECO:0000269\|PubMed:36103527, ECO:0000269\|PubMed:37079666}.
Q8NI08	NCOA7	S162	ochoa	Nuclear receptor coactivator 7 (140 kDa estrogen receptor-associated protein) (Estrogen nuclear receptor coactivator 1)	Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269\|PubMed:11971969}.
Q8NI08	NCOA7	S173	ochoa	Nuclear receptor coactivator 7 (140 kDa estrogen receptor-associated protein) (Estrogen nuclear receptor coactivator 1)	Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269\|PubMed:11971969}.
Q8TBZ3	WDR20	S347	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}.
Q8TDM6	DLG5	S1254	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}.
Q8TF40	FNIP1	S938	psp	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}.
Q8WWM7	ATXN2L	S594	ochoa	Ataxin-2-like protein (Ataxin-2 domain protein) (Ataxin-2-related protein)	Involved in the regulation of stress granule and P-body formation. {ECO:0000269\|PubMed:23209657}.
Q8WYQ5	DGCR8	S367	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}.
Q92900	UPF1	S1100	ochoa	Regulator of nonsense transcripts 1 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (hUpf1)	RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD (PubMed:11544179, PubMed:25220460). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD (PubMed:21419344). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors (PubMed:12554878). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (PubMed:18447585). Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (PubMed:16086026, PubMed:18172165). For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (PubMed:21145460). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (By similarity). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (PubMed:30218034). {ECO:0000250\|UniProtKB:Q9EPU0, ECO:0000269\|PubMed:11163187, ECO:0000269\|PubMed:11544179, ECO:0000269\|PubMed:12554878, ECO:0000269\|PubMed:16086026, ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:18447585, ECO:0000269\|PubMed:19417104, ECO:0000269\|PubMed:21145460, ECO:0000269\|PubMed:21419344, ECO:0000269\|PubMed:24726324, ECO:0000269\|PubMed:25220460, ECO:0000269\|PubMed:30218034}.
Q92985	IRF7	S477	psp	Interferon regulatory factor 7 (IRF-7)	Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:28342865, PubMed:28768858). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:17574024, PubMed:32972995). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (By similarity). Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages (By similarity) (PubMed:11073981, PubMed:12374802, PubMed:15361868, PubMed:17404045). {ECO:0000250\|UniProtKB:P70434, ECO:0000269\|PubMed:11073981, ECO:0000269\|PubMed:12374802, ECO:0000269\|PubMed:15361868, ECO:0000269\|PubMed:17404045, ECO:0000269\|PubMed:17574024, ECO:0000269\|PubMed:28342865, ECO:0000269\|PubMed:28768858, ECO:0000269\|PubMed:32972995}.
Q96BY7	ATG2B	S1008	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}.
Q96EV2	RBM33	S731	ochoa	RNA-binding protein 33 (Proline-rich protein 8) (RNA-binding motif protein 33)	RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as mRNA export, mRNA stability and/or translation (PubMed:35589130, PubMed:37257451). Binds a subset of intronless RNAs containing GC-rich elements, such as NORAD, and promotes their nuclear export by recruiting target RNAs to components of the NXF1-NXT1 RNA export machinery (PubMed:35589130). Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, promoting their demethylation by ALKBH5 (PubMed:37257451). Acts as an molecular adapter, which (1) promotes ALKBH5 recruitment to m6A-containing transcripts and (2) activates ALKBH5 demethylase activity by recruiting SENP1, leading to ALKBH5 deSUMOylation and subsequent activation (PubMed:37257451). {ECO:0000269\|PubMed:35589130, ECO:0000269\|PubMed:37257451}.
Q96I24	FUBP3	S528	ochoa	Far upstream element-binding protein 3 (FUSE-binding protein 3)	May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression.
Q96K76	USP47	S946	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}.
Q96Q15	SMG1	S1897	ochoa	Serine/threonine-protein kinase SMG1 (SMG-1) (hSMG-1) (EC 2.7.11.1) (Lambda/iota protein kinase C-interacting protein) (Lambda-interacting protein) (Nonsense mediated mRNA decay-associated PI3K-related kinase SMG1)	Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. {ECO:0000269\|PubMed:11331269, ECO:0000269\|PubMed:11544179, ECO:0000269\|PubMed:15175154, ECO:0000269\|PubMed:16452507}.
Q96RG2	PASK	S109	ochoa	PAS domain-containing serine/threonine-protein kinase (PAS-kinase) (PASKIN) (hPASK) (EC 2.7.11.1)	Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. {ECO:0000269\|PubMed:16275910, ECO:0000269\|PubMed:17052199, ECO:0000269\|PubMed:17595531, ECO:0000269\|PubMed:20943661, ECO:0000269\|PubMed:21181396, ECO:0000269\|PubMed:21418524}.
Q99081	TCF12	S534	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}.
Q99640	PKMYT1	S94	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}.
Q99700	ATXN2	S207	ochoa	Ataxin-2 (Spinocerebellar ataxia type 2 protein) (Trinucleotide repeat-containing gene 13 protein)	Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269\|PubMed:18602463}.
Q99704	DOK1	S450	ochoa\|psp	Docking protein 1 (Downstream of tyrosine kinase 1) (p62(dok)) (pp62)	DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269\|PubMed:18156175}.
Q99755	PIP5K1A	S476	ochoa	Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha)	Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:21477596, PubMed:22942276, PubMed:8955136). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (PubMed:19158393, PubMed:20660631). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Can also use phosphatidylinositol (PtdIns) as substrate in vitro (PubMed:22942276). Together with PIP5K1C, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (By similarity). Promotes particle ingestion by activating the WAS GTPase-binding protein that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup (By similarity). Together with PIP5K1B, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, IP3 and DAG, that will mobilize internal calcium and drive keratinocyte differentiation (PubMed:19158393). Positively regulates insulin-induced translocation of SLC2A4 to the cell membrane in adipocytes (By similarity). Together with PIP5K1C has a role during embryogenesis (By similarity). Independently of its catalytic activity, is required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of the small GTPase RAC1 to the plasma membrane (PubMed:20660631). Also functions in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs (PubMed:18288197). {ECO:0000250\|UniProtKB:P70182, ECO:0000269\|PubMed:18288197, ECO:0000269\|PubMed:19158393, ECO:0000269\|PubMed:20660631, ECO:0000269\|PubMed:21477596, ECO:0000269\|PubMed:22942276, ECO:0000269\|PubMed:8955136}.
Q99816	TSG101	S222	ochoa	Tumor susceptibility gene 101 protein (ESCRT-I complex subunit TSG101)	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). It may also play a role in the extracellular release of microvesicles that differ from the exosomes (PubMed:22315426). {ECO:0000269\|PubMed:11916981, ECO:0000269\|PubMed:17556548, ECO:0000269\|PubMed:17853893, ECO:0000269\|PubMed:21070952, ECO:0000269\|PubMed:21757351, ECO:0000269\|PubMed:22315426, ECO:0000269\|PubMed:22660413}.
Q9BQL6	FERMT1	S169	ochoa	Fermitin family homolog 1 (Kindlerin) (Kindlin syndrome protein) (Kindlin-1) (Unc-112-related protein 1)	Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression. {ECO:0000269\|PubMed:14634021, ECO:0000269\|PubMed:17012746, ECO:0000269\|PubMed:19804783}.
Q9BSQ5	CCM2	S238	ochoa\|psp	Cerebral cavernous malformations 2 protein (Malcavernin)	Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity). {ECO:0000250}.
Q9BTA9	WAC	S436	ochoa	WW domain-containing adapter protein with coiled-coil	Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1) (PubMed:21329877). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription (PubMed:21329877). Regulates the cell-cycle checkpoint activation in response to DNA damage (PubMed:21329877). Positive regulator of amino acid starvation-induced autophagy (PubMed:22354037). Also acts as a negative regulator of basal autophagy (PubMed:26812014). Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014). May negatively regulate the ubiquitin proteasome pathway (PubMed:21329877). {ECO:0000269\|PubMed:21329877, ECO:0000269\|PubMed:22354037, ECO:0000269\|PubMed:26812014}.
Q9BTC0	DIDO1	S1030	ochoa	Death-inducer obliterator 1 (DIO-1) (hDido1) (Death-associated transcription factor 1) (DATF-1)	Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development. {ECO:0000250, ECO:0000269\|PubMed:16127461}.; FUNCTION: [Isoform 2]: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes. {ECO:0000269\|PubMed:16127461}.
Q9BUL5	PHF23	S64	ochoa	PHD finger protein 23 (PDH-containing protein JUNE-1)	Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000269\|PubMed:25484098}.
Q9BUL5	PHF23	S305	ochoa	PHD finger protein 23 (PDH-containing protein JUNE-1)	Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria. {ECO:0000269\|PubMed:25484098}.
Q9BX66	SORBS1	S272	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}.
Q9C0B0	UNK	S598	ochoa\|psp	RING finger protein unkempt homolog (Zinc finger CCCH domain-containing protein 5)	Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280). {ECO:0000269\|PubMed:25737280}.
Q9C0D5	TANC1	S207	ochoa	Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1)	May be a scaffold component in the postsynaptic density. {ECO:0000250}.
Q9C0D5	TANC1	S1670	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}.
Q9GZR1	SENP6	S352	ochoa	Sentrin-specific protease 6 (EC 3.4.22.-) (SUMO-1-specific protease 1) (Sentrin/SUMO-specific protease SENP6)	Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Also desumoylates RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. {ECO:0000269\|PubMed:16912044, ECO:0000269\|PubMed:17000875, ECO:0000269\|PubMed:18799455, ECO:0000269\|PubMed:20212317, ECO:0000269\|PubMed:20705237, ECO:0000269\|PubMed:21148299}.
Q9GZY8	MFF	S223	ochoa	Mitochondrial fission factor	Plays a role in mitochondrial and peroxisomal fission (PubMed:18353969, PubMed:23530241, PubMed:24196833). Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (PubMed:23530241). May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity). {ECO:0000250\|UniProtKB:Q4KM98, ECO:0000269\|PubMed:18353969, ECO:0000269\|PubMed:23530241, ECO:0000269\|PubMed:24196833}.
Q9H019	MTFR1L	S224	ochoa	Mitochondrial fission regulator 1-like	Mitochondrial protein required for adaptation of miochondrial dynamics to metabolic changes. Regulates mitochondrial morphology at steady state and mediates AMPK-dependent stress-induced mitochondrial fragmentation via the control of OPA1 levels. {ECO:0000269\|PubMed:36367943}.
Q9H1A4	ANAPC1	S299	ochoa	Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein)	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269\|PubMed:18485873, ECO:0000269\|PubMed:29033132}.
Q9H1H9	KIF13A	S1753	ochoa	Kinesin-like protein KIF13A (Kinesin-like protein RBKIN)	Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abscission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269\|PubMed:19841138, ECO:0000269\|PubMed:20208530}.
Q9H1K0	RBSN	S209	ochoa	Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20)	Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269\|PubMed:11062261, ECO:0000269\|PubMed:11788822, ECO:0000269\|PubMed:15020713, ECO:0000269\|PubMed:22308388}.
Q9H211	CDT1	S380	ochoa	DNA replication factor Cdt1 (Double parked homolog) (DUP)	Required for both DNA replication and mitosis (PubMed:11125146, PubMed:14993212, PubMed:21856198, PubMed:22581055, PubMed:26842564). DNA replication licensing factor, required for pre-replication complex assembly. Cooperates with CDC6 and the origin recognition complex (ORC) during G1 phase of the cell cycle to promote the loading of the mini-chromosome maintenance (MCM) complex onto DNA to generate pre-replication complexes (pre-RC) (PubMed:14672932). Required also for mitosis by promoting stable kinetochore-microtubule attachments (PubMed:22581055). Potential oncogene (By similarity). {ECO:0000250\|UniProtKB:Q8R4E9, ECO:0000269\|PubMed:11125146, ECO:0000269\|PubMed:14672932, ECO:0000269\|PubMed:14993212, ECO:0000269\|PubMed:21856198, ECO:0000269\|PubMed:22581055, ECO:0000269\|PubMed:26842564}.
Q9H5V7	IKZF5	S298	ochoa	Zinc finger protein Pegasus (Ikaros family zinc finger protein 5)	Transcriptional repressor that binds the core 5'GNNTGTNG-3' DNA consensus sequence (PubMed:10978333, PubMed:31217188). Involved in megakaryocyte differentiation. {ECO:0000269\|PubMed:10978333, ECO:0000269\|PubMed:31217188}.
Q9H6S1	AZI2	S343	ochoa	5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1) (Nap1) (TILP)	Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity (PubMed:14560022, PubMed:21931631). Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization (PubMed:14560022, PubMed:21931631). Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1 (PubMed:14560022, PubMed:21931631). Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B (PubMed:14560022, PubMed:21931631). Participates in IFNB promoter activation via TICAM1 (PubMed:15611223). {ECO:0000269\|PubMed:14560022, ECO:0000269\|PubMed:15611223, ECO:0000269\|PubMed:21931631}.
Q9HCM3	KIAA1549	S1913	ochoa	UPF0606 protein KIAA1549	May play a role in photoreceptor function. {ECO:0000269\|PubMed:30120214}.
Q9NPG3	UBN1	S724	ochoa	Ubinuclein-1 (HIRA-binding protein) (Protein VT4) (Ubiquitously expressed nuclear protein)	Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly. {ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:19029251}.
Q9NRA8	EIF4ENIF1	S742	ochoa	Eukaryotic translation initiation factor 4E transporter (4E-T) (eIF4E transporter) (Eukaryotic translation initiation factor 4E nuclear import factor 1)	EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (PubMed:24335285, PubMed:32354837). Acts as a binding platform for multiple RNA-binding proteins: promotes deadenylation of mRNAs via its interaction with the CCR4-NOT complex, and blocks decapping via interaction with eIF4E (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs from degradation (PubMed:27342281, PubMed:32354837). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). Promotes miRNA-mediated translational repression (PubMed:24335285, PubMed:27342281, PubMed:28487484). Required for the formation of P-bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281, PubMed:32354837). Involved in mRNA translational repression mediated by the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from decapping and subsequent decay (PubMed:32354837). Also acts as a nucleoplasmic shuttling protein, which mediates the nuclear import of EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257, PubMed:28216671). {ECO:0000250\|UniProtKB:Q9EST3, ECO:0000269\|PubMed:10856257, ECO:0000269\|PubMed:16157702, ECO:0000269\|PubMed:22966201, ECO:0000269\|PubMed:24335285, ECO:0000269\|PubMed:27342281, ECO:0000269\|PubMed:28216671, ECO:0000269\|PubMed:28487484, ECO:0000269\|PubMed:32354837}.
Q9NRH2	SNRK	S599	ochoa	SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase)	May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis. {ECO:0000250\|UniProtKB:Q63553, ECO:0000269\|PubMed:12234663, ECO:0000269\|PubMed:15733851}.
Q9NXR1	NDE1	S214	ochoa	Nuclear distribution protein nudE homolog 1 (NudE)	Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a postmitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. Acts as a RAB9A/B effector that tethers RAB9-associated late endosomes to the dynein motor for their retrograde transport to the trans-Golgi network (PubMed:34793709). {ECO:0000269\|PubMed:17600710, ECO:0000269\|PubMed:21529752, ECO:0000269\|PubMed:34793709}.
Q9NZJ0	DTL	S462	ochoa	Denticleless protein homolog (DDB1- and CUL4-associated factor 2) (Lethal(2) denticleless protein homolog) (Retinoic acid-regulated nuclear matrix-associated protein)	Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). {ECO:0000269\|PubMed:16861906, ECO:0000269\|PubMed:16949367, ECO:0000269\|PubMed:16964240, ECO:0000269\|PubMed:17085480, ECO:0000269\|PubMed:18703516, ECO:0000269\|PubMed:18794347, ECO:0000269\|PubMed:18794348, ECO:0000269\|PubMed:19332548, ECO:0000269\|PubMed:20129063, ECO:0000269\|PubMed:23478441, ECO:0000269\|PubMed:23478445, ECO:0000269\|PubMed:23677613, ECO:0000269\|PubMed:26431207, ECO:0000269\|PubMed:27906959}.
Q9NZN8	CNOT2	S159	ochoa	CCR4-NOT transcription complex subunit 2 (CCR4-associated factor 2)	Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of embryonic stem (ES) cell identity. {ECO:0000269\|PubMed:14707134, ECO:0000269\|PubMed:16712523, ECO:0000269\|PubMed:21299754, ECO:0000269\|PubMed:22367759}.
Q9UBY5	LPAR3	S325	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.
Q9UKG1	APPL1	S393	ochoa	DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)	Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism (PubMed:10490823, PubMed:15016378, PubMed:19661063, PubMed:26073777, PubMed:26583432). Regulates signaling pathway leading to cell proliferation through interaction with RAB5A and subunits of the NuRD/MeCP1 complex (PubMed:15016378). Functions as a positive regulator of innate immune response via activation of AKT1 signaling pathway by forming a complex with APPL1 and PIK3R1 (By similarity). Inhibits Fc-gamma receptor-mediated phagocytosis through PI3K/Akt signaling in macrophages (By similarity). Regulates TLR4 signaling in activated macrophages (By similarity). Involved in trafficking of the TGFBR1 from the endosomes to the nucleus via microtubules in a TRAF6-dependent manner (PubMed:26583432). Plays a role in cell metabolism by regulating adiponecting and insulin signaling pathways (PubMed:19661063, PubMed:24879834, PubMed:26073777). Required for fibroblast migration through HGF cell signaling (By similarity). Positive regulator of beta-catenin/TCF-dependent transcription through direct interaction with RUVBL2/reptin resulting in the relief of RUVBL2-mediated repression of beta-catenin/TCF target genes by modulating the interactions within the beta-catenin-reptin-HDAC complex (PubMed:19433865). {ECO:0000250\|UniProtKB:Q8K3H0, ECO:0000269\|PubMed:10490823, ECO:0000269\|PubMed:15016378, ECO:0000269\|PubMed:19433865, ECO:0000269\|PubMed:19661063, ECO:0000269\|PubMed:24879834, ECO:0000269\|PubMed:26073777, ECO:0000269\|PubMed:26583432}.
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}.
Q9ULT8	HECTD1	S1510	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}.
Q9UPN3	MACF1	S7226	psp	Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)	[Isoform 2]: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity). As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity). {ECO:0000250\|UniProtKB:Q9QXZ0, ECO:0000269\|PubMed:15265687, ECO:0000269\|PubMed:20937854, ECO:0000269\|PubMed:27693509}.
Q9UPQ0	LIMCH1	S225	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}.
Q9Y2L5	TRAPPC8	S269	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}.
Q9Y2X7	GIT1	S571	ochoa	ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1)	GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250\|UniProtKB:Q68FF6, ECO:0000250\|UniProtKB:Q9Z272, ECO:0000269\|PubMed:10938112, ECO:0000269\|PubMed:11896197, ECO:0000269\|PubMed:12695502, ECO:0000269\|PubMed:15800193, ECO:0000269\|PubMed:15923189, ECO:0000269\|PubMed:19273721, ECO:0000269\|PubMed:23108400, ECO:0000269\|PubMed:25284783, ECO:0000269\|PubMed:27012601, ECO:0000269\|PubMed:31502302}.
Q9Y3P9	RABGAP1	S491	ochoa	Rab GTPase-activating protein 1 (GAP and centrosome-associated protein) (Rab6 GTPase-activating protein GAPCenA)	May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition. {ECO:0000269\|PubMed:10202141, ECO:0000269\|PubMed:16395330}.
Q9Y3R5	DOP1B	S586	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
P07900	HSP90AA1	S460	Sugiyama	Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269\|PubMed:11274138, ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:12526792, ECO:0000269\|PubMed:15577939, ECO:0000269\|PubMed:15937123, ECO:0000269\|PubMed:20628368, ECO:0000269\|PubMed:24613385, ECO:0000269\|PubMed:25609812, ECO:0000269\|PubMed:27353360, ECO:0000269\|PubMed:29127155, ECO:0000303\|PubMed:25973397, ECO:0000303\|PubMed:26991466, ECO:0000303\|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305\|PubMed:22066472}.
O15075	DCLK1	S164	Sugiyama	Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Doublecortin domain-containing protein 3A) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.
P24046	GABRR1	S434	SIGNOR	Gamma-aminobutyric acid receptor subunit rho-1 (GABA(A) receptor subunit rho-1) (GABAAR subunit rho-1) (GABA(C) receptor)	Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain (PubMed:37659407). Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (PubMed:37659407). When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:37659407). Rho-1 subunits are primarily expressed in retina where rho-1-containing GABAARs may play a role in retinal neurotransmission (PubMed:1849271). Rho-1 GABAARs are also involved in neuronal tonic (extrasynaptic) and phasic (synaptic) transmission in the Purkinje neurons of the cerebellum (By similarity). Rho-1 GABAARs may also contribute to the regulation of glial development in the cerebellum by controlling extrasynaptic transmission (By similarity). {ECO:0000250\|UniProtKB:P56475, ECO:0000269\|PubMed:1849271, ECO:0000269\|PubMed:37659407}.
Q07157	TJP1	S1188	Sugiyama	Tight junction protein 1 (Tight junction protein ZO-1) (Zona occludens protein 1) (Zonula occludens protein 1)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity). {ECO:0000250\|UniProtKB:O97758, ECO:0000250\|UniProtKB:P39447, ECO:0000269\|PubMed:20930113, ECO:0000269\|PubMed:21240187}.
P36894	BMPR1A	S205	Sugiyama	Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292)	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. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6. May promote the expression of HAMP, potentially via its interaction with BMP2 (By similarity). {ECO:0000250\|UniProtKB:P36895}.
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}.
Q5T4S7	UBR4	S1723	Sugiyama	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}.
Q04637	EIF4G1	S1134	Sugiyama	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}.
Q9H0H5	RACGAP1	S144	SIGNOR\|iPTMNet	Rac GTPase-activating protein 1 (Male germ cell RacGap) (MgcRacGAP) (Protein CYK4 homolog) (CYK4) (HsCYK-4)	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which regulates cleavage furrow ingression and abscission during cytokinesis (PubMed:18511905). Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity (PubMed:10979956). Has a critical role in erythropoiesis (PubMed:34818416). Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269\|PubMed:10979956, ECO:0000269\|PubMed:11085985, ECO:0000269\|PubMed:11278976, ECO:0000269\|PubMed:11782313, ECO:0000269\|PubMed:14729465, ECO:0000269\|PubMed:15642749, ECO:0000269\|PubMed:16103226, ECO:0000269\|PubMed:16129829, ECO:0000269\|PubMed:16236794, ECO:0000269\|PubMed:18511905, ECO:0000269\|PubMed:19468300, ECO:0000269\|PubMed:19468302, ECO:0000269\|PubMed:23235882, ECO:0000269\|PubMed:9497316}.
Q86V48	LUZP1	S794	Sugiyama	Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin)	F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250\|UniProtKB:Q8R4U7, ECO:0000269\|PubMed:30990684, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:38009294, ECO:0000269\|PubMed:38832964}.
Q9NRM7	LATS2	S829	Sugiyama	Serine/threonine-protein kinase LATS2 (EC 2.7.11.1) (Kinase phosphorylated during mitosis protein) (Large tumor suppressor homolog 2) (Serine/threonine-protein kinase kpm) (Warts-like kinase)	Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:18158288, PubMed:26437443, PubMed:26598551, PubMed:34404733). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:26437443, PubMed:26598551, PubMed:34404733). Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:26598551, PubMed:34404733). Also phosphorylates YAP1 in response to cell contact inhibition-driven WWP1 ubiquitination of AMOTL2, which results in LATS2 activation (PubMed:34404733). Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability (PubMed:10871863). Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity (PubMed:12853976). Negative regulator of the androgen receptor (PubMed:15131260). Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities (PubMed:21952048). This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ (PubMed:21952048). Acts as an activator of the NLRP3 inflammasome by mediating phosphorylation of 'Ser-265' of NLRP3 following NLRP3 palmitoylation, promoting NLRP3 activation by NEK7 (PubMed:39173637). {ECO:0000269\|PubMed:10871863, ECO:0000269\|PubMed:12853976, ECO:0000269\|PubMed:15131260, ECO:0000269\|PubMed:18158288, ECO:0000269\|PubMed:21952048, ECO:0000269\|PubMed:26437443, ECO:0000269\|PubMed:26598551, ECO:0000269\|PubMed:34404733, ECO:0000269\|PubMed:39173637}.
A0A0C4DFX4	None	S244	ochoa	Snf2 related CREBBP activator protein	None
H0YJW9	None	T58	ochoa	Uncharacterized protein	None
O00571	DDX3X	S24	ochoa	ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (CAP-Rf) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (DBX) (Helicase-like protein 2) (HLP2)	Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation (PubMed:23478265). Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity (By similarity). Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (By similarity). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250\|UniProtKB:Q62167, ECO:0000269\|PubMed:16818630, ECO:0000269\|PubMed:17095540, ECO:0000269\|PubMed:17357160, ECO:0000269\|PubMed:17667941, ECO:0000269\|PubMed:18264132, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18628297, ECO:0000269\|PubMed:18636090, ECO:0000269\|PubMed:18846110, ECO:0000269\|PubMed:19913487, ECO:0000269\|PubMed:20127681, ECO:0000269\|PubMed:20837705, ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:21730191, ECO:0000269\|PubMed:21883093, ECO:0000269\|PubMed:22323517, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:23413191, ECO:0000269\|PubMed:23478265, ECO:0000269\|PubMed:27736973, ECO:0000269\|PubMed:27980081, ECO:0000269\|PubMed:28128295, ECO:0000269\|PubMed:28842590, ECO:0000269\|PubMed:29062139, ECO:0000269\|PubMed:29222110, ECO:0000269\|PubMed:30256975, ECO:0000269\|PubMed:30341167, ECO:0000269\|PubMed:31575075, ECO:0000269\|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269\|PubMed:21170385, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269\|PubMed:15507209, ECO:0000269\|PubMed:18583960, ECO:0000269\|PubMed:21589879, ECO:0000269\|PubMed:22872150, ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269\|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269\|PubMed:27105836}.
O14523	C2CD2L	S492	ochoa	Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (C2CD2-like) (Transmembrane protein 24)	Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (PubMed:28209843). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (PubMed:28209843). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (PubMed:28209843). Positively regulates insulin secretion in response to glucose: phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (PubMed:28209843). {ECO:0000269\|PubMed:28209843}.
O14920	IKBKB	S672	ochoa	Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697). {ECO:0000250\|UniProtKB:O88351, ECO:0000269\|PubMed:11297557, ECO:0000269\|PubMed:14673179, ECO:0000269\|PubMed:15084260, ECO:0000269\|PubMed:17213322, ECO:0000269\|PubMed:19716809, ECO:0000269\|PubMed:20410276, ECO:0000269\|PubMed:20434986, ECO:0000269\|PubMed:20797629, ECO:0000269\|PubMed:21138416, ECO:0000269\|PubMed:25326418, ECO:0000269\|PubMed:30337470, ECO:0000269\|PubMed:32209697, ECO:0000269\|PubMed:38621137, ECO:0000269\|PubMed:9346484}.
O15164	TRIM24	T761	ochoa	Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)	Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. During the DNA damage response, participates in an autoregulatory feedback loop with TP53. Early in response to DNA damage, ATM kinase phosphorylates TRIM24 leading to its ubiquitination and degradation. After sufficient DNA repair has occurred, TP53 activates TRIM24 transcription, ultimately leading to TRIM24-mediated TP53 ubiquitination and degradation (PubMed:24820418). Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). Also participates in innate immunity by mediating the specific 'Lys-63'-linked ubiquitination of TRAF3 leading to activation of downstream signal transduction of the type I IFN pathway (PubMed:32324863). Additionally, negatively regulates NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration probably by ubiquitinating NLRP3 (PubMed:33724611). {ECO:0000250, ECO:0000269\|PubMed:16322096, ECO:0000269\|PubMed:19556538, ECO:0000269\|PubMed:21164480, ECO:0000269\|PubMed:24820418, ECO:0000269\|PubMed:32324863, ECO:0000269\|PubMed:33724611}.
O15265	ATXN7	S206	ochoa	Ataxin-7 (Spinocerebellar ataxia type 7 protein)	Acts as a component of the SAGA (aka STAGA) transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of SAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Probably involved in tethering the deubiquitination module within the SAGA complex (PubMed:24493646). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). Involved in neurodegeneration (PubMed:9288099). {ECO:0000269\|PubMed:15932940, ECO:0000269\|PubMed:18206972, ECO:0000269\|PubMed:22100762, ECO:0000269\|PubMed:24493646, ECO:0000269\|PubMed:9288099}.
O15534	PER1	S1030	ochoa	Period circadian protein homolog 1 (hPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)	Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK\|NPAS2-BMAL1\|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/BMAL1 target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by BMAL1:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. {ECO:0000269\|PubMed:24005054}.
O60242	ADGRB3	S1410	ochoa	Adhesion G protein-coupled receptor B3 (Brain-specific angiogenesis inhibitor 3)	Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (By similarity). Promotes myoblast fusion through ELMO/DOCK1 (PubMed:24567399). {ECO:0000250\|UniProtKB:Q80ZF8, ECO:0000269\|PubMed:24567399}.
O60307	MAST3	S1094	ochoa	Microtubule-associated serine/threonine-protein kinase 3 (EC 2.7.11.1)	None
O60664	PLIN3	S127	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}.
O75582	RPS6KA5	S750	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}.
O75995	SASH3	S27	ochoa\|psp	SAM and SH3 domain-containing protein 3 (SH3 protein expressed in lymphocytes homolog)	May function as a signaling adapter protein in lymphocytes. {ECO:0000250\|UniProtKB:Q8K352}.
O94915	FRYL	S1475	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}.
O95049	TJP3	Y361	ochoa	Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3)	TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250\|UniProtKB:O62683, ECO:0000250\|UniProtKB:Q9QXY1, ECO:0000269\|PubMed:16129888, ECO:0000269\|PubMed:21411630}.
P08172	CHRM2	S283	psp	Muscarinic acetylcholine receptor M2	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269\|PubMed:24256733, ECO:0000269\|PubMed:3443095}.
P08581	MET	S990	ochoa	Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (By similarity). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity). {ECO:0000250\|UniProtKB:P16056}.; FUNCTION: (Microbial infection) Acts as a receptor for Listeria monocytogenes internalin InlB, mediating entry of the pathogen into cells. {ECO:0000269\|PubMed:11081636, ECO:0000305\|PubMed:17662939, ECO:0000305\|PubMed:19900460}.
P08651	NFIC	S276	ochoa	Nuclear factor 1 C-type (NF1-C) (Nuclear factor 1/C) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/C) (NF-I/C) (NFI-C) (TGGCA-binding protein)	Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
P11362	FGFR1	S779	psp	Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)	Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation. {ECO:0000250\|UniProtKB:P16092, ECO:0000269\|PubMed:10830168, ECO:0000269\|PubMed:11353842, ECO:0000269\|PubMed:12181353, ECO:0000269\|PubMed:1379697, ECO:0000269\|PubMed:1379698, ECO:0000269\|PubMed:15117958, ECO:0000269\|PubMed:16597617, ECO:0000269\|PubMed:17311277, ECO:0000269\|PubMed:17623664, ECO:0000269\|PubMed:18480409, ECO:0000269\|PubMed:19224897, ECO:0000269\|PubMed:19261810, ECO:0000269\|PubMed:19665973, ECO:0000269\|PubMed:20133753, ECO:0000269\|PubMed:20139426, ECO:0000269\|PubMed:21765395, ECO:0000269\|PubMed:8622701, ECO:0000269\|PubMed:8663044}.
P17812	CTPS1	S568	ochoa	CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1)	This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000269\|PubMed:16179339, ECO:0000269\|PubMed:24870241}.
P17936	IGFBP3	S194	psp	Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3)	Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including proliferation, differentiation, and apoptosis in a cell-type specific manner (PubMed:10874028, PubMed:19556345). Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R (PubMed:20353938). Inhibits the positive effect of humanin on insulin sensitivity (PubMed:19623253). Promotes testicular germ cell apoptosis (PubMed:19952275). Acts via LRP-1/alpha2M receptor, also known as TGF-beta type V receptor, to mediate cell growth inhibition independent of IGF1 (PubMed:9252371). Mechanistically, induces serine-specific dephosphorylation of IRS1 or IRS2 upon ligation to its receptor, leading to the inhibitory cascade (PubMed:15371331). In the nucleus, interacts with transcription factors such as retinoid X receptor-alpha/RXRA to regulate transcriptional signaling and apoptosis (PubMed:10874028). {ECO:0000269\|PubMed:10874028, ECO:0000269\|PubMed:15371331, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19556345, ECO:0000269\|PubMed:19623253, ECO:0000269\|PubMed:19952275, ECO:0000269\|PubMed:20353938}.
P18583	SON	S1773	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}.
P19484	TFEB	S452	ochoa	Transcription factor EB (Class E basic helix-loop-helix protein 35) (bHLHe35)	Transcription factor that acts as a master regulator of lysosomal biogenesis, autophagy, lysosomal exocytosis, lipid catabolism, energy metabolism and immune response (PubMed:21617040, PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:30120233, PubMed:31672913, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823, PubMed:36749723, PubMed:37079666). Specifically recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF (PubMed:1748288, PubMed:19556463, PubMed:29146937). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, TFEB phosphorylation by MTOR promotes its cytosolic retention and subsequent inactivation (PubMed:21617040, PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823). Upon starvation or lysosomal stress, inhibition of MTOR induces TFEB dephosphorylation, resulting in nuclear localization and transcription factor activity (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823). Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression, thereby playing a central role in expression of lysosomal genes (PubMed:19556463, PubMed:22692423). Regulates lysosomal positioning in response to nutrient deprivation by promoting the expression of PIP4P1 (PubMed:29146937). Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy (PubMed:21617040, PubMed:22576015, PubMed:23434374, PubMed:27278822). In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity (By similarity). Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer (PubMed:2115126). Plays a role in the signal transduction processes required for normal vascularization of the placenta (By similarity). Involved in the immune response to infection by the bacteria S.aureus, S.typhimurium or S.enterica: infection promotes itaconate production, leading to alkylation, resulting in nuclear localization and transcription factor activity (PubMed:35662396). Itaconate-mediated alkylation activates TFEB-dependent lysosomal biogenesis, facilitating the bacteria clearance during the antibacterial innate immune response (PubMed:35662396). In association with ACSS2, promotes the expression of genes involved in lysosome biogenesis and both autophagy upon glucose deprivation (PubMed:28552616). {ECO:0000250\|UniProtKB:Q9R210, ECO:0000269\|PubMed:1748288, ECO:0000269\|PubMed:19556463, ECO:0000269\|PubMed:2115126, ECO:0000269\|PubMed:21617040, ECO:0000269\|PubMed:22343943, ECO:0000269\|PubMed:22576015, ECO:0000269\|PubMed:22692423, ECO:0000269\|PubMed:23434374, ECO:0000269\|PubMed:25720963, ECO:0000269\|PubMed:27278822, ECO:0000269\|PubMed:28552616, ECO:0000269\|PubMed:29146937, ECO:0000269\|PubMed:30120233, ECO:0000269\|PubMed:31672913, ECO:0000269\|PubMed:32612235, ECO:0000269\|PubMed:32753672, ECO:0000269\|PubMed:35662396, ECO:0000269\|PubMed:36697823, ECO:0000269\|PubMed:36749723, ECO:0000269\|PubMed:37079666}.
P19532	TFE3	S553	ochoa	Transcription factor E3 (Class E basic helix-loop-helix protein 33) (bHLHe33)	Transcription factor that acts as a master regulator of lysosomal biogenesis and immune response (PubMed:2338243, PubMed:24448649, PubMed:29146937, PubMed:30733432, PubMed:31672913, PubMed:37079666). Specifically recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF (PubMed:24448649). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, TFE3 phosphorylation by MTOR promotes its inactivation (PubMed:24448649, PubMed:31672913, PubMed:36608670). Upon starvation or lysosomal stress, inhibition of MTOR induces TFE3 dephosphorylation, resulting in transcription factor activity (PubMed:24448649, PubMed:31672913, PubMed:36608670). Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression, thereby playing a central role in expression of lysosomal genes (PubMed:24448649). Maintains the pluripotent state of embryonic stem cells by promoting the expression of genes such as ESRRB; mTOR-dependent TFE3 cytosolic retention and inactivation promotes exit from pluripotency (By similarity). Required to maintain the naive pluripotent state of hematopoietic stem cell; mTOR-dependent cytoplasmic retention of TFE3 promotes the exit of hematopoietic stem cell from pluripotency (PubMed:30733432). TFE3 activity is also involved in the inhibition of neuronal progenitor differentiation (By similarity). Acts as a positive regulator of browning of adipose tissue by promoting expression of target genes; mTOR-dependent phosphorylation promotes cytoplasmic retention of TFE3 and inhibits browning of adipose tissue (By similarity). In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity (By similarity). Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer (PubMed:2338243). It also binds very well to a USF/MLTF site (PubMed:2338243). Promotes TGF-beta-induced transcription of COL1A2; via its interaction with TSC22D1 at E-boxes in the gene proximal promoter (By similarity). May regulate lysosomal positioning in response to nutrient deprivation by promoting the expression of PIP4P1 (PubMed:29146937). {ECO:0000250\|UniProtKB:Q64092, ECO:0000269\|PubMed:2338243, ECO:0000269\|PubMed:24448649, ECO:0000269\|PubMed:29146937, ECO:0000269\|PubMed:30733432, ECO:0000269\|PubMed:31672913, ECO:0000269\|PubMed:36608670, ECO:0000269\|PubMed:37079666}.
P25116	F2R	S392	psp	Proteinase-activated receptor 1 (PAR-1) (Coagulation factor II receptor) (Thrombin receptor)	High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores (PubMed:1672265, PubMed:8136362). The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores (By similarity). In astrocytes, the calcium released into the cytosol allows the Ca(2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). May play a role in platelets activation and in vascular development (PubMed:10079109). Mediates up-regulation of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, triggered by coagulation factor Xa (F10) in cardiac fibroblasts and umbilical vein endothelial cells (PubMed:30568593, PubMed:34831181). {ECO:0000250\|UniProtKB:P26824, ECO:0000250\|UniProtKB:P30558, ECO:0000269\|PubMed:10079109, ECO:0000269\|PubMed:1672265, ECO:0000269\|PubMed:30568593, ECO:0000269\|PubMed:34831181, ECO:0000269\|PubMed:8136362}.
P29474	NOS3	S624	ochoa	Nitric oxide synthase 3 (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (NOS type III) (NOSIII) (Nitric oxide synthase, endothelial) (Endothelial NOS) (eNOS)	Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway (PubMed:1378832). NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. {ECO:0000269\|PubMed:1378832}.; FUNCTION: [Isoform eNOS13C]: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.
P49792	RANBP2	S1107	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}.
P50454	SERPINH1	S132	ochoa	Serpin H1 (47 kDa heat shock protein) (Arsenic-transactivated protein 3) (AsTP3) (Cell proliferation-inducing gene 14 protein) (Collagen-binding protein) (Colligin) (Rheumatoid arthritis-related antigen RA-A47)	Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
P50851	LRBA	S1052	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}.
P52179	MYOM1	S58	ochoa	Myomesin-1 (190 kDa connectin-associated protein) (190 kDa titin-associated protein) (Myomesin family member 1)	Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.
P53814	SMTN	T372	ochoa	Smoothelin	Structural protein of the cytoskeleton.
P56945	BCAR1	S430	ochoa	Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (PubMed:12432078, PubMed:12832404). Implicated in induction of cell migration and cell branching (PubMed:12432078, PubMed:12832404, PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). {ECO:0000250\|UniProtKB:Q61140, ECO:0000269\|PubMed:12432078, ECO:0000269\|PubMed:12832404, ECO:0000269\|PubMed:17038317}.
P61764	STXBP1	S506	ochoa	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}.
Q00341	HDLBP	S1237	ochoa	Vigilin (High density lipoprotein-binding protein) (HDL-binding protein)	Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.
Q00587	CDC42EP1	S143	ochoa	Cdc42 effector protein 1 (Binder of Rho GTPases 5) (Serum protein MSE55)	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269\|PubMed:10430899}.
Q01974	ROR2	S861	ochoa	Tyrosine-protein kinase transmembrane receptor ROR2 (EC 2.7.10.1) (Neurotrophic tyrosine kinase, receptor-related 2)	Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation (PubMed:17717073). In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443). {ECO:0000250\|UniProtKB:Q9Z138, ECO:0000269\|PubMed:17717073, ECO:0000269\|PubMed:25029443}.
Q02880	TOP2B	S1454	ochoa	DNA topoisomerase 2-beta (EC 5.6.2.2) (DNA topoisomerase II, beta isozyme)	Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation. {ECO:0000269\|PubMed:10684600, ECO:0000269\|PubMed:31409799, ECO:0000269\|PubMed:32128574}.
Q08174	PCDH1	S1011	ochoa	Protocadherin-1 (Cadherin-like protein 1) (Protocadherin-42) (PC42)	May be involved in cell-cell interaction processes and in cell adhesion.
Q12888	TP53BP1	S523	ochoa\|psp	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}.
Q13163	MAP2K5	S132	ochoa	Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)	Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis. As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). {ECO:0000250\|UniProtKB:Q62862, ECO:0000269\|PubMed:7759517, ECO:0000269\|PubMed:9384584}.
Q13439	GOLGA4	S30	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}.
Q13523	PRP4K	S562	ochoa	Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 kinase) (PRP4 pre-mRNA-processing factor 4 homolog)	Serine/threonine kinase involved in spliceosomal assembly as well as mitosis and signaling regulation (PubMed:10799319, PubMed:12077342, PubMed:17513757, PubMed:17998396). Connects chromatin mediated regulation of transcription and pre-mRNA splicing (PubMed:12077342). During spliceosomal assembly, interacts with and phosphorylates PRPF6 and PRPF31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), to facilitate the formation of the spliceosome B complex. Plays a role in regulating transcription and the spindle assembly checkpoint (SAC) (PubMed:20118938). Associates with U5 snRNP and NCOR1 deacetylase complexes which may allow a coordination of pre-mRNA splicing with chromatin remodeling events involved in transcriptional regulation (PubMed:12077342). Associates and probably phosphorylates SMARCA4 and NCOR1 (PubMed:12077342). Phosphorylates SRSF1 (PubMed:11418604). Associates with kinetochores during mitosis and is necessary for recruitment and maintenance of the checkpoint proteins such as MAD1L1 and MAD12L1 at the kinetochores (PubMed:17998396). Phosphorylates and regulates the activity of the transcription factors such as ELK1 and KLF13 (PubMed:10799319, PubMed:17513757). Phosphorylates nuclear YAP1 and WWTR1/TAZ which induces nuclear exclusion and regulates Hippo signaling pathway, involved in tissue growth control (PubMed:29695716). {ECO:0000269\|PubMed:10799319, ECO:0000269\|PubMed:11418604, ECO:0000269\|PubMed:12077342, ECO:0000269\|PubMed:17513757, ECO:0000269\|PubMed:17998396, ECO:0000269\|PubMed:20118938, ECO:0000269\|PubMed:29695716}.
Q13950	RUNX2	S237	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}.
Q14005	IL16	S1073	ochoa	Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]	Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.; FUNCTION: [Isoform 1]: May act as a scaffolding protein that anchors ion channels in the membrane.; FUNCTION: Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Q14161	GIT2	S558	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}.
Q14289	PTK2B	S389	ochoa	Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)	Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. {ECO:0000269\|PubMed:10022920, ECO:0000269\|PubMed:12771146, ECO:0000269\|PubMed:12893833, ECO:0000269\|PubMed:14585963, ECO:0000269\|PubMed:15050747, ECO:0000269\|PubMed:15166227, ECO:0000269\|PubMed:17634955, ECO:0000269\|PubMed:18086875, ECO:0000269\|PubMed:18339875, ECO:0000269\|PubMed:18587400, ECO:0000269\|PubMed:18765415, ECO:0000269\|PubMed:19086031, ECO:0000269\|PubMed:19207108, ECO:0000269\|PubMed:19244237, ECO:0000269\|PubMed:19428251, ECO:0000269\|PubMed:19648005, ECO:0000269\|PubMed:19880522, ECO:0000269\|PubMed:20001213, ECO:0000269\|PubMed:20381867, ECO:0000269\|PubMed:20521079, ECO:0000269\|PubMed:21357692, ECO:0000269\|PubMed:21533080, ECO:0000269\|PubMed:7544443, ECO:0000269\|PubMed:8670418, ECO:0000269\|PubMed:8849729}.
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}.
Q15942	ZYX	S143	ochoa	Zyxin (Zyxin-2)	Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). {ECO:0000250}.
Q2KHR3	QSER1	S488	ochoa	Glutamine and serine-rich protein 1	Plays an essential role in the protection and maintenance of transcriptional and developmental programs. Protects many bivalent promoters and poised enhancers from hypermethylation, showing a marked preference for these regulatory elements over other types of promoters or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in a common complex to inhibit the binding of DNMT3A/3B and therefore de novo methylation. {ECO:0000269\|PubMed:33833093}.
Q4V328	GRIPAP1	S681	ochoa	GRIP1-associated protein 1 (GRASP-1) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)]	Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity). {ECO:0000250\|UniProtKB:Q9JHZ4}.; FUNCTION: [GRASP-1 C-terminal chain]: Functions as a scaffold protein to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity. {ECO:0000269\|PubMed:17761173}.
Q5HYJ3	FAM76B	S224	ochoa	Protein FAM76B	Negatively regulates the NF-kappa-B-mediated inflammatory pathway by preventing the translocation of HNRNPA2B1 from the nucleus to the cytoplasm (PubMed:37643469). Inhibits the PI3K/Akt/NF-kappa-B pathway-mediated polarization of M1 macrophages by binding to and stabilizing PIK3CD mRNA, resulting in increased levels of PIK3CD protein and increased levels of phosphorylated downstream target AKT which leads to decreased NF-kappa-B signaling (PubMed:38421448). {ECO:0000269\|PubMed:37643469, ECO:0000269\|PubMed:38421448}.
Q5JSZ5	PRRC2B	S1224	ochoa	Protein PRRC2B (HLA-B-associated transcript 2-like 1) (Proline-rich coiled-coil protein 2B)	None
Q5JTV8	TOR1AIP1	S254	ochoa	Torsin-1A-interacting protein 1 (Lamin-associated protein 1B) (LAP1B)	Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269\|PubMed:23569223}.
Q5SW79	CEP170	Y923	ochoa	Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein)	Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269\|PubMed:15616186, ECO:0000269\|PubMed:28422092}.
Q5SW79	CEP170	S1270	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}.
Q5T1M5	FKBP15	S1155	ochoa	FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL)	May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269\|PubMed:19121306}.
Q5T4S7	UBR4	S2885	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}.
Q5VUA4	ZNF318	S1613	ochoa	Zinc finger protein 318 (Endocrine regulatory protein)	[Isoform 2]: Acts as a transcriptional corepressor for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.; FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. {ECO:0000250\|UniProtKB:Q99PP2}.
Q6AI08	HEATR6	S390	ochoa	HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1)	Amplification-dependent oncogene.
Q6P1L5	FAM117B	S407	ochoa	Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein)	None
Q6P6C2	ALKBH5	S364	ochoa	RNA demethylase ALKBH5 (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 5) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5)	Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178, PubMed:34048572, PubMed:36944332, PubMed:37257451, PubMed:37369679). Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178). Demethylation of m6A mRNA affects mRNA processing, translation and export (PubMed:23177736, PubMed:34048572, PubMed:36944332, PubMed:37257451). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity). Involved in paraspeckle assembly, a nuclear membraneless organelle, by undergoing liquid-liquid phase separation (PubMed:37369679, PubMed:37474102). Paraspeckle assembly is coupled with m6A demethylation of RNAs, such as NEAT1 non-coding RNA (PubMed:37474102). Also acts as a negative regulator of T-cell development: inhibits gamma-delta T-cell proliferation via demethylation of JAG1 and NOTCH2 transcripts (By similarity). Inhibits regulatory T-cell (Treg) recruitment by mediating demethylation and destabilization of CCL28 mRNAs (By similarity). {ECO:0000250\|UniProtKB:Q3TSG4, ECO:0000269\|PubMed:21264265, ECO:0000269\|PubMed:23177736, ECO:0000269\|PubMed:24489119, ECO:0000269\|PubMed:24616105, ECO:0000269\|PubMed:24778178, ECO:0000269\|PubMed:34048572, ECO:0000269\|PubMed:36944332, ECO:0000269\|PubMed:37257451, ECO:0000269\|PubMed:37369679, ECO:0000269\|PubMed:37474102}.
Q6R327	RICTOR	S1210	ochoa	Rapamycin-insensitive companion of mTOR (AVO3 homolog) (hAVO3)	Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). {ECO:0000250\|UniProtKB:Q6QI06, ECO:0000269\|PubMed:15268862, ECO:0000269\|PubMed:15467718, ECO:0000269\|PubMed:15718470, ECO:0000269\|PubMed:19720745, ECO:0000269\|PubMed:19935711, ECO:0000269\|PubMed:19995915, ECO:0000269\|PubMed:21343617, ECO:0000269\|PubMed:33158864, ECO:0000269\|PubMed:35904232, ECO:0000269\|PubMed:35926713}.
Q6R327	RICTOR	T1224	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}.
Q6SZW1	SARM1	S704	ochoa	NAD(+) hydrolase SARM1 (NADase SARM1) (hSARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and Armadillo repeat protein) (Sterile alpha and TIR motif-containing protein 1) (Sterile alpha motif domain-containing protein 2) (MyD88-5) (SAM domain-containing protein 2) (Tir-1 homolog) (HsTIR)	NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (PubMed:25908823, PubMed:27671644, PubMed:28334607). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (PubMed:15123841, PubMed:16964262, PubMed:20306472, PubMed:25908823). Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction (PubMed:25908823, PubMed:28334607, PubMed:30333228, PubMed:31128467, PubMed:31439792, PubMed:31439793, PubMed:32049506, PubMed:32828421, PubMed:33053563). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:29395922). Can activate neuronal cell death in response to stress (PubMed:20306472). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (PubMed:16964262). {ECO:0000250\|UniProtKB:Q6PDS3, ECO:0000269\|PubMed:15123841, ECO:0000269\|PubMed:16964262, ECO:0000269\|PubMed:20306472, ECO:0000269\|PubMed:25908823, ECO:0000269\|PubMed:27671644, ECO:0000269\|PubMed:28334607, ECO:0000269\|PubMed:29395922, ECO:0000269\|PubMed:30333228, ECO:0000269\|PubMed:31128467, ECO:0000269\|PubMed:31439792, ECO:0000269\|PubMed:31439793, ECO:0000269\|PubMed:32049506, ECO:0000269\|PubMed:32828421, ECO:0000269\|PubMed:33053563}.
Q6VY07	PACS1	S486	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}.
Q6ZRS2	SRCAP	S263	ochoa	Helicase SRCAP (EC 3.6.4.-) (Domino homolog 2) (Snf2-related CBP activator)	Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269\|PubMed:10347196, ECO:0000269\|PubMed:11522779, ECO:0000269\|PubMed:14500758, ECO:0000269\|PubMed:16024792, ECO:0000269\|PubMed:16634648, ECO:0000269\|PubMed:17617668}.
Q70E73	RAPH1	S541	ochoa	Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)	Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
Q765P7	MTSS2	S257	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}.
Q76FK4	NOL8	S653	ochoa	Nucleolar protein 8 (Nucleolar protein Nop132)	Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells. {ECO:0000269\|PubMed:14660641, ECO:0000269\|PubMed:15132771, ECO:0000269\|PubMed:16963496}.
Q7L0Y3	TRMT10C	S73	ochoa	tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)	Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607, PubMed:23042678, PubMed:27132592). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit (PubMed:23042678). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA (PubMed:29072297). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. {ECO:0000269\|PubMed:18984158, ECO:0000269\|PubMed:21593607, ECO:0000269\|PubMed:23042678, ECO:0000269\|PubMed:24703694, ECO:0000269\|PubMed:27132592, ECO:0000269\|PubMed:29040705, ECO:0000269\|PubMed:29072297}.
Q7Z6B7	SRGAP1	S819	ochoa	SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13)	GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269\|PubMed:11672528}.
Q86UR5	RIMS1	S1486	ochoa	Regulating synaptic membrane exocytosis protein 1 (Rab-3-interacting molecule 1) (RIM 1) (Rab-3-interacting protein 2)	Rab effector involved in exocytosis (By similarity). May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250\|UniProtKB:Q99NE5, ECO:0000269\|PubMed:23999003}.
Q86VP3	PACS2	S330	ochoa	Phosphofurin acidic cluster sorting protein 2 (PACS-2) (PACS1-like protein)	Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269\|PubMed:15692563, ECO:0000269\|PubMed:15692567}.
Q8IUD2	ERC1	Y987	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}.
Q8IV63	VRK3	S75	ochoa	Serine/threonine-protein kinase VRK3 (EC 2.7.11.22) (Vaccinia-related kinase 3)	Plays a role in the regulation of the cell cycle by phosphorylating the nuclear envelope protein barrier-to-autointegration factor/BAF that is required for disassembly and reassembly, respectively, of the nuclear envelope during mitosis (PubMed:25899223). Under normal physiological conditions, negatively regulates ERK activity along with VHR/DUSP3 phosphatase in the nucleus, causing timely and transient action of ERK. Stress conditions activate CDK5 which phosphorylates VRK3 to increase VHR phosphatase activity and suppress prolonged ERK activation that causes cell death (PubMed:27346674). For example, upon glutamate induction, promotes nuclear localization of HSP70/HSPA1A to inhibit ERK activation via VHR/DUSP3 phosphatase (PubMed:27941812). {ECO:0000250\|UniProtKB:Q8K3G5, ECO:0000269\|PubMed:14645249, ECO:0000269\|PubMed:19141289, ECO:0000269\|PubMed:25899223, ECO:0000269\|PubMed:27346674, ECO:0000269\|PubMed:27941812}.
Q8IY63	AMOTL1	S786	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}.
Q8IZD0	SAMD14	S140	ochoa	Sterile alpha motif domain-containing protein 14 (SAM domain-containing protein 14)	None
Q8NC44	RETREG2	S337	ochoa	Reticulophagy regulator 2	Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress (PubMed:34338405). When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins (PubMed:34338405). Required for collagen quality control in a LIR motif-independent manner (By similarity). {ECO:0000250\|UniProtKB:Q6NS82, ECO:0000269\|PubMed:34338405}.
Q8NCN4	RNF169	S532	ochoa	E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169)	Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269\|PubMed:22492721, ECO:0000269\|PubMed:22733822, ECO:0000269\|PubMed:22742833, ECO:0000269\|PubMed:30104380, ECO:0000269\|PubMed:30773093}.
Q8NDF8	TENT4B	S45	ochoa	Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2)	Terminal nucleotidyltransferase that catalyzes preferentially the transfer of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation (PubMed:21788334, PubMed:30026317). Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro) (PubMed:21788334, PubMed:21855801). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1 (PubMed:28383716). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion (PubMed:18172165). Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation (PubMed:25049417). Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation (PubMed:22442037). {ECO:0000269\|PubMed:18172165, ECO:0000269\|PubMed:21788334, ECO:0000269\|PubMed:21855801, ECO:0000269\|PubMed:22442037, ECO:0000269\|PubMed:25049417, ECO:0000269\|PubMed:28383716, ECO:0000269\|PubMed:30026317}.
Q8NEM2	SHCBP1	S44	ochoa	SHC SH2 domain-binding protein 1	May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells. {ECO:0000250\|UniProtKB:Q9Z179}.
Q8NEM7	SUPT20H	S427	ochoa	Transcription factor SPT20 homolog (p38-interacting protein) (p38IP)	Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail (By similarity). Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000250, ECO:0000269\|PubMed:19893488}.
Q8NFH3	NUP43	S308	ochoa	Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) (p42)	Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269\|PubMed:17363900}.
Q8NI08	NCOA7	S172	ochoa	Nuclear receptor coactivator 7 (140 kDa estrogen receptor-associated protein) (Estrogen nuclear receptor coactivator 1)	Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269\|PubMed:11971969}.
Q8WXG6	MADD	S1192	ochoa	MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)	Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (PubMed:18559336, PubMed:20937701). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (By similarity). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (PubMed:32761064). May link TNFRSF1A with MAP kinase activation (PubMed:9115275). May be involved in the regulation of TNFA-induced apoptosis (PubMed:11577081, PubMed:32761064). {ECO:0000250\|UniProtKB:O08873, ECO:0000250\|UniProtKB:Q80U28, ECO:0000269\|PubMed:11577081, ECO:0000269\|PubMed:18559336, ECO:0000269\|PubMed:20937701, ECO:0000269\|PubMed:32761064, ECO:0000269\|PubMed:9115275}.
Q92560	BAP1	S482	ochoa	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}.
Q92997	DVL3	S197	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}.
Q96N64	PWWP2A	S577	ochoa	PWWP domain-containing protein 2A	Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260, PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation (By similarity). Essential for proper mitosis progression (PubMed:28645917). {ECO:0000250\|UniProtKB:Q69Z61, ECO:0000269\|PubMed:28645917, ECO:0000269\|PubMed:30228260, ECO:0000269\|PubMed:30327463}.
Q96QT4	TRPM7	S1351	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}.
Q96QZ7	MAGI1	S611	ochoa	Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (Atrophin-1-interacting protein 3) (AIP-3) (BAI1-associated protein 1) (BAP-1) (Membrane-associated guanylate kinase inverted 1) (MAGI-1) (Trinucleotide repeat-containing gene 19 protein) (WW domain-containing protein 3) (WWP3)	Plays a role in coupling actin fibers to cell junctions in endothelial cells, via its interaction with AMOTL2 and CDH5 (By similarity). May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:Q6RHR9}.
Q99501	GAS2L1	Y351	ochoa	GAS2-like protein 1 (GAS2-related protein on chromosome 22) (Growth arrest-specific protein 2-like 1)	Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). {ECO:0000269\|PubMed:12584248, ECO:0000269\|PubMed:24706950}.
Q9BZ95	NSD3	S561	ochoa	Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.370) (EC 2.1.1.371) (Nuclear SET domain-containing protein 3) (Protein whistle) (WHSC1-like 1 isoform 9 with methyltransferase activity to lysine) (Wolf-Hirschhorn syndrome candidate 1-like protein 1) (WHSC1-like protein 1)	Histone methyltransferase. Preferentially dimethylates 'Lys-4' and 'Lys-27' of histone H3 forming H3K4me2 and H3K27me2. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression. {ECO:0000269\|PubMed:16682010}.
Q9C0B5	ZDHHC5	S361	ochoa	Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)	Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239). {ECO:0000250\|UniProtKB:Q8VDZ4, ECO:0000269\|PubMed:21820437, ECO:0000269\|PubMed:26334723, ECO:0000269\|PubMed:29185452, ECO:0000269\|PubMed:31402609, ECO:0000269\|PubMed:31649195, ECO:0000269\|PubMed:32958780, ECO:0000269\|PubMed:34293401, ECO:0000269\|PubMed:38092000, ECO:0000269\|PubMed:38530158, ECO:0000269\|PubMed:38599239}.
Q9H4A3	WNK1	S2002	ochoa	Serine/threonine-protein kinase WNK1 (EC 2.7.11.1) (Erythrocyte 65 kDa protein) (p65) (Kinase deficient protein) (Protein kinase lysine-deficient 1) (Protein kinase with no lysine 1) (hWNK1)	Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204). {ECO:0000250\|UniProtKB:P83741, ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:10660600, ECO:0000269\|PubMed:15883153, ECO:0000269\|PubMed:16263722, ECO:0000269\|PubMed:17190791, ECO:0000269\|PubMed:19665974, ECO:0000269\|PubMed:19739668, ECO:0000269\|PubMed:21220314, ECO:0000269\|PubMed:21321328, ECO:0000269\|PubMed:22989884, ECO:0000269\|PubMed:25362046, ECO:0000269\|PubMed:25477473, ECO:0000269\|PubMed:27911840, ECO:0000269\|PubMed:29196535, ECO:0000269\|PubMed:31656913, ECO:0000269\|PubMed:33964204, ECO:0000269\|PubMed:34289367, ECO:0000269\|PubMed:36318922, ECO:0000269\|PubMed:36373794}.; FUNCTION: [Isoform 3]: Kinase-defective isoform specifically expressed in kidney, which acts as a dominant-negative regulator of the longer isoform 1 (PubMed:14645531). Does not directly inhibit WNK4 and has no direct effect on sodium and chloride ion transport (By similarity). Down-regulates sodium-chloride cotransporter activity indirectly by inhibiting isoform 1, it associates with isoform 1 and attenuates its kinase activity (By similarity). In kidney, may play an important role regulating sodium and potassium balance (By similarity). {ECO:0000250\|UniProtKB:Q9JIH7, ECO:0000269\|PubMed:14645531}.
Q9H4X1	RGCC	S72	ochoa	Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)	Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269\|PubMed:11687586, ECO:0000269\|PubMed:17146433, ECO:0000269\|PubMed:19158077, ECO:0000269\|PubMed:22163048}.
Q9H9A7	RMI1	S274	ochoa	RecQ-mediated genome instability protein 1 (BLM-associated protein of 75 kDa) (BLAP75) (FAAP75)	Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability. {ECO:0000269\|PubMed:15775963, ECO:0000269\|PubMed:16537486, ECO:0000269\|PubMed:16595695}.
Q9NRF8	CTPS2	S564	ochoa\|psp	CTP synthase 2 (EC 6.3.4.2) (CTP synthetase 2) (UTP--ammonia ligase 2)	Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. {ECO:0000269\|PubMed:10899599, ECO:0000269\|PubMed:16179339}.
Q9NYF8	BCLAF1	S753	ochoa	Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)	Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269\|PubMed:18794151}.
Q9NYP9	MIS18A	S29	ochoa	Protein Mis18-alpha (FAPP1-associated protein 1)	Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269\|PubMed:17199038}.
Q9P2Q2	FRMD4A	S950	ochoa	FERM domain-containing protein 4A	Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling (PubMed:27044754). {ECO:0000250\|UniProtKB:Q8BIE6, ECO:0000269\|PubMed:27044754}.
Q9UHB6	LIMA1	S336	ochoa	LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm)	Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity). {ECO:0000250\|UniProtKB:Q9ERG0, ECO:0000269\|PubMed:12566430, ECO:0000269\|PubMed:32496561, ECO:0000269\|PubMed:33999101}.
Q9UI08	EVL	S338	ochoa	Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
Q9UJF2	RASAL2	S634	ochoa	Ras GTPase-activating protein nGAP (RAS protein activator-like 2)	Inhibitory regulator of the Ras-cyclic AMP pathway.
Q9ULT8	HECTD1	S1520	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}.
Q9UQ26	RIMS2	S1205	ochoa	Regulating synaptic membrane exocytosis protein 2 (Rab-3-interacting molecule 2) (RIM 2) (Rab-3-interacting protein 3)	Rab effector involved in exocytosis. May act as scaffold protein. Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269\|PubMed:23999003}.
Q9UQR0	SCML2	S583	ochoa	Sex comb on midleg-like protein 2	Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity). {ECO:0000250}.
Q9Y3R5	DOP1B	S711	ochoa	Protein DOP1B	May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation. {ECO:0000269\|PubMed:30213940}.
Q9Y4F5	CEP170B	S1357	ochoa	Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B)	Plays a role in microtubule organization. {ECO:0000250\|UniProtKB:Q5SW79}.
P08195	SLC3A2	S403	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}.
Q9H501	ESF1	Y72	Sugiyama	ESF1 homolog (ABT1-associated protein)	May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity). {ECO:0000250}.

Download

reactome_id	name	p	-log10_p
R-HSA-162582	Signal Transduction	3.506970e-09	8.455
R-HSA-2980766	Nuclear Envelope Breakdown	1.740282e-07	6.759
R-HSA-111465	Apoptotic cleavage of cellular proteins	2.570014e-07	6.590
R-HSA-5663202	Diseases of signal transduction by growth factor receptors and second messengers	3.598235e-07	6.444
R-HSA-168276	NS1 Mediated Effects on Host Pathways	2.083368e-06	5.681
R-HSA-75153	Apoptotic execution phase	2.294527e-06	5.639
R-HSA-159236	Transport of Mature mRNA derived from an Intron-Containing Transcript	3.321934e-06	5.479
R-HSA-72202	Transport of Mature Transcript to Cytoplasm	3.336365e-06	5.477
R-HSA-6802952	Signaling by BRAF and RAF1 fusions	3.745184e-06	5.427
R-HSA-1169408	ISG15 antiviral mechanism	4.555619e-06	5.341
R-HSA-6802957	Oncogenic MAPK signaling	5.188872e-06	5.285
R-HSA-165159	MTOR signalling	5.066977e-06	5.295
R-HSA-5619107	Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC...	6.088404e-06	5.215
R-HSA-1855196	IP3 and IP4 transport between cytosol and nucleus	7.842214e-06	5.106
R-HSA-1855229	IP6 and IP7 transport between cytosol and nucleus	7.842214e-06	5.106
R-HSA-159231	Transport of Mature mRNA Derived from an Intronless Transcript	1.120889e-05	4.950
R-HSA-1855170	IPs transport between nucleus and cytosol	1.270698e-05	4.896
R-HSA-159227	Transport of the SLBP independent Mature mRNA	1.270698e-05	4.896
R-HSA-159234	Transport of Mature mRNAs Derived from Intronless Transcripts	1.382257e-05	4.859
R-HSA-159230	Transport of the SLBP Dependant Mature mRNA	1.599778e-05	4.796
R-HSA-170822	Regulation of Glucokinase by Glucokinase Regulatory Protein	1.599778e-05	4.796
R-HSA-180746	Nuclear import of Rev protein	2.000317e-05	4.699
R-HSA-3371556	Cellular response to heat stress	2.311444e-05	4.636
R-HSA-3301854	Nuclear Pore Complex (NPC) Disassembly	2.484870e-05	4.605
R-HSA-180910	Vpr-mediated nuclear import of PICs	3.764750e-05	4.424
R-HSA-6784531	tRNA processing in the nucleus	3.968887e-05	4.401
R-HSA-165054	Rev-mediated nuclear export of HIV RNA	4.594146e-05	4.338
R-HSA-177243	Interactions of Rev with host cellular proteins	6.732718e-05	4.172
R-HSA-176033	Interactions of Vpr with host cellular proteins	6.732718e-05	4.172
R-HSA-168271	Transport of Ribonucleoproteins into the Host Nucleus	8.089174e-05	4.092
R-HSA-6796648	TP53 Regulates Transcription of DNA Repair Genes	9.698093e-05	4.013
R-HSA-68882	Mitotic Anaphase	1.290361e-04	3.889
R-HSA-2555396	Mitotic Metaphase and Anaphase	1.381723e-04	3.860
R-HSA-6802948	Signaling by high-kinase activity BRAF mutants	1.797418e-04	3.745
R-HSA-380972	Energy dependent regulation of mTOR by LKB1-AMPK	1.874458e-04	3.727
R-HSA-68884	Mitotic Telophase/Cytokinesis	1.937559e-04	3.713
R-HSA-168333	NEP/NS2 Interacts with the Cellular Export Machinery	1.892789e-04	3.723
R-HSA-3371453	Regulation of HSF1-mediated heat shock response	1.971035e-04	3.705
R-HSA-9856651	MITF-M-dependent gene expression	1.758248e-04	3.755
R-HSA-1640170	Cell Cycle	2.197896e-04	3.658
R-HSA-168274	Export of Viral Ribonucleoproteins from Nucleus	2.216101e-04	3.654
R-HSA-2470946	Cohesin Loading onto Chromatin	2.417811e-04	3.617
R-HSA-191859	snRNP Assembly	3.705347e-04	3.431
R-HSA-194441	Metabolism of non-coding RNA	3.705347e-04	3.431
R-HSA-351906	Apoptotic cleavage of cell adhesion proteins	3.725891e-04	3.429
R-HSA-2995410	Nuclear Envelope (NE) Reassembly	4.069397e-04	3.390
R-HSA-5674135	MAP2K and MAPK activation	4.157643e-04	3.381
R-HSA-9656223	Signaling by RAF1 mutants	4.157643e-04	3.381
R-HSA-69278	Cell Cycle, Mitotic	4.428658e-04	3.354
R-HSA-68886	M Phase	4.528014e-04	3.344
R-HSA-68875	Mitotic Prophase	4.919722e-04	3.308
R-HSA-9730414	MITF-M-regulated melanocyte development	5.456751e-04	3.263
R-HSA-446353	Cell-extracellular matrix interactions	6.679688e-04	3.175
R-HSA-9612973	Autophagy	6.905906e-04	3.161
R-HSA-9825892	Regulation of MITF-M-dependent genes involved in cell cycle and proliferation	7.721359e-04	3.112
R-HSA-2468052	Establishment of Sister Chromatid Cohesion	7.865958e-04	3.104
R-HSA-6802946	Signaling by moderate kinase activity BRAF mutants	8.666845e-04	3.062
R-HSA-9649948	Signaling downstream of RAS mutants	8.666845e-04	3.062
R-HSA-6802955	Paradoxical activation of RAF signaling by kinase inactive BRAF	8.666845e-04	3.062
R-HSA-6802949	Signaling by RAS mutants	8.666845e-04	3.062
R-HSA-166208	mTORC1-mediated signalling	9.513673e-04	3.022
R-HSA-199991	Membrane Trafficking	1.005339e-03	2.998
R-HSA-5674499	Negative feedback regulation of MAPK pathway	1.021784e-03	2.991
R-HSA-163765	ChREBP activates metabolic gene expression	1.090434e-03	2.962
R-HSA-1632852	Macroautophagy	1.263081e-03	2.899
R-HSA-3700989	Transcriptional Regulation by TP53	1.372082e-03	2.863
R-HSA-2028269	Signaling by Hippo	1.406503e-03	2.852
R-HSA-9827857	Specification of primordial germ cells	1.406503e-03	2.852
R-HSA-168325	Viral Messenger RNA Synthesis	1.605520e-03	2.794
R-HSA-5578749	Transcriptional regulation by small RNAs	1.667758e-03	2.778
R-HSA-4419969	Depolymerization of the Nuclear Lamina	1.755788e-03	2.756
R-HSA-9926550	Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adh...	1.755788e-03	2.756
R-HSA-9615933	Postmitotic nuclear pore complex (NPC) reformation	2.017677e-03	2.695
R-HSA-428890	Role of ABL in ROBO-SLIT signaling	2.292362e-03	2.640
R-HSA-211000	Gene Silencing by RNA	2.541253e-03	2.595
R-HSA-9823730	Formation of definitive endoderm	2.647361e-03	2.577
R-HSA-1169410	Antiviral mechanism by IFN-stimulated genes	3.191202e-03	2.496
R-HSA-196025	Formation of annular gap junctions	3.217729e-03	2.492
R-HSA-2500257	Resolution of Sister Chromatid Cohesion	3.373218e-03	2.472
R-HSA-8856828	Clathrin-mediated endocytosis	3.571340e-03	2.447
R-HSA-9675108	Nervous system development	3.575715e-03	2.447
R-HSA-193639	p75NTR signals via NF-kB	4.034231e-03	2.394
R-HSA-9933946	Formation of the embryonic stem cell BAF (esBAF) complex	4.034231e-03	2.394
R-HSA-2995383	Initiation of Nuclear Envelope (NE) Reformation	3.841619e-03	2.415
R-HSA-72203	Processing of Capped Intron-Containing Pre-mRNA	4.217392e-03	2.375
R-HSA-9613354	Lipophagy	4.369535e-03	2.360
R-HSA-190873	Gap junction degradation	4.369535e-03	2.360
R-HSA-428543	Inactivation of CDC42 and RAC1	4.369535e-03	2.360
R-HSA-8941333	RUNX2 regulates genes involved in differentiation of myeloid cells	4.434935e-03	2.353
R-HSA-73856	RNA Polymerase II Transcription Termination	4.957683e-03	2.305
R-HSA-169893	Prolonged ERK activation events	4.991531e-03	2.302
R-HSA-4420097	VEGFA-VEGFR2 Pathway	5.258255e-03	2.279
R-HSA-9764790	Positive Regulation of CDH1 Gene Transcription	5.771006e-03	2.239
R-HSA-8875555	MET activates RAP1 and RAC1	5.771006e-03	2.239
R-HSA-5655302	Signaling by FGFR1 in disease	5.793699e-03	2.237
R-HSA-1839124	FGFR1 mutant receptor activation	5.860805e-03	2.232
R-HSA-72187	mRNA 3'-end processing	6.043598e-03	2.219
R-HSA-68877	Mitotic Prometaphase	6.743443e-03	2.171
R-HSA-9839394	TGFBR3 expression	7.363727e-03	2.133
R-HSA-3134963	DEx/H-box helicases activate type I IFN and inflammatory cytokines production	6.768937e-03	2.169
R-HSA-1474165	Reproduction	6.934642e-03	2.159
R-HSA-9705671	SARS-CoV-2 activates/modulates innate and adaptive immune responses	7.347688e-03	2.134
R-HSA-74160	Gene expression (Transcription)	7.662063e-03	2.116
R-HSA-9931510	Phosphorylated BMAL1:CLOCK (ARNTL:CLOCK) activates expression of core clock gene...	8.521884e-03	2.069
R-HSA-9613829	Chaperone Mediated Autophagy	8.813921e-03	2.055
R-HSA-209560	NF-kB is activated and signals survival	9.407828e-03	2.027
R-HSA-8935964	RUNX1 regulates expression of components of tight junctions	9.712665e-03	2.013
R-HSA-5603029	IkBA variant leads to EDA-ID	9.712665e-03	2.013
R-HSA-8940973	RUNX2 regulates osteoblast differentiation	1.122014e-02	1.950
R-HSA-422475	Axon guidance	1.147289e-02	1.940
R-HSA-194138	Signaling by VEGF	1.056789e-02	1.976
R-HSA-209543	p75NTR recruits signalling complexes	1.168109e-02	1.933
R-HSA-2467813	Separation of Sister Chromatids	1.168603e-02	1.932
R-HSA-352238	Breakdown of the nuclear lamina	1.176215e-02	1.930
R-HSA-9934037	Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF)	1.226520e-02	1.911
R-HSA-9927432	Developmental Lineage of Mammary Gland Myoepithelial Cells	1.277363e-02	1.894
R-HSA-9006934	Signaling by Receptor Tyrosine Kinases	1.326650e-02	1.877
R-HSA-2559584	Formation of Senescence-Associated Heterochromatin Foci (SAHF)	1.427959e-02	1.845
R-HSA-141444	Amplification of signal from unattached kinetochores via a MAD2 inhibitory si...	1.478286e-02	1.830
R-HSA-141424	Amplification of signal from the kinetochores	1.478286e-02	1.830
R-HSA-9013508	NOTCH3 Intracellular Domain Regulates Transcription	1.447195e-02	1.839
R-HSA-170968	Frs2-mediated activation	1.427959e-02	1.845
R-HSA-1445148	Translocation of SLC2A4 (GLUT4) to the plasma membrane	1.406030e-02	1.852
R-HSA-8953750	Transcriptional Regulation by E2F6	1.356699e-02	1.868
R-HSA-6806003	Regulation of TP53 Expression and Degradation	1.356699e-02	1.868
R-HSA-162599	Late Phase of HIV Life Cycle	1.528240e-02	1.816
R-HSA-162587	HIV Life Cycle	1.632280e-02	1.787
R-HSA-8876384	Listeria monocytogenes entry into host cells	1.653324e-02	1.782
R-HSA-3214841	PKMTs methylate histone lysines	1.670389e-02	1.777
R-HSA-2032785	YAP1- and WWTR1 (TAZ)-stimulated gene expression	1.721730e-02	1.764
R-HSA-9933939	Formation of the polybromo-BAF (pBAF) complex	1.721730e-02	1.764
R-HSA-8951430	RUNX3 regulates WNT signaling	1.753486e-02	1.756
R-HSA-4411364	Binding of TCF/LEF:CTNNB1 to target gene promoters	1.753486e-02	1.756
R-HSA-1221632	Meiotic synapsis	1.930775e-02	1.714
R-HSA-193704	p75 NTR receptor-mediated signalling	1.832289e-02	1.737
R-HSA-69618	Mitotic Spindle Checkpoint	1.948507e-02	1.710
R-HSA-9663891	Selective autophagy	1.814663e-02	1.741
R-HSA-5633007	Regulation of TP53 Activity	1.885806e-02	1.725
R-HSA-1483249	Inositol phosphate metabolism	1.930873e-02	1.714
R-HSA-70171	Glycolysis	1.948507e-02	1.710
R-HSA-9665230	Drug resistance in ERBB2 KD mutants	2.018464e-02	1.695
R-HSA-9652282	Drug-mediated inhibition of ERBB2 signaling	2.018464e-02	1.695
R-HSA-8951911	RUNX3 regulates RUNX1-mediated transcription	2.018464e-02	1.695
R-HSA-9665250	Resistance of ERBB2 KD mutants to AEE788	2.018464e-02	1.695
R-HSA-9665246	Resistance of ERBB2 KD mutants to neratinib	2.018464e-02	1.695
R-HSA-9665233	Resistance of ERBB2 KD mutants to trastuzumab	2.018464e-02	1.695
R-HSA-9665737	Drug resistance in ERBB2 TMD/JMD mutants	2.018464e-02	1.695
R-HSA-9665249	Resistance of ERBB2 KD mutants to afatinib	2.018464e-02	1.695
R-HSA-9665244	Resistance of ERBB2 KD mutants to sapitinib	2.018464e-02	1.695
R-HSA-9665245	Resistance of ERBB2 KD mutants to tesevatinib	2.018464e-02	1.695
R-HSA-9665247	Resistance of ERBB2 KD mutants to osimertinib	2.018464e-02	1.695
R-HSA-9665251	Resistance of ERBB2 KD mutants to lapatinib	2.018464e-02	1.695
R-HSA-8939246	RUNX1 regulates transcription of genes involved in differentiation of myeloid ce...	2.244258e-02	1.649
R-HSA-8939243	RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno...	2.049597e-02	1.688
R-HSA-6804754	Regulation of TP53 Expression	2.018464e-02	1.695
R-HSA-1810476	RIP-mediated NFkB activation via ZBP1	2.050608e-02	1.688
R-HSA-9909649	Regulation of PD-L1(CD274) transcription	2.089596e-02	1.680
R-HSA-9018519	Estrogen-dependent gene expression	2.147996e-02	1.668
R-HSA-69273	Cyclin A/B1/B2 associated events during G2/M transition	2.049597e-02	1.688
R-HSA-109581	Apoptosis	2.070944e-02	1.684
R-HSA-5674400	Constitutive Signaling by AKT1 E17K in Cancer	2.168782e-02	1.664
R-HSA-5357801	Programmed Cell Death	2.283305e-02	1.641
R-HSA-168138	Toll Like Receptor 9 (TLR9) Cascade	2.414441e-02	1.617
R-HSA-3928662	EPHB-mediated forward signaling	2.445185e-02	1.612
R-HSA-8856825	Cargo recognition for clathrin-mediated endocytosis	2.468871e-02	1.608
R-HSA-177929	Signaling by EGFR	2.473833e-02	1.607
R-HSA-193648	NRAGE signals death through JNK	2.473833e-02	1.607
R-HSA-5673000	RAF activation	2.534104e-02	1.596
R-HSA-5693532	DNA Double-Strand Break Repair	2.612358e-02	1.583
R-HSA-73887	Death Receptor Signaling	2.733807e-02	1.563
R-HSA-168164	Toll Like Receptor 3 (TLR3) Cascade	2.764248e-02	1.558
R-HSA-9932444	ATP-dependent chromatin remodelers	2.778726e-02	1.556
R-HSA-9932451	SWI/SNF chromatin remodelers	2.778726e-02	1.556
R-HSA-264870	Caspase-mediated cleavage of cytoskeletal proteins	2.802090e-02	1.553
R-HSA-9931521	The CRY:PER:kinase complex represses transactivation by the BMAL:CLOCK (ARNTL:CL...	2.817400e-02	1.550
R-HSA-1839120	Signaling by FGFR1 amplification mutants	3.044872e-02	1.516
R-HSA-5368598	Negative regulation of TCF-dependent signaling by DVL-interacting proteins	3.044872e-02	1.516
R-HSA-8875513	MET interacts with TNS proteins	3.044872e-02	1.516
R-HSA-8865999	MET activates PTPN11	3.044872e-02	1.516
R-HSA-8941326	RUNX2 regulates bone development	3.089420e-02	1.510
R-HSA-525793	Myogenesis	3.120615e-02	1.506
R-HSA-204998	Cell death signalling via NRAGE, NRIF and NADE	3.420275e-02	1.466
R-HSA-429914	Deadenylation-dependent mRNA decay	3.115586e-02	1.506
R-HSA-1500620	Meiosis	3.208986e-02	1.494
R-HSA-975155	MyD88 dependent cascade initiated on endosome	3.430569e-02	1.465
R-HSA-9854907	Regulation of MITF-M dependent genes involved in metabolism	3.044872e-02	1.516
R-HSA-2151209	Activation of PPARGC1A (PGC-1alpha) by phosphorylation	3.426600e-02	1.465
R-HSA-72306	tRNA processing	3.080290e-02	1.511
R-HSA-9725371	Nuclear events stimulated by ALK signaling in cancer	3.436513e-02	1.464
R-HSA-8878159	Transcriptional regulation by RUNX3	3.541288e-02	1.451
R-HSA-166166	MyD88-independent TLR4 cascade	3.613602e-02	1.442
R-HSA-937061	TRIF (TICAM1)-mediated TLR4 signaling	3.613602e-02	1.442
R-HSA-6804756	Regulation of TP53 Activity through Phosphorylation	3.620085e-02	1.441
R-HSA-9665348	Signaling by ERBB2 ECD mutants	3.733736e-02	1.428
R-HSA-180292	GAB1 signalosome	3.733736e-02	1.428
R-HSA-1839117	Signaling by cytosolic FGFR1 fusion mutants	3.733736e-02	1.428
R-HSA-1606322	ZBP1(DAI) mediated induction of type I IFNs	3.733736e-02	1.428
R-HSA-5653656	Vesicle-mediated transport	3.918865e-02	1.407
R-HSA-162909	Host Interactions of HIV factors	4.007254e-02	1.397
R-HSA-168181	Toll Like Receptor 7/8 (TLR7/8) Cascade	4.203996e-02	1.376
R-HSA-191650	Regulation of gap junction activity	4.233810e-02	1.373
R-HSA-165181	Inhibition of TSC complex formation by PKB	4.233810e-02	1.373
R-HSA-9652169	Signaling by MAP2K mutants	4.233810e-02	1.373
R-HSA-9705677	SARS-CoV-2 targets PDZ proteins in cell-cell junction	4.233810e-02	1.373
R-HSA-9615710	Late endosomal microautophagy	4.299148e-02	1.367
R-HSA-210745	Regulation of gene expression in beta cells	4.299148e-02	1.367
R-HSA-5683057	MAPK family signaling cascades	4.574838e-02	1.340
R-HSA-2559583	Cellular Senescence	4.585548e-02	1.339
R-HSA-5467333	APC truncation mutants are not K63 polyubiquitinated	5.253641e-02	1.280
R-HSA-3134973	LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production	5.565407e-02	1.255
R-HSA-8941284	RUNX2 regulates chondrocyte maturation	5.565407e-02	1.255
R-HSA-9673768	Signaling by membrane-tethered fusions of PDGFRA or PDGFRB	5.565407e-02	1.255
R-HSA-9931512	Phosphorylation of CLOCK, acetylation of BMAL1 (ARNTL) at target gene promoters	4.871393e-02	1.312
R-HSA-5693607	Processing of DNA double-strand break ends	5.547332e-02	1.256
R-HSA-6806834	Signaling by MET	5.243478e-02	1.280
R-HSA-1227990	Signaling by ERBB2 in Cancer	4.743918e-02	1.324
R-HSA-182971	EGFR downregulation	5.214935e-02	1.283
R-HSA-5673001	RAF/MAP kinase cascade	5.176725e-02	1.286
R-HSA-5675221	Negative regulation of MAPK pathway	5.208616e-02	1.283
R-HSA-416482	G alpha (12/13) signalling events	4.668953e-02	1.331
R-HSA-445144	Signal transduction by L1	4.801908e-02	1.319
R-HSA-8853884	Transcriptional Regulation by VENTX	4.806675e-02	1.318
R-HSA-9705683	SARS-CoV-2-host interactions	5.263186e-02	1.279
R-HSA-70326	Glucose metabolism	5.579529e-02	1.253
R-HSA-8851805	MET activates RAS signaling	5.688414e-02	1.245
R-HSA-4641265	Repression of WNT target genes	5.688414e-02	1.245
R-HSA-9634285	Constitutive Signaling by Overexpressed ERBB2	5.688414e-02	1.245
R-HSA-9617629	Regulation of FOXO transcriptional activity by acetylation	5.688414e-02	1.245
R-HSA-9012852	Signaling by NOTCH3	5.747423e-02	1.241
R-HSA-5693538	Homology Directed Repair	5.835038e-02	1.234
R-HSA-2219528	PI3K/AKT Signaling in Cancer	5.835038e-02	1.234
R-HSA-446728	Cell junction organization	5.905026e-02	1.229
R-HSA-9617828	FOXO-mediated transcription of cell cycle genes	6.021349e-02	1.220
R-HSA-9725370	Signaling by ALK fusions and activated point mutants	6.186263e-02	1.209
R-HSA-9700206	Signaling by ALK in cancer	6.186263e-02	1.209
R-HSA-5685938	HDR through Single Strand Annealing (SSA)	6.235838e-02	1.205
R-HSA-5684996	MAPK1/MAPK3 signaling	6.309377e-02	1.200
R-HSA-5684264	MAP3K8 (TPL2)-dependent MAPK1/3 activation	7.500884e-02	1.125
R-HSA-5696394	DNA Damage Recognition in GG-NER	6.785600e-02	1.168
R-HSA-9764560	Regulation of CDH1 Gene Transcription	6.411422e-02	1.193
R-HSA-9764725	Negative Regulation of CDH1 Gene Transcription	7.873223e-02	1.104
R-HSA-5693565	Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at...	7.415900e-02	1.130
R-HSA-9933937	Formation of the canonical BAF (cBAF) complex	7.500884e-02	1.125
R-HSA-9764562	Regulation of CDH1 mRNA translation by microRNAs	7.500884e-02	1.125
R-HSA-1500931	Cell-Cell communication	7.058647e-02	1.151
R-HSA-5693616	Presynaptic phase of homologous DNA pairing and strand exchange	7.962888e-02	1.099
R-HSA-975138	TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation	6.477344e-02	1.189
R-HSA-166016	Toll Like Receptor 4 (TLR4) Cascade	7.073075e-02	1.150
R-HSA-73857	RNA Polymerase II Transcription	7.919656e-02	1.101
R-HSA-187687	Signalling to ERKs	7.962888e-02	1.099
R-HSA-975871	MyD88 cascade initiated on plasma membrane	7.536752e-02	1.123
R-HSA-168176	Toll Like Receptor 5 (TLR5) Cascade	7.536752e-02	1.123
R-HSA-168142	Toll Like Receptor 10 (TLR10) Cascade	7.536752e-02	1.123
R-HSA-9758941	Gastrulation	7.341384e-02	1.134
R-HSA-446388	Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen...	7.021428e-02	1.154
R-HSA-9758919	Epithelial-Mesenchymal Transition (EMT) during gastrulation	7.021428e-02	1.154
R-HSA-9818030	NFE2L2 regulating tumorigenic genes	6.565731e-02	1.183
R-HSA-9839373	Signaling by TGFBR3	7.517519e-02	1.124
R-HSA-9856649	Transcriptional and post-translational regulation of MITF-M expression and activ...	6.789189e-02	1.168
R-HSA-9619665	EGR2 and SOX10-mediated initiation of Schwann cell myelination	6.785600e-02	1.168
R-HSA-6804115	TP53 regulates transcription of additional cell cycle genes whose exact role in ...	6.686909e-02	1.175
R-HSA-9648025	EML4 and NUDC in mitotic spindle formation	6.777185e-02	1.169
R-HSA-186712	Regulation of beta-cell development	7.415900e-02	1.130
R-HSA-1226099	Signaling by FGFR in disease	8.003019e-02	1.097
R-HSA-69620	Cell Cycle Checkpoints	8.124925e-02	1.090
R-HSA-429947	Deadenylation of mRNA	8.126685e-02	1.090
R-HSA-75067	Processing of Capped Intronless Pre-mRNA	8.126685e-02	1.090
R-HSA-8863678	Neurodegenerative Diseases	8.126685e-02	1.090
R-HSA-8862803	Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis...	8.126685e-02	1.090
R-HSA-9734091	Drug-mediated inhibition of MET activation	1.023158e-01	0.990
R-HSA-9006821	Alternative Lengthening of Telomeres (ALT)	1.023158e-01	0.990
R-HSA-9670621	Defective Inhibition of DNA Recombination at Telomere	1.023158e-01	0.990
R-HSA-9673013	Diseases of Telomere Maintenance	1.023158e-01	0.990
R-HSA-9670615	Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations	1.023158e-01	0.990
R-HSA-5619043	Defective SLC2A1 causes GLUT1 deficiency syndrome 1 (GLUT1DS1)	1.023158e-01	0.990
R-HSA-9699150	Defective DNA double strand break response due to BARD1 loss of function	1.023158e-01	0.990
R-HSA-5602566	TICAM1 deficiency - HSE	1.023158e-01	0.990
R-HSA-9670613	Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations	1.023158e-01	0.990
R-HSA-9663199	Defective DNA double strand break response due to BRCA1 loss of function	1.023158e-01	0.990
R-HSA-8951671	RUNX3 regulates YAP1-mediated transcription	8.585157e-02	1.066
R-HSA-6802953	RAS signaling downstream of NF1 loss-of-function variants	8.585157e-02	1.066
R-HSA-8851907	MET activates PI3K/AKT signaling	1.024129e-01	0.990
R-HSA-9726840	SHOC2 M1731 mutant abolishes MRAS complex function	1.024129e-01	0.990
R-HSA-8875360	InlB-mediated entry of Listeria monocytogenes into host cell	8.491187e-02	1.071
R-HSA-450385	Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA	8.491187e-02	1.071
R-HSA-936964	Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE)	1.062562e-01	0.974
R-HSA-77595	Processing of Intronless Pre-mRNAs	1.062562e-01	0.974
R-HSA-8934593	Regulation of RUNX1 Expression and Activity	9.705854e-02	1.013
R-HSA-3769402	Deactivation of the beta-catenin transactivating complex	9.241928e-02	1.034
R-HSA-8875878	MET promotes cell motility	9.918641e-02	1.004
R-HSA-9764265	Regulation of CDH1 Expression and Function	1.023370e-01	0.990
R-HSA-9764274	Regulation of Expression and Function of Type I Classical Cadherins	1.023370e-01	0.990
R-HSA-400685	Sema4D in semaphorin signaling	8.899312e-02	1.051
R-HSA-5693571	Nonhomologous End-Joining (NHEJ)	8.580427e-02	1.066
R-HSA-3371571	HSF1-dependent transactivation	1.032093e-01	0.986
R-HSA-430039	mRNA decay by 5' to 3' exoribonuclease	1.062562e-01	0.974
R-HSA-5693579	Homologous DNA Pairing and Strand Exchange	9.918641e-02	1.004
R-HSA-9818749	Regulation of NFE2L2 gene expression	8.585157e-02	1.066
R-HSA-3371511	HSF1 activation	8.589867e-02	1.066
R-HSA-6794361	Neurexins and neuroligins	1.093914e-01	0.961
R-HSA-169131	Inhibition of PKR	1.023158e-01	0.990
R-HSA-199920	CREB phosphorylation	8.585157e-02	1.066
R-HSA-8948747	Regulation of PTEN localization	1.024129e-01	0.990
R-HSA-445095	Interaction between L1 and Ankyrins	1.054525e-01	0.977
R-HSA-9931509	Expression of BMAL (ARNTL), CLOCK, and NPAS2	1.061952e-01	0.974
R-HSA-450294	MAP kinase activation	8.346588e-02	1.078
R-HSA-373755	Semaphorin interactions	9.341160e-02	1.030
R-HSA-166058	MyD88:MAL(TIRAP) cascade initiated on plasma membrane	1.106927e-01	0.956
R-HSA-168188	Toll Like Receptor TLR6:TLR2 Cascade	1.106927e-01	0.956
R-HSA-418885	DCC mediated attractive signaling	8.491187e-02	1.071
R-HSA-210500	Glutamate Neurotransmitter Release Cycle	9.705854e-02	1.013
R-HSA-9734009	Defective Intrinsic Pathway for Apoptosis	1.054525e-01	0.977
R-HSA-8939211	ESR-mediated signaling	1.084581e-01	0.965
R-HSA-1266738	Developmental Biology	8.590810e-02	1.066
R-HSA-8953897	Cellular responses to stimuli	1.067266e-01	0.972
R-HSA-6804757	Regulation of TP53 Degradation	8.589867e-02	1.066
R-HSA-373760	L1CAM interactions	9.875741e-02	1.005
R-HSA-5336415	Uptake and function of diphtheria toxin	1.024129e-01	0.990
R-HSA-9022699	MECP2 regulates neuronal receptors and channels	9.705854e-02	1.013
R-HSA-5696395	Formation of Incision Complex in GG-NER	1.134402e-01	0.945
R-HSA-9619483	Activation of AMPK downstream of NMDARs	1.141637e-01	0.942
R-HSA-5693606	DNA Double Strand Break Response	1.151828e-01	0.939
R-HSA-9639288	Amino acids regulate mTORC1	1.157588e-01	0.936
R-HSA-5637812	Signaling by EGFRvIII in Cancer	1.176364e-01	0.929
R-HSA-5637810	Constitutive Signaling by EGFRvIII	1.176364e-01	0.929
R-HSA-9759194	Nuclear events mediated by NFE2L2	1.190913e-01	0.924
R-HSA-446107	Type I hemidesmosome assembly	1.197582e-01	0.922
R-HSA-444473	Formyl peptide receptors bind formyl peptides and many other ligands	1.197582e-01	0.922
R-HSA-8875656	MET receptor recycling	1.197582e-01	0.922
R-HSA-9660537	Signaling by MRAS-complex mutants	1.197582e-01	0.922
R-HSA-9726842	Gain-of-function MRAS complexes activate RAF signaling	1.197582e-01	0.922
R-HSA-8849469	PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1	1.197582e-01	0.922
R-HSA-9825895	Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ...	1.197582e-01	0.922
R-HSA-9820841	M-decay: degradation of maternal mRNAs by maternally stored factors	1.209155e-01	0.918
R-HSA-5218920	VEGFR2 mediated vascular permeability	1.209155e-01	0.918
R-HSA-168255	Influenza Infection	1.226807e-01	0.911
R-HSA-9709570	Impaired BRCA2 binding to RAD51	1.231798e-01	0.909
R-HSA-9664565	Signaling by ERBB2 KD Mutants	1.231798e-01	0.909
R-HSA-9759475	Regulation of CDH11 Expression and Function	1.231798e-01	0.909
R-HSA-168179	Toll Like Receptor TLR1:TLR2 Cascade	1.234217e-01	0.909
R-HSA-181438	Toll Like Receptor 2 (TLR2) Cascade	1.234217e-01	0.909
R-HSA-2262752	Cellular responses to stress	1.234320e-01	0.909
R-HSA-8878171	Transcriptional regulation by RUNX1	1.236041e-01	0.908
R-HSA-9609690	HCMV Early Events	1.267807e-01	0.897
R-HSA-162906	HIV Infection	1.268373e-01	0.897
R-HSA-181429	Serotonin Neurotransmitter Release Cycle	1.294464e-01	0.888
R-HSA-176034	Interactions of Tat with host cellular proteins	1.494826e-01	0.825
R-HSA-205017	NFG and proNGF binds to p75NTR	1.494826e-01	0.825
R-HSA-5339700	Signaling by TCF7L2 mutants	1.494826e-01	0.825
R-HSA-5602571	TRAF3 deficiency - HSE	1.494826e-01	0.825
R-HSA-5602636	IKBKB deficiency causes SCID	1.494826e-01	0.825
R-HSA-5619111	Defective SLC20A2 causes idiopathic basal ganglia calcification 1 (IBGC1)	1.494826e-01	0.825
R-HSA-5603027	IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (E...	1.494826e-01	0.825
R-HSA-8985801	Regulation of cortical dendrite branching	1.941738e-01	0.712
R-HSA-3828062	Glycogen storage disease type 0 (muscle GYS1)	1.941738e-01	0.712
R-HSA-3814836	Glycogen storage disease type XV (GYG1)	1.941738e-01	0.712
R-HSA-3656535	TGFBR1 LBD Mutants in Cancer	1.941738e-01	0.712
R-HSA-170984	ARMS-mediated activation	1.377597e-01	0.861
R-HSA-193692	Regulated proteolysis of p75NTR	1.377597e-01	0.861
R-HSA-8941332	RUNX2 regulates genes involved in cell migration	1.752751e-01	0.756
R-HSA-8876493	InlA-mediated entry of Listeria monocytogenes into host cells	1.752751e-01	0.756
R-HSA-9013973	TICAM1-dependent activation of IRF3/IRF7	1.945862e-01	0.711
R-HSA-1839122	Signaling by activated point mutants of FGFR1	1.945862e-01	0.711
R-HSA-5339716	Signaling by GSK3beta mutants	1.945862e-01	0.711
R-HSA-937041	IKK complex recruitment mediated by RIP1	1.416541e-01	0.849
R-HSA-9709603	Impaired BRCA2 binding to PALB2	1.416541e-01	0.849
R-HSA-6807004	Negative regulation of MET activity	1.542271e-01	0.812
R-HSA-9701193	Defective homologous recombination repair (HRR) due to PALB2 loss of function	1.542271e-01	0.812
R-HSA-9701192	Defective homologous recombination repair (HRR) due to BRCA1 loss of function	1.542271e-01	0.812
R-HSA-9704646	Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of...	1.542271e-01	0.812
R-HSA-9704331	Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of...	1.542271e-01	0.812
R-HSA-5637815	Signaling by Ligand-Responsive EGFR Variants in Cancer	1.671333e-01	0.777
R-HSA-1236382	Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants	1.671333e-01	0.777
R-HSA-5654689	PI-3K cascade:FGFR1	1.938178e-01	0.713
R-HSA-390522	Striated Muscle Contraction	1.723671e-01	0.764
R-HSA-9843970	Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex	1.829262e-01	0.738
R-HSA-380284	Loss of proteins required for interphase microtubule organization from the centr...	1.887372e-01	0.724
R-HSA-380259	Loss of Nlp from mitotic centrosomes	1.887372e-01	0.724
R-HSA-416572	Sema4D induced cell migration and growth-cone collapse	1.542271e-01	0.812
R-HSA-9664873	Pexophagy	1.563007e-01	0.806
R-HSA-9759476	Regulation of Homotypic Cell-Cell Adhesion	1.919023e-01	0.717
R-HSA-9614399	Regulation of localization of FOXO transcription factors	1.752751e-01	0.756
R-HSA-5620916	VxPx cargo-targeting to cilium	1.542271e-01	0.812
R-HSA-5693567	HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA)	1.489521e-01	0.827
R-HSA-9675136	Diseases of DNA Double-Strand Break Repair	1.829262e-01	0.738
R-HSA-445989	TAK1-dependent IKK and NF-kappa-B activation	1.791083e-01	0.747
R-HSA-163680	AMPK inhibits chREBP transcriptional activation activity	1.377597e-01	0.861
R-HSA-9832991	Formation of the posterior neural plate	1.752751e-01	0.756
R-HSA-1227986	Signaling by ERBB2	1.651972e-01	0.782
R-HSA-2682334	EPH-Ephrin signaling	1.904747e-01	0.720
R-HSA-2426168	Activation of gene expression by SREBF (SREBP)	1.887372e-01	0.724
R-HSA-168315	Inhibition of Host mRNA Processing and RNA Silencing	1.494826e-01	0.825
R-HSA-190827	Transport of connexins along the secretory pathway	1.494826e-01	0.825
R-HSA-446343	Localization of the PINCH-ILK-PARVIN complex to focal adhesions	1.941738e-01	0.712
R-HSA-198765	Signalling to ERK5	1.941738e-01	0.712
R-HSA-418889	Caspase activation via Dependence Receptors in the absence of ligand	1.377597e-01	0.861
R-HSA-9701190	Defective homologous recombination repair (HRR) due to BRCA2 loss of function	1.829262e-01	0.738
R-HSA-69473	G2/M DNA damage checkpoint	1.589768e-01	0.799
R-HSA-9764260	Regulation of Expression and Function of Type II Classical Cadherins	1.620290e-01	0.790
R-HSA-212436	Generic Transcription Pathway	1.911242e-01	0.719
R-HSA-168898	Toll-like Receptor Cascades	1.698469e-01	0.770
R-HSA-1257604	PIP3 activates AKT signaling	1.362624e-01	0.866
R-HSA-8863795	Downregulation of ERBB2 signaling	1.324881e-01	0.878
R-HSA-448424	Interleukin-17 signaling	1.330992e-01	0.876
R-HSA-9616222	Transcriptional regulation of granulopoiesis	1.807493e-01	0.743
R-HSA-212676	Dopamine Neurotransmitter Release Cycle	1.938178e-01	0.713
R-HSA-9909648	Regulation of PD-L1(CD274) expression	1.576805e-01	0.802
R-HSA-9913351	Formation of the dystrophin-glycoprotein complex (DGC)	1.420750e-01	0.847
R-HSA-8848021	Signaling by PTK6	1.887372e-01	0.724
R-HSA-9006927	Signaling by Non-Receptor Tyrosine Kinases	1.887372e-01	0.724
R-HSA-190704	Oligomerization of connexins into connexons	1.494826e-01	0.825
R-HSA-264642	Acetylcholine Neurotransmitter Release Cycle	1.671333e-01	0.777
R-HSA-6794362	Protein-protein interactions at synapses	1.347333e-01	0.871
R-HSA-9855142	Cellular responses to mechanical stimuli	1.489521e-01	0.827
R-HSA-9860931	Response of endothelial cells to shear stress	1.740358e-01	0.759
R-HSA-9824585	Regulation of MITF-M-dependent genes involved in pigmentation	1.615102e-01	0.792
R-HSA-8854214	TBC/RABGAPs	1.446578e-01	0.840
R-HSA-168273	Influenza Viral RNA Transcription and Replication	1.488582e-01	0.827
R-HSA-844456	The NLRP3 inflammasome	1.416541e-01	0.849
R-HSA-187037	Signaling by NTRK1 (TRKA)	1.561139e-01	0.807
R-HSA-9860927	Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ...	1.936914e-01	0.713
R-HSA-9708296	tRNA-derived small RNA (tsRNA or tRNA-related fragment, tRF) biogenesis	1.941738e-01	0.712
R-HSA-9818032	NFE2L2 regulating MDR associated enzymes	1.377597e-01	0.861
R-HSA-198693	AKT phosphorylates targets in the nucleus	1.377597e-01	0.861
R-HSA-9820962	Assembly and release of respiratory syncytial virus (RSV) virions	1.563007e-01	0.806
R-HSA-9818028	NFE2L2 regulates pentose phosphate pathway genes	1.945862e-01	0.711
R-HSA-3000171	Non-integrin membrane-ECM interactions	1.657808e-01	0.780
R-HSA-5628897	TP53 Regulates Metabolic Genes	1.594272e-01	0.797
R-HSA-9762293	Regulation of CDH11 gene transcription	1.377597e-01	0.861
R-HSA-9610379	HCMV Late Events	1.577037e-01	0.802
R-HSA-448706	Interleukin-1 processing	1.377597e-01	0.861
R-HSA-9834752	Respiratory syncytial virus genome replication	1.377597e-01	0.861
R-HSA-1834949	Cytosolic sensors of pathogen-associated DNA	1.330992e-01	0.876
R-HSA-166520	Signaling by NTRKs	1.919363e-01	0.717
R-HSA-8986944	Transcriptional Regulation by MECP2	1.773230e-01	0.751
R-HSA-5619102	SLC transporter disorders	1.330727e-01	0.876
R-HSA-157858	Gap junction trafficking and regulation	1.973842e-01	0.705
R-HSA-9694516	SARS-CoV-2 Infection	2.043621e-01	0.690
R-HSA-8853659	RET signaling	2.046474e-01	0.689
R-HSA-749476	RNA Polymerase III Abortive And Retractive Initiation	2.046474e-01	0.689
R-HSA-74158	RNA Polymerase III Transcription	2.046474e-01	0.689
R-HSA-200425	Carnitine shuttle	2.075338e-01	0.683
R-HSA-9755511	KEAP1-NFE2L2 pathway	2.078069e-01	0.682
R-HSA-8953854	Metabolism of RNA	2.088101e-01	0.680
R-HSA-4839726	Chromatin organization	2.099361e-01	0.678
R-HSA-8853336	Signaling by plasma membrane FGFR1 fusions	2.365193e-01	0.626
R-HSA-209563	Axonal growth stimulation	2.365193e-01	0.626
R-HSA-5660862	Defective SLC7A7 causes lysinuric protein intolerance (LPI)	2.365193e-01	0.626
R-HSA-9013957	TLR3-mediated TICAM1-dependent programmed cell death	2.766419e-01	0.558
R-HSA-205025	NADE modulates death signalling	2.766419e-01	0.558
R-HSA-211163	AKT-mediated inactivation of FOXO1A	2.766419e-01	0.558
R-HSA-8952158	RUNX3 regulates BCL2L11 (BIM) transcription	2.766419e-01	0.558
R-HSA-1251932	PLCG1 events in ERBB2 signaling	2.766419e-01	0.558
R-HSA-2644607	Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling	2.766419e-01	0.558
R-HSA-2644605	FBXW7 Mutants and NOTCH1 in Cancer	2.766419e-01	0.558
R-HSA-5083630	Defective LFNG causes SCDO3	2.766419e-01	0.558
R-HSA-8939247	RUNX1 regulates transcription of genes involved in interleukin signaling	3.146584e-01	0.502
R-HSA-8939245	RUNX1 regulates transcription of genes involved in BCR signaling	3.146584e-01	0.502
R-HSA-74713	IRS activation	3.146584e-01	0.502
R-HSA-190374	FGFR1c and Klotho ligand binding and activation	3.146584e-01	0.502
R-HSA-203754	NOSIP mediated eNOS trafficking	3.146584e-01	0.502
R-HSA-9027276	Erythropoietin activates Phosphoinositide-3-kinase (PI3K)	2.141466e-01	0.669
R-HSA-937039	IRAK1 recruits IKK complex	2.141466e-01	0.669
R-HSA-975144	IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation	2.141466e-01	0.669
R-HSA-9820865	Z-decay: degradation of maternal mRNAs by zygotically expressed factors	2.141466e-01	0.669
R-HSA-4839743	Signaling by CTNNB1 phospho-site mutants	2.141466e-01	0.669
R-HSA-5358751	CTNNB1 S45 mutants aren't phosphorylated	2.141466e-01	0.669
R-HSA-5358747	CTNNB1 S33 mutants aren't phosphorylated	2.141466e-01	0.669
R-HSA-5358752	CTNNB1 T41 mutants aren't phosphorylated	2.141466e-01	0.669
R-HSA-5358749	CTNNB1 S37 mutants aren't phosphorylated	2.141466e-01	0.669
R-HSA-2660825	Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant	3.506790e-01	0.455
R-HSA-2660826	Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant	3.506790e-01	0.455
R-HSA-9833576	CDH11 homotypic and heterotypic interactions	3.506790e-01	0.455
R-HSA-176417	Phosphorylation of Emi1	3.506790e-01	0.455
R-HSA-5638302	Signaling by Overexpressed Wild-Type EGFR in Cancer	3.506790e-01	0.455
R-HSA-5638303	Inhibition of Signaling by Overexpressed EGFR	3.506790e-01	0.455
R-HSA-8985586	SLIT2:ROBO1 increases RHOA activity	3.506790e-01	0.455
R-HSA-8857538	PTK6 promotes HIF1A stabilization	3.848085e-01	0.415
R-HSA-426486	Small interfering RNA (siRNA) biogenesis	3.848085e-01	0.415
R-HSA-8939256	RUNX1 regulates transcription of genes involved in WNT signaling	3.848085e-01	0.415
R-HSA-9842640	Signaling by LTK in cancer	3.848085e-01	0.415
R-HSA-9027283	Erythropoietin activates STAT5	3.848085e-01	0.415
R-HSA-9027284	Erythropoietin activates RAS	2.735665e-01	0.563
R-HSA-937072	TRAF6-mediated induction of TAK1 complex within TLR4 complex	2.735665e-01	0.563
R-HSA-196299	Beta-catenin phosphorylation cascade	2.735665e-01	0.563
R-HSA-168927	TICAM1, RIP1-mediated IKK complex recruitment	2.735665e-01	0.563
R-HSA-9665686	Signaling by ERBB2 TMD/JMD mutants	2.214585e-01	0.655
R-HSA-9687136	Aberrant regulation of mitotic exit in cancer due to RB1 defects	2.934033e-01	0.533
R-HSA-203641	NOSTRIN mediated eNOS trafficking	4.171460e-01	0.380
R-HSA-2562578	TRIF-mediated programmed cell death	4.171460e-01	0.380
R-HSA-9732724	IFNG signaling activates MAPKs	4.171460e-01	0.380
R-HSA-1912399	Pre-NOTCH Processing in the Endoplasmic Reticulum	4.171460e-01	0.380
R-HSA-112412	SOS-mediated signalling	4.171460e-01	0.380
R-HSA-111367	SLBP independent Processing of Histone Pre-mRNAs	4.171460e-01	0.380
R-HSA-5693554	Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD...	2.355625e-01	0.628
R-HSA-1643713	Signaling by EGFR in Cancer	2.498175e-01	0.602
R-HSA-5654219	Phospholipase C-mediated cascade: FGFR1	3.327995e-01	0.478
R-HSA-176407	Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase	3.327995e-01	0.478
R-HSA-9006335	Signaling by Erythropoietin	2.932183e-01	0.533
R-HSA-8854518	AURKA Activation by TPX2	2.134792e-01	0.671
R-HSA-9764561	Regulation of CDH1 Function	2.758270e-01	0.559
R-HSA-176187	Activation of ATR in response to replication stress	3.516552e-01	0.454
R-HSA-201722	Formation of the beta-catenin:TCF transactivating complex	2.860814e-01	0.544
R-HSA-9768727	Regulation of CDH1 posttranslational processing and trafficking to plasma membra...	3.662196e-01	0.436
R-HSA-380270	Recruitment of mitotic centrosome proteins and complexes	2.749671e-01	0.561
R-HSA-5696400	Dual Incision in GG-NER	3.807271e-01	0.419
R-HSA-380287	Centrosome maturation	2.932740e-01	0.533
R-HSA-380320	Recruitment of NuMA to mitotic centrosomes	2.725107e-01	0.565
R-HSA-5654687	Downstream signaling of activated FGFR1	3.951604e-01	0.403
R-HSA-9925563	Developmental Lineage of Pancreatic Ductal Cells	4.015483e-01	0.396
R-HSA-6807505	RNA polymerase II transcribes snRNA genes	4.063219e-01	0.391
R-HSA-9614657	FOXO-mediated transcription of cell death genes	3.522707e-01	0.453
R-HSA-76046	RNA Polymerase III Transcription Initiation	3.078128e-01	0.512
R-HSA-195253	Degradation of beta-catenin by the destruction complex	4.120749e-01	0.385
R-HSA-5696399	Global Genome Nucleotide Excision Repair (GG-NER)	2.322547e-01	0.634
R-HSA-9013695	NOTCH4 Intracellular Domain Regulates Transcription	4.093468e-01	0.388
R-HSA-8931987	RUNX1 regulates estrogen receptor mediated transcription	4.171460e-01	0.380
R-HSA-9924644	Developmental Lineages of the Mammary Gland	2.659177e-01	0.575
R-HSA-156711	Polo-like kinase mediated events	3.522707e-01	0.453
R-HSA-9646399	Aggrephagy	2.500776e-01	0.602
R-HSA-205043	NRIF signals cell death from the nucleus	2.537049e-01	0.596
R-HSA-190242	FGFR1 ligand binding and activation	3.522707e-01	0.453
R-HSA-9609523	Insertion of tail-anchored proteins into the endoplasmic reticulum membrane	3.905749e-01	0.408
R-HSA-110314	Recognition of DNA damage by PCNA-containing replication complex	2.214585e-01	0.655
R-HSA-3371568	Attenuation phase	2.500776e-01	0.602
R-HSA-8939236	RUNX1 regulates transcription of genes involved in differentiation of HSCs	3.778430e-01	0.423
R-HSA-418990	Adherens junctions interactions	2.213432e-01	0.655
R-HSA-421270	Cell-cell junction organization	2.992332e-01	0.524
R-HSA-9931529	Phosphorylation and nuclear translocation of BMAL1 (ARNTL) and CLOCK	3.146584e-01	0.502
R-HSA-8852405	Signaling by MST1	3.506790e-01	0.455
R-HSA-9796292	Formation of axial mesoderm	2.338767e-01	0.631
R-HSA-933542	TRAF6 mediated NF-kB activation	2.214585e-01	0.655
R-HSA-9930044	Nuclear RNA decay	3.516552e-01	0.454
R-HSA-9909396	Circadian clock	2.811620e-01	0.551
R-HSA-8941856	RUNX3 regulates NOTCH signaling	2.141466e-01	0.669
R-HSA-4641262	Disassembly of the destruction complex and recruitment of AXIN to the membrane	2.641958e-01	0.578
R-HSA-9842860	Regulation of endogenous retroelements	4.094980e-01	0.388
R-HSA-5693537	Resolution of D-Loop Structures	3.662196e-01	0.436
R-HSA-110381	Resolution of AP sites via the single-nucleotide replacement pathway	3.146584e-01	0.502
R-HSA-426496	Post-transcriptional silencing by small RNAs	3.146584e-01	0.502
R-HSA-163754	Insulin effects increased synthesis of Xylulose-5-Phosphate	4.171460e-01	0.380
R-HSA-5693568	Resolution of D-loop Structures through Holliday Junction Intermediates	3.516552e-01	0.454
R-HSA-9734779	Developmental Cell Lineages of the Integumentary System	3.234210e-01	0.490
R-HSA-5685942	HDR through Homologous Recombination (HRR)	3.804404e-01	0.420
R-HSA-190828	Gap junction trafficking	3.093689e-01	0.510
R-HSA-9758274	Regulation of NF-kappa B signaling	2.934033e-01	0.533
R-HSA-5685939	HDR through MMEJ (alt-NHEJ)	2.338767e-01	0.631
R-HSA-4791275	Signaling by WNT in cancer	3.370527e-01	0.472
R-HSA-69481	G2/M Checkpoints	3.603234e-01	0.443
R-HSA-8937144	Aryl hydrocarbon receptor signalling	3.506790e-01	0.455
R-HSA-6806942	MET Receptor Activation	3.848085e-01	0.415
R-HSA-9675126	Diseases of mitotic cell cycle	3.370527e-01	0.472
R-HSA-9793380	Formation of paraxial mesoderm	3.172244e-01	0.499
R-HSA-912631	Regulation of signaling by CBL	3.715400e-01	0.430
R-HSA-376176	Signaling by ROBO receptors	3.156310e-01	0.501
R-HSA-9020702	Interleukin-1 signaling	2.616486e-01	0.582
R-HSA-5621575	CD209 (DC-SIGN) signaling	2.214585e-01	0.655
R-HSA-73894	DNA Repair	3.178296e-01	0.498
R-HSA-8875791	MET activates STAT3	2.365193e-01	0.626
R-HSA-8866376	Reelin signalling pathway	3.146584e-01	0.502
R-HSA-3656534	Loss of Function of TGFBR1 in Cancer	3.146584e-01	0.502
R-HSA-193681	Ceramide signalling	3.506790e-01	0.455
R-HSA-9933947	Formation of the non-canonical BAF (ncBAF) complex	2.338767e-01	0.631
R-HSA-69478	G2/M DNA replication checkpoint	3.848085e-01	0.415
R-HSA-162588	Budding and maturation of HIV virion	3.224316e-01	0.492
R-HSA-2559586	DNA Damage/Telomere Stress Induced Senescence	3.277026e-01	0.485
R-HSA-2219530	Constitutive Signaling by Aberrant PI3K in Cancer	3.315025e-01	0.480
R-HSA-73933	Resolution of Abasic Sites (AP sites)	2.617618e-01	0.582
R-HSA-9609646	HCMV Infection	2.142192e-01	0.669
R-HSA-913531	Interferon Signaling	2.716486e-01	0.566
R-HSA-69275	G2/M Transition	2.233947e-01	0.651
R-HSA-1655829	Regulation of cholesterol biosynthesis by SREBP (SREBF)	3.305420e-01	0.481
R-HSA-6811442	Intra-Golgi and retrograde Golgi-to-ER traffic	4.031259e-01	0.395
R-HSA-453274	Mitotic G2-G2/M phases	2.336286e-01	0.631
R-HSA-6803211	TP53 Regulates Transcription of Death Receptors and Ligands	2.537049e-01	0.596
R-HSA-1963642	PI3K events in ERBB2 signaling	3.327995e-01	0.478
R-HSA-5260271	Diseases of Immune System	2.500776e-01	0.602
R-HSA-5602358	Diseases associated with the TLR signaling cascade	2.500776e-01	0.602
R-HSA-198753	ERK/MAPK targets	4.093468e-01	0.388
R-HSA-1660499	Synthesis of PIPs at the plasma membrane	3.277026e-01	0.485
R-HSA-2565942	Regulation of PLK1 Activity at G2/M Transition	2.322547e-01	0.634
R-HSA-2173796	SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription	4.237400e-01	0.373
R-HSA-446652	Interleukin-1 family signaling	3.143091e-01	0.503
R-HSA-390648	Muscarinic acetylcholine receptors	3.146584e-01	0.502
R-HSA-9937080	Developmental Lineage of Multipotent Pancreatic Progenitor Cells	3.370527e-01	0.472
R-HSA-5654726	Negative regulation of FGFR1 signaling	3.516552e-01	0.454
R-HSA-199418	Negative regulation of the PI3K/AKT network	3.829208e-01	0.417
R-HSA-168928	DDX58/IFIH1-mediated induction of interferon-alpha/beta	3.400985e-01	0.468
R-HSA-389948	Co-inhibition by PD-1	2.985977e-01	0.525
R-HSA-9022692	Regulation of MECP2 expression and activity	3.516552e-01	0.454
R-HSA-6811440	Retrograde transport at the Trans-Golgi-Network	3.456047e-01	0.461
R-HSA-9006925	Intracellular signaling by second messengers	3.161394e-01	0.500
R-HSA-5626978	TNFR1-mediated ceramide production	2.766419e-01	0.558
R-HSA-193670	p75NTR negatively regulates cell cycle via SC1	2.766419e-01	0.558
R-HSA-187706	Signalling to p38 via RIT and RIN	3.506790e-01	0.455
R-HSA-5653890	Lactose synthesis	3.848085e-01	0.415
R-HSA-399954	Sema3A PAK dependent Axon repulsion	2.735665e-01	0.563
R-HSA-181430	Norepinephrine Neurotransmitter Release Cycle	2.214585e-01	0.655
R-HSA-6787450	tRNA modification in the mitochondrion	3.131632e-01	0.504
R-HSA-9834899	Specification of the neural plate border	3.715400e-01	0.430
R-HSA-168643	Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali...	3.487530e-01	0.457
R-HSA-2173793	Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer	2.656509e-01	0.576
R-HSA-450282	MAPK targets/ Nuclear events mediated by MAP kinases	2.932183e-01	0.533
R-HSA-9772755	Formation of WDR5-containing histone-modifying complexes	3.951604e-01	0.403
R-HSA-5357769	Caspase activation via extrinsic apoptotic signalling pathway	2.498175e-01	0.602
R-HSA-9008059	Interleukin-37 signaling	3.078128e-01	0.512
R-HSA-437239	Recycling pathway of L1	3.456047e-01	0.461
R-HSA-388841	Regulation of T cell activation by CD28 family	3.248522e-01	0.488
R-HSA-8943724	Regulation of PTEN gene transcription	3.067890e-01	0.513
R-HSA-3247509	Chromatin modifying enzymes	3.983056e-01	0.400
R-HSA-9007101	Rab regulation of trafficking	4.116715e-01	0.385
R-HSA-9006936	Signaling by TGFB family members	2.585429e-01	0.587
R-HSA-5660668	CLEC7A/inflammasome pathway	3.506790e-01	0.455
R-HSA-427652	Sodium-coupled phosphate cotransporters	3.506790e-01	0.455
R-HSA-450513	Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA	2.735665e-01	0.563
R-HSA-210744	Regulation of gene expression in late stage (branching morphogenesis) pancreatic...	2.934033e-01	0.533
R-HSA-3371599	Defective HLCS causes multiple carboxylase deficiency	4.171460e-01	0.380
R-HSA-426117	Cation-coupled Chloride cotransporters	4.171460e-01	0.380
R-HSA-69242	S Phase	2.884278e-01	0.540
R-HSA-196780	Biotin transport and metabolism	2.735665e-01	0.563
R-HSA-198323	AKT phosphorylates targets in the cytosol	2.141466e-01	0.669
R-HSA-2173795	Downregulation of SMAD2/3:SMAD4 transcriptional activity	3.370527e-01	0.472
R-HSA-9830364	Formation of the nephric duct	2.355625e-01	0.628
R-HSA-9675135	Diseases of DNA repair	3.335018e-01	0.477
R-HSA-9764302	Regulation of CDH19 Expression and Function	3.506790e-01	0.455
R-HSA-8964011	HDL clearance	3.848085e-01	0.415
R-HSA-391906	Leukotriene receptors	3.848085e-01	0.415
R-HSA-9823739	Formation of the anterior neural plate	2.735665e-01	0.563
R-HSA-9707616	Heme signaling	3.277026e-01	0.485
R-HSA-9931269	AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274)	4.060066e-01	0.391
R-HSA-9701898	STAT3 nuclear events downstream of ALK signaling	2.735665e-01	0.563
R-HSA-622312	Inflammasomes	2.786712e-01	0.555
R-HSA-69205	G1/S-Specific Transcription	4.095031e-01	0.388
R-HSA-373752	Netrin-1 signaling	3.093689e-01	0.510
R-HSA-1280215	Cytokine Signaling in Immune system	3.175746e-01	0.498
R-HSA-9860276	SLC15A4:TASL-dependent IRF5 activation	3.506790e-01	0.455
R-HSA-388844	Receptor-type tyrosine-protein phosphatases	2.934033e-01	0.533
R-HSA-109704	PI3K Cascade	3.819136e-01	0.418
R-HSA-163685	Integration of energy metabolism	3.152336e-01	0.501
R-HSA-9830369	Kidney development	3.804404e-01	0.420
R-HSA-3304351	Signaling by TGF-beta Receptor Complex in Cancer	3.848085e-01	0.415
R-HSA-110357	Displacement of DNA glycosylase by APEX1	4.171460e-01	0.380
R-HSA-5357905	Regulation of TNFR1 signaling	3.335018e-01	0.477
R-HSA-449147	Signaling by Interleukins	2.594489e-01	0.586
R-HSA-75893	TNF signaling	2.656509e-01	0.576
R-HSA-6791312	TP53 Regulates Transcription of Cell Cycle Genes	2.758270e-01	0.559
R-HSA-9831926	Nephron development	3.522707e-01	0.453
R-HSA-8866910	TFAP2 (AP-2) family regulates transcription of growth factors and their receptor...	3.131632e-01	0.504
R-HSA-5210891	Uptake and function of anthrax toxins	3.327995e-01	0.478
R-HSA-210991	Basigin interactions	4.093468e-01	0.388
R-HSA-9692916	SARS-CoV-1 activates/modulates innate immune responses	4.060066e-01	0.391
R-HSA-6785807	Interleukin-4 and Interleukin-13 signaling	2.546454e-01	0.594
R-HSA-381038	XBP1(S) activates chaperone genes	4.063219e-01	0.391
R-HSA-5339562	Uptake and actions of bacterial toxins	4.060066e-01	0.391
R-HSA-8878166	Transcriptional regulation by RUNX2	4.278022e-01	0.369
R-HSA-76066	RNA Polymerase III Transcription Initiation From Type 2 Promoter	4.278308e-01	0.369
R-HSA-5696397	Gap-filling DNA repair synthesis and ligation in GG-NER	4.278308e-01	0.369
R-HSA-9671555	Signaling by PDGFR in disease	4.278308e-01	0.369
R-HSA-450531	Regulation of mRNA stability by proteins that bind AU-rich elements	4.330382e-01	0.363
R-HSA-5620912	Anchoring of the basal body to the plasma membrane	4.441012e-01	0.353
R-HSA-5696398	Nucleotide Excision Repair	4.441673e-01	0.352
R-HSA-9938206	Developmental Lineage of Mammary Stem Cells	4.460053e-01	0.351
R-HSA-76061	RNA Polymerase III Transcription Initiation From Type 1 Promoter	4.460053e-01	0.351
R-HSA-112409	RAF-independent MAPK1/3 activation	4.460053e-01	0.351
R-HSA-350054	Notch-HLH transcription pathway	4.460053e-01	0.351
R-HSA-6803205	TP53 regulates transcription of several additional cell death genes whose specif...	4.460053e-01	0.351
R-HSA-212718	EGFR interacts with phospholipase C-gamma	4.477856e-01	0.349
R-HSA-9828211	Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation	4.477856e-01	0.349
R-HSA-9028335	Activated NTRK2 signals through PI3K	4.477856e-01	0.349
R-HSA-9768778	Regulation of NPAS4 mRNA translation	4.477856e-01	0.349
R-HSA-190370	FGFR1b ligand binding and activation	4.477856e-01	0.349
R-HSA-3785653	Myoclonic epilepsy of Lafora	4.477856e-01	0.349
R-HSA-193634	Axonal growth inhibition (RHOA activation)	4.477856e-01	0.349
R-HSA-8939242	RUNX1 regulates transcription of genes involved in differentiation of keratinocy...	4.477856e-01	0.349
R-HSA-164940	Nef mediated downregulation of MHC class I complex cell surface expression	4.477856e-01	0.349
R-HSA-77588	SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs	4.477856e-01	0.349
R-HSA-1253288	Downregulation of ERBB4 signaling	4.477856e-01	0.349
R-HSA-390696	Adrenoceptors	4.477856e-01	0.349
R-HSA-1912408	Pre-NOTCH Transcription and Translation	4.534780e-01	0.343
R-HSA-5654736	Signaling by FGFR1	4.535548e-01	0.343
R-HSA-9662361	Sensory processing of sound by outer hair cells of the cochlea	4.535548e-01	0.343
R-HSA-9679506	SARS-CoV Infections	4.585256e-01	0.339
R-HSA-6811558	PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling	4.599150e-01	0.337
R-HSA-381070	IRE1alpha activates chaperones	4.628179e-01	0.335
R-HSA-9634638	Estrogen-dependent nuclear events downstream of ESR-membrane signaling	4.638519e-01	0.334
R-HSA-3000170	Syndecan interactions	4.638519e-01	0.334
R-HSA-5633008	TP53 Regulates Transcription of Cell Death Genes	4.641609e-01	0.333
R-HSA-112399	IRS-mediated signalling	4.652560e-01	0.332
R-HSA-202433	Generation of second messenger molecules	4.656788e-01	0.332
R-HSA-6807070	PTEN Regulation	4.659512e-01	0.332
R-HSA-983231	Factors involved in megakaryocyte development and platelet production	4.758073e-01	0.323
R-HSA-201688	WNT mediated activation of DVL	4.768163e-01	0.322
R-HSA-112411	MAPK1 (ERK2) activation	4.768163e-01	0.322
R-HSA-193697	p75NTR regulates axonogenesis	4.768163e-01	0.322
R-HSA-2025928	Calcineurin activates NFAT	4.768163e-01	0.322
R-HSA-5649702	APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement P...	4.768163e-01	0.322
R-HSA-428542	Regulation of commissural axon pathfinding by SLIT and ROBO	4.768163e-01	0.322
R-HSA-9619229	Activation of RAC1 downstream of NMDARs	4.768163e-01	0.322
R-HSA-430116	GP1b-IX-V activation signalling	4.768163e-01	0.322
R-HSA-3323169	Defects in biotin (Btn) metabolism	4.768163e-01	0.322
R-HSA-72163	mRNA Splicing - Major Pathway	4.799487e-01	0.319
R-HSA-5654688	SHC-mediated cascade:FGFR1	4.813548e-01	0.318
R-HSA-202403	TCR signaling	4.869669e-01	0.313
R-HSA-5654693	FRS-mediated FGFR1 signaling	4.985007e-01	0.302
R-HSA-203927	MicroRNA (miRNA) biogenesis	4.985007e-01	0.302
R-HSA-1482801	Acyl chain remodelling of PS	4.985007e-01	0.302
R-HSA-1660661	Sphingolipid de novo biosynthesis	4.997866e-01	0.301
R-HSA-9006931	Signaling by Nuclear Receptors	5.007959e-01	0.300
R-HSA-9014325	TICAM1,TRAF6-dependent induction of TAK1 complex	5.043224e-01	0.297
R-HSA-110056	MAPK3 (ERK1) activation	5.043224e-01	0.297
R-HSA-9027277	Erythropoietin activates Phospholipase C gamma (PLCG)	5.043224e-01	0.297
R-HSA-390450	Folding of actin by CCT/TriC	5.043224e-01	0.297
R-HSA-5140745	WNT5A-dependent internalization of FZD2, FZD5 and ROR2	5.043224e-01	0.297
R-HSA-9762292	Regulation of CDH11 function	5.043224e-01	0.297
R-HSA-198203	PI3K/AKT activation	5.043224e-01	0.297
R-HSA-173107	Binding and entry of HIV virion	5.043224e-01	0.297
R-HSA-140342	Apoptosis induced DNA fragmentation	5.043224e-01	0.297
R-HSA-2179392	EGFR Transactivation by Gastrin	5.043224e-01	0.297
R-HSA-6803544	Ion influx/efflux at host-pathogen interface	5.043224e-01	0.297
R-HSA-74749	Signal attenuation	5.043224e-01	0.297
R-HSA-428359	Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RN...	5.043224e-01	0.297
R-HSA-8934903	Receptor Mediated Mitophagy	5.043224e-01	0.297
R-HSA-5689877	Josephin domain DUBs	5.043224e-01	0.297
R-HSA-2586552	Signaling by Leptin	5.043224e-01	0.297
R-HSA-2428928	IRS-related events triggered by IGF1R	5.110826e-01	0.292
R-HSA-9856530	High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR...	5.147825e-01	0.288
R-HSA-9703465	Signaling by FLT3 fusion proteins	5.152790e-01	0.288
R-HSA-110373	Resolution of AP sites via the multiple-nucleotide patch replacement pathway	5.152790e-01	0.288
R-HSA-381340	Transcriptional regulation of white adipocyte differentiation	5.178453e-01	0.286
R-HSA-6807878	COPI-mediated anterograde transport	5.178453e-01	0.286
R-HSA-6811434	COPI-dependent Golgi-to-ER retrograde traffic	5.178453e-01	0.286
R-HSA-375165	NCAM signaling for neurite out-growth	5.222610e-01	0.282
R-HSA-170834	Signaling by TGF-beta Receptor Complex	5.268108e-01	0.278
R-HSA-9759811	Regulation of CDH11 mRNA translation by microRNAs	5.303840e-01	0.275
R-HSA-4839744	Signaling by APC mutants	5.303840e-01	0.275
R-HSA-5467340	AXIN missense mutants destabilize the destruction complex	5.303840e-01	0.275
R-HSA-5467337	APC truncation mutants have impaired AXIN binding	5.303840e-01	0.275
R-HSA-5467348	Truncations of AMER1 destabilize the destruction complex	5.303840e-01	0.275
R-HSA-192814	vRNA Synthesis	5.303840e-01	0.275
R-HSA-192905	vRNP Assembly	5.303840e-01	0.275
R-HSA-9706019	RHOBTB3 ATPase cycle	5.303840e-01	0.275
R-HSA-933543	NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10	5.303840e-01	0.275
R-HSA-210990	PECAM1 interactions	5.303840e-01	0.275
R-HSA-9758890	Transport of RCbl within the body	5.303840e-01	0.275
R-HSA-9020558	Interleukin-2 signaling	5.303840e-01	0.275
R-HSA-3928663	EPHA-mediated growth cone collapse	5.316809e-01	0.274
R-HSA-167243	Tat-mediated HIV elongation arrest and recovery	5.316809e-01	0.274
R-HSA-167238	Pausing and recovery of Tat-mediated HIV elongation	5.316809e-01	0.274
R-HSA-389357	CD28 dependent PI3K/Akt signaling	5.316809e-01	0.274
R-HSA-264876	Insulin processing	5.316809e-01	0.274
R-HSA-199977	ER to Golgi Anterograde Transport	5.322854e-01	0.274
R-HSA-2559582	Senescence-Associated Secretory Phenotype (SASP)	5.344743e-01	0.272
R-HSA-74751	Insulin receptor signalling cascade	5.442425e-01	0.264
R-HSA-2428924	IGF1R signaling cascade	5.442425e-01	0.264
R-HSA-3214847	HATs acetylate histones	5.445335e-01	0.264
R-HSA-9824272	Somitogenesis	5.450921e-01	0.264
R-HSA-167287	HIV elongation arrest and recovery	5.476995e-01	0.261
R-HSA-167290	Pausing and recovery of HIV elongation	5.476995e-01	0.261
R-HSA-72172	mRNA Splicing	5.493159e-01	0.260
R-HSA-2404192	Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)	5.550355e-01	0.256
R-HSA-8950505	Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati...	5.550355e-01	0.256
R-HSA-416550	Sema4D mediated inhibition of cell attachment and migration	5.550769e-01	0.256
R-HSA-428540	Activation of RAC1	5.550769e-01	0.256
R-HSA-9824878	Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7	5.550769e-01	0.256
R-HSA-110362	POLB-Dependent Long Patch Base Excision Repair	5.550769e-01	0.256
R-HSA-202670	ERKs are inactivated	5.550769e-01	0.256
R-HSA-4839748	Signaling by AMER1 mutants	5.550769e-01	0.256
R-HSA-4839735	Signaling by AXIN mutants	5.550769e-01	0.256
R-HSA-5693548	Sensing of DNA Double Strand Breaks	5.550769e-01	0.256
R-HSA-72165	mRNA Splicing - Minor Pathway	5.576492e-01	0.254
R-HSA-9660826	Purinergic signaling in leishmaniasis infection	5.576492e-01	0.254
R-HSA-9664424	Cell recruitment (pro-inflammatory response)	5.576492e-01	0.254
R-HSA-9734767	Developmental Cell Lineages	5.630831e-01	0.249
R-HSA-917729	Endosomal Sorting Complex Required For Transport (ESCRT)	5.633298e-01	0.249
R-HSA-3928665	EPH-ephrin mediated repulsion of cells	5.699957e-01	0.244
R-HSA-2197563	NOTCH2 intracellular domain regulates transcription	5.784727e-01	0.238
R-HSA-2691230	Signaling by NOTCH1 HD Domain Mutants in Cancer	5.784727e-01	0.238
R-HSA-2691232	Constitutive Signaling by NOTCH1 HD Domain Mutants	5.784727e-01	0.238
R-HSA-3000484	Scavenging by Class F Receptors	5.784727e-01	0.238
R-HSA-9931530	Phosphorylation and nuclear translocation of the CRY:PER:kinase complex	5.784727e-01	0.238
R-HSA-179812	GRB2 events in EGFR signaling	5.784727e-01	0.238
R-HSA-380615	Serotonin clearance from the synaptic cleft	5.784727e-01	0.238
R-HSA-8951936	RUNX3 regulates p14-ARF	5.784727e-01	0.238
R-HSA-8983711	OAS antiviral response	5.784727e-01	0.238
R-HSA-73943	Reversal of alkylation damage by DNA dioxygenases	5.784727e-01	0.238
R-HSA-1250196	SHC1 events in ERBB2 signaling	5.785685e-01	0.238
R-HSA-68962	Activation of the pre-replicative complex	5.785685e-01	0.238
R-HSA-9687139	Aberrant regulation of mitotic cell cycle due to RB1 defects	5.785685e-01	0.238
R-HSA-888590	GABA synthesis, release, reuptake and degradation	5.785685e-01	0.238
R-HSA-1474151	Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation	5.785685e-01	0.238
R-HSA-5619115	Disorders of transmembrane transporters	5.793729e-01	0.237
R-HSA-389356	Co-stimulation by CD28	5.821268e-01	0.235
R-HSA-9662360	Sensory processing of sound by inner hair cells of the cochlea	5.865708e-01	0.232
R-HSA-438064	Post NMDA receptor activation events	5.912087e-01	0.228
R-HSA-5694530	Cargo concentration in the ER	5.934134e-01	0.227
R-HSA-186763	Downstream signal transduction	5.934134e-01	0.227
R-HSA-9766229	Degradation of CDH1	5.940385e-01	0.226
R-HSA-2122947	NOTCH1 Intracellular Domain Regulates Transcription	5.940385e-01	0.226
R-HSA-73893	DNA Damage Bypass	5.940385e-01	0.226
R-HSA-8877330	RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)	6.006397e-01	0.221
R-HSA-190373	FGFR1c ligand binding and activation	6.006397e-01	0.221
R-HSA-174490	Membrane binding and targetting of GAG proteins	6.006397e-01	0.221
R-HSA-8963901	Chylomicron remodeling	6.006397e-01	0.221
R-HSA-75035	Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex	6.006397e-01	0.221
R-HSA-6811555	PI5P Regulates TP53 Acetylation	6.006397e-01	0.221
R-HSA-9683610	Maturation of nucleoprotein	6.006397e-01	0.221
R-HSA-5658442	Regulation of RAS by GAPs	6.057275e-01	0.218
R-HSA-9816359	Maternal to zygotic transition (MZT)	6.079237e-01	0.216
R-HSA-5620920	Cargo trafficking to the periciliary membrane	6.167654e-01	0.210
R-HSA-912446	Meiotic recombination	6.171909e-01	0.210
R-HSA-2029482	Regulation of actin dynamics for phagocytic cup formation	6.187928e-01	0.208
R-HSA-8847993	ERBB2 Activates PTK6 Signaling	6.216422e-01	0.206
R-HSA-69166	Removal of the Flap Intermediate	6.216422e-01	0.206
R-HSA-174495	Synthesis And Processing Of GAG, GAGPOL Polyproteins	6.216422e-01	0.206
R-HSA-1433559	Regulation of KIT signaling	6.216422e-01	0.206
R-HSA-5655291	Signaling by FGFR4 in disease	6.216422e-01	0.206
R-HSA-975163	IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation	6.216422e-01	0.206
R-HSA-5578768	Physiological factors	6.216422e-01	0.206
R-HSA-391160	Signal regulatory protein family interactions	6.216422e-01	0.206
R-HSA-6804758	Regulation of TP53 Activity through Acetylation	6.219201e-01	0.206
R-HSA-5675482	Regulation of necroptotic cell death	6.219201e-01	0.206
R-HSA-198725	Nuclear Events (kinase and transcription factor activation)	6.265188e-01	0.203
R-HSA-112382	Formation of RNA Pol II elongation complex	6.284264e-01	0.202
R-HSA-9634815	Transcriptional Regulation by NPAS4	6.284264e-01	0.202
R-HSA-390471	Association of TriC/CCT with target proteins during biosynthesis	6.355839e-01	0.197
R-HSA-4086398	Ca2+ pathway	6.361128e-01	0.196
R-HSA-75955	RNA Polymerase II Transcription Elongation	6.394323e-01	0.194
R-HSA-445355	Smooth Muscle Contraction	6.394323e-01	0.194
R-HSA-8948700	Competing endogenous RNAs (ceRNAs) regulate PTEN translation	6.415415e-01	0.193
R-HSA-180336	SHC1 events in EGFR signaling	6.415415e-01	0.193
R-HSA-6785631	ERBB2 Regulates Cell Motility	6.415415e-01	0.193
R-HSA-110312	Translesion synthesis by REV1	6.415415e-01	0.193
R-HSA-69183	Processive synthesis on the lagging strand	6.415415e-01	0.193
R-HSA-2173791	TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)	6.415415e-01	0.193
R-HSA-419408	Lysosphingolipid and LPA receptors	6.415415e-01	0.193
R-HSA-1295596	Spry regulation of FGF signaling	6.415415e-01	0.193
R-HSA-9735871	SARS-CoV-1 targets host intracellular signalling and regulatory pathways	6.415415e-01	0.193
R-HSA-73942	DNA Damage Reversal	6.415415e-01	0.193
R-HSA-1368108	BMAL1:CLOCK,NPAS2 activates circadian expression	6.488575e-01	0.188
R-HSA-203615	eNOS activation	6.488575e-01	0.188
R-HSA-168638	NOD1/2 Signaling Pathway	6.488575e-01	0.188
R-HSA-5205647	Mitophagy	6.488575e-01	0.188
R-HSA-9768919	NPAS4 regulates expression of target genes	6.488575e-01	0.188
R-HSA-1362300	Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL...	6.603952e-01	0.180
R-HSA-5656121	Translesion synthesis by POLI	6.603952e-01	0.180
R-HSA-176412	Phosphorylation of the APC/C	6.603952e-01	0.180
R-HSA-9664420	Killing mechanisms	6.603952e-01	0.180
R-HSA-9673324	WNT5:FZD7-mediated leishmania damping	6.603952e-01	0.180
R-HSA-399955	SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion	6.603952e-01	0.180
R-HSA-9603798	Class I peroxisomal membrane protein import	6.603952e-01	0.180
R-HSA-9634600	Regulation of glycolysis by fructose 2,6-bisphosphate metabolism	6.603952e-01	0.180
R-HSA-5635838	Activation of SMO	6.603952e-01	0.180
R-HSA-140534	Caspase activation via Death Receptors in the presence of ligand	6.603952e-01	0.180
R-HSA-9945266	Differentiation of T cells	6.603952e-01	0.180
R-HSA-9942503	Differentiation of naive CD+ T cells to T helper 1 cells (Th1 cells)	6.603952e-01	0.180
R-HSA-6803207	TP53 Regulates Transcription of Caspase Activators and Caspases	6.603952e-01	0.180
R-HSA-983168	Antigen processing: Ubiquitination & Proteasome degradation	6.615597e-01	0.179
R-HSA-2559585	Oncogene Induced Senescence	6.617442e-01	0.179
R-HSA-9020591	Interleukin-12 signaling	6.639215e-01	0.178
R-HSA-1912422	Pre-NOTCH Expression and Processing	6.665656e-01	0.176
R-HSA-6782210	Gap-filling DNA repair synthesis and ligation in TC-NER	6.710627e-01	0.173
R-HSA-450408	AUF1 (hnRNP D0) binds and destabilizes mRNA	6.742479e-01	0.171
R-HSA-9682385	FLT3 signaling in disease	6.742479e-01	0.171
R-HSA-8964616	G beta:gamma signalling through CDC42	6.782584e-01	0.169
R-HSA-975110	TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling	6.782584e-01	0.169
R-HSA-5655862	Translesion synthesis by POLK	6.782584e-01	0.169
R-HSA-1963640	GRB2 events in ERBB2 signaling	6.782584e-01	0.169
R-HSA-141430	Inactivation of APC/C via direct inhibition of the APC/C complex	6.782584e-01	0.169
R-HSA-918233	TRAF3-dependent IRF activation pathway	6.782584e-01	0.169
R-HSA-141405	Inhibition of the proteolytic activity of APC/C required for the onset of anapha...	6.782584e-01	0.169
R-HSA-1483148	Synthesis of PG	6.782584e-01	0.169
R-HSA-6804114	TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest	6.782584e-01	0.169
R-HSA-196783	Coenzyme A biosynthesis	6.782584e-01	0.169
R-HSA-8856688	Golgi-to-ER retrograde transport	6.861395e-01	0.164
R-HSA-549127	SLC-mediated transport of organic cations	6.863732e-01	0.163
R-HSA-5689896	Ovarian tumor domain proteases	6.863732e-01	0.163
R-HSA-9711123	Cellular response to chemical stress	6.886584e-01	0.162
R-HSA-9659379	Sensory processing of sound	6.902470e-01	0.161
R-HSA-5617833	Cilium Assembly	6.904872e-01	0.161
R-HSA-9029569	NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu...	6.909909e-01	0.161
R-HSA-372708	p130Cas linkage to MAPK signaling for integrins	6.951831e-01	0.158
R-HSA-190840	Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane	6.951831e-01	0.158
R-HSA-174437	Removal of the Flap Intermediate from the C-strand	6.951831e-01	0.158
R-HSA-4641263	Regulation of FZD by ubiquitination	6.951831e-01	0.158
R-HSA-3229121	Glycogen storage diseases	6.951831e-01	0.158
R-HSA-139853	Elevation of cytosolic Ca2+ levels	6.951831e-01	0.158
R-HSA-5358606	Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)	6.951831e-01	0.158
R-HSA-164938	Nef-mediates down modulation of cell surface receptors by recruiting them to cla...	6.951831e-01	0.158
R-HSA-5358565	Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)	6.951831e-01	0.158
R-HSA-9768759	Regulation of NPAS4 gene expression	6.951831e-01	0.158
R-HSA-9909505	Modulation of host responses by IFN-stimulated genes	6.951831e-01	0.158
R-HSA-1660517	Synthesis of PIPs at the late endosome membrane	6.951831e-01	0.158
R-HSA-9820448	Developmental Cell Lineages of the Exocrine Pancreas	6.973901e-01	0.157
R-HSA-202131	Metabolism of nitric oxide: NOS3 activation and regulation	6.981254e-01	0.156
R-HSA-6785470	tRNA processing in the mitochondrion	6.981254e-01	0.156
R-HSA-5213460	RIPK1-mediated regulated necrosis	6.981254e-01	0.156
R-HSA-9958790	SLC-mediated transport of inorganic anions	6.981254e-01	0.156
R-HSA-352230	Amino acid transport across the plasma membrane	7.006087e-01	0.155
R-HSA-9614085	FOXO-mediated transcription	7.072147e-01	0.150
R-HSA-167200	Formation of HIV-1 elongation complex containing HIV-1 Tat	7.095102e-01	0.149
R-HSA-9725554	Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin	7.095102e-01	0.149
R-HSA-381771	Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)	7.095102e-01	0.149
R-HSA-201556	Signaling by ALK	7.095102e-01	0.149
R-HSA-9820965	Respiratory syncytial virus (RSV) genome replication, transcription and translat...	7.095102e-01	0.149
R-HSA-9845323	Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs)	7.099970e-01	0.149
R-HSA-983189	Kinesins	7.099970e-01	0.149
R-HSA-5651801	PCNA-Dependent Long Patch Base Excision Repair	7.112184e-01	0.148
R-HSA-190872	Transport of connexons to the plasma membrane	7.112184e-01	0.148
R-HSA-3928664	Ephrin signaling	7.112184e-01	0.148
R-HSA-73980	RNA Polymerase III Transcription Termination	7.112184e-01	0.148
R-HSA-5358508	Mismatch Repair	7.112184e-01	0.148
R-HSA-6804760	Regulation of TP53 Activity through Methylation	7.112184e-01	0.148
R-HSA-9679504	Translation of Replicase and Assembly of the Replication Transcription Complex	7.112184e-01	0.148
R-HSA-2029480	Fcgamma receptor (FCGR) dependent phagocytosis	7.134503e-01	0.147
R-HSA-8939902	Regulation of RUNX2 expression and activity	7.191572e-01	0.143
R-HSA-167246	Tat-mediated elongation of the HIV-1 transcript	7.205336e-01	0.142
R-HSA-167152	Formation of HIV elongation complex in the absence of HIV Tat	7.205336e-01	0.142
R-HSA-167169	HIV Transcription Elongation	7.205336e-01	0.142
R-HSA-8982491	Glycogen metabolism	7.205336e-01	0.142
R-HSA-8868766	rRNA processing in the mitochondrion	7.205336e-01	0.142
R-HSA-9009391	Extra-nuclear estrogen signaling	7.217426e-01	0.142
R-HSA-9820952	Respiratory Syncytial Virus Infection Pathway	7.243257e-01	0.140
R-HSA-1912420	Pre-NOTCH Processing in Golgi	7.264111e-01	0.139
R-HSA-5654710	PI-3K cascade:FGFR3	7.264111e-01	0.139
R-HSA-174048	APC/C:Cdc20 mediated degradation of Cyclin B	7.264111e-01	0.139
R-HSA-167242	Abortive elongation of HIV-1 transcript in the absence of Tat	7.264111e-01	0.139
R-HSA-110320	Translesion Synthesis by POLH	7.264111e-01	0.139
R-HSA-9754189	Germ layer formation at gastrulation	7.264111e-01	0.139
R-HSA-9856532	Mechanical load activates signaling by PIEZO1 and integrins in osteocytes	7.264111e-01	0.139
R-HSA-881907	Gastrin-CREB signalling pathway via PKC and MAPK	7.264111e-01	0.139
R-HSA-429958	mRNA decay by 3' to 5' exoribonuclease	7.264111e-01	0.139
R-HSA-449836	Other interleukin signaling	7.264111e-01	0.139
R-HSA-392517	Rap1 signalling	7.264111e-01	0.139
R-HSA-9694631	Maturation of nucleoprotein	7.264111e-01	0.139
R-HSA-9913635	Strand-asynchronous mitochondrial DNA replication	7.264111e-01	0.139
R-HSA-186797	Signaling by PDGF	7.280910e-01	0.138
R-HSA-2559580	Oxidative Stress Induced Senescence	7.288106e-01	0.137
R-HSA-1483255	PI Metabolism	7.288106e-01	0.137
R-HSA-442755	Activation of NMDA receptors and postsynaptic events	7.288106e-01	0.137
R-HSA-9694548	Maturation of spike protein	7.312022e-01	0.136
R-HSA-9711097	Cellular response to starvation	7.325391e-01	0.135
R-HSA-381119	Unfolded Protein Response (UPR)	7.363225e-01	0.133
R-HSA-5687128	MAPK6/MAPK4 signaling	7.384112e-01	0.132
R-HSA-9909620	Regulation of PD-L1(CD274) translation	7.408053e-01	0.130
R-HSA-1362277	Transcription of E2F targets under negative control by DREAM complex	7.408053e-01	0.130
R-HSA-5654720	PI-3K cascade:FGFR4	7.408053e-01	0.130
R-HSA-3322077	Glycogen synthesis	7.408053e-01	0.130
R-HSA-389513	Co-inhibition by CTLA4	7.408053e-01	0.130
R-HSA-5620922	BBSome-mediated cargo-targeting to cilium	7.408053e-01	0.130
R-HSA-9629569	Protein hydroxylation	7.408053e-01	0.130
R-HSA-1181150	Signaling by NODAL	7.408053e-01	0.130
R-HSA-373753	Nephrin family interactions	7.408053e-01	0.130
R-HSA-391903	Eicosanoid ligand-binding receptors	7.408053e-01	0.130
R-HSA-140875	Common Pathway of Fibrin Clot Formation	7.408053e-01	0.130
R-HSA-9615017	FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes	7.415227e-01	0.130
R-HSA-6811438	Intra-Golgi traffic	7.415227e-01	0.130
R-HSA-9664417	Leishmania phagocytosis	7.421829e-01	0.129
R-HSA-9664407	Parasite infection	7.421829e-01	0.129
R-HSA-9664422	FCGR3A-mediated phagocytosis	7.421829e-01	0.129
R-HSA-157118	Signaling by NOTCH	7.446283e-01	0.128
R-HSA-936837	Ion transport by P-type ATPases	7.452876e-01	0.128
R-HSA-8876198	RAB GEFs exchange GTP for GDP on RABs	7.458607e-01	0.127
R-HSA-9909615	Regulation of PD-L1(CD274) Post-translational modification	7.458607e-01	0.127
R-HSA-9927418	Developmental Lineage of Mammary Gland Luminal Epithelial Cells	7.515023e-01	0.124
R-HSA-73762	RNA Polymerase I Transcription Initiation	7.515023e-01	0.124
R-HSA-512988	Interleukin-3, Interleukin-5 and GM-CSF signaling	7.515023e-01	0.124
R-HSA-400508	Incretin synthesis, secretion, and inactivation	7.515023e-01	0.124
R-HSA-179409	APC-Cdc20 mediated degradation of Nek2A	7.544431e-01	0.122
R-HSA-450321	JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ...	7.544431e-01	0.122
R-HSA-69186	Lagging Strand Synthesis	7.544431e-01	0.122
R-HSA-9824594	Regulation of MITF-M-dependent genes involved in apoptosis	7.544431e-01	0.122
R-HSA-162594	Early Phase of HIV Life Cycle	7.544431e-01	0.122
R-HSA-9819196	Zygotic genome activation (ZGA)	7.544431e-01	0.122
R-HSA-196836	Vitamin C (ascorbate) metabolism	7.544431e-01	0.122
R-HSA-447115	Interleukin-12 family signaling	7.602721e-01	0.119
R-HSA-201681	TCF dependent signaling in response to WNT	7.607706e-01	0.119
R-HSA-1433557	Signaling by SCF-KIT	7.611482e-01	0.119
R-HSA-5654743	Signaling by FGFR4	7.611482e-01	0.119
R-HSA-2173789	TGF-beta receptor signaling activates SMADs	7.611482e-01	0.119
R-HSA-9692914	SARS-CoV-1-host interactions	7.622002e-01	0.118
R-HSA-9645723	Diseases of programmed cell death	7.672364e-01	0.115
R-HSA-450302	activated TAK1 mediates p38 MAPK activation	7.673641e-01	0.115
R-HSA-175474	Assembly Of The HIV Virion	7.673641e-01	0.115
R-HSA-9958863	SLC-mediated transport of amino acids	7.694410e-01	0.114
R-HSA-69231	Cyclin D associated events in G1	7.704680e-01	0.113
R-HSA-69236	G1 Phase	7.704680e-01	0.113
R-HSA-375280	Amine ligand-binding receptors	7.704680e-01	0.113
R-HSA-8864260	Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors	7.704680e-01	0.113
R-HSA-3371497	HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig...	7.770652e-01	0.110
R-HSA-5218859	Regulated Necrosis	7.770652e-01	0.110
R-HSA-5654741	Signaling by FGFR3	7.794691e-01	0.108
R-HSA-76071	RNA Polymerase III Transcription Initiation From Type 3 Promoter	7.796059e-01	0.108
R-HSA-9670439	Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT m...	7.796059e-01	0.108
R-HSA-9669938	Signaling by KIT in disease	7.796059e-01	0.108
R-HSA-189200	Cellular hexose transport	7.796059e-01	0.108
R-HSA-2173788	Downregulation of TGF-beta receptor signaling	7.796059e-01	0.108
R-HSA-9013507	NOTCH3 Activation and Transmission of Signal to the Nucleus	7.796059e-01	0.108
R-HSA-6807062	Cholesterol biosynthesis via lathosterol	7.796059e-01	0.108
R-HSA-9694676	Translation of Replicase and Assembly of the Replication Transcription Complex	7.796059e-01	0.108
R-HSA-112310	Neurotransmitter release cycle	7.806891e-01	0.108
R-HSA-73884	Base Excision Repair	7.806891e-01	0.108
R-HSA-174084	Autodegradation of Cdh1 by Cdh1:APC/C	7.881594e-01	0.103
R-HSA-389957	Prefoldin mediated transfer of substrate to CCT/TriC	7.912043e-01	0.102
R-HSA-8943723	Regulation of PTEN mRNA translation	7.912043e-01	0.102
R-HSA-9648895	Response of EIF2AK1 (HRI) to heme deficiency	7.912043e-01	0.102
R-HSA-77075	RNA Pol II CTD phosphorylation and interaction with CE	7.912043e-01	0.102
R-HSA-167160	RNA Pol II CTD phosphorylation and interaction with CE during HIV infection	7.912043e-01	0.102
R-HSA-164952	The role of Nef in HIV-1 replication and disease pathogenesis	7.912043e-01	0.102
R-HSA-9830674	Formation of the ureteric bud	7.912043e-01	0.102
R-HSA-982772	Growth hormone receptor signaling	7.912043e-01	0.102
R-HSA-1168372	Downstream signaling events of B Cell Receptor (BCR)	7.916917e-01	0.101
R-HSA-5632684	Hedgehog 'on' state	7.987004e-01	0.098
R-HSA-74752	Signaling by Insulin receptor	7.997027e-01	0.097
R-HSA-9821993	Replacement of protamines by nucleosomes in the male pronucleus	8.021929e-01	0.096
R-HSA-8963889	Assembly of active LPL and LIPC lipase complexes	8.021929e-01	0.096
R-HSA-9843745	Adipogenesis	8.037989e-01	0.095
R-HSA-9031628	NGF-stimulated transcription	8.046384e-01	0.094
R-HSA-69656	Cyclin A:Cdk2-associated events at S phase entry	8.055107e-01	0.094
R-HSA-69052	Switching of origins to a post-replicative state	8.121260e-01	0.090
R-HSA-5654695	PI-3K cascade:FGFR2	8.126038e-01	0.090
R-HSA-420029	Tight junction interactions	8.126038e-01	0.090
R-HSA-3214842	HDMs demethylate histones	8.126038e-01	0.090
R-HSA-3000157	Laminin interactions	8.126038e-01	0.090
R-HSA-5601884	PIWI-interacting RNA (piRNA) biogenesis	8.126038e-01	0.090
R-HSA-70221	Glycogen breakdown (glycogenolysis)	8.126038e-01	0.090
R-HSA-1266695	Interleukin-7 signaling	8.126038e-01	0.090
R-HSA-1852241	Organelle biogenesis and maintenance	8.166413e-01	0.088
R-HSA-674695	RNA Polymerase II Pre-transcription Events	8.185499e-01	0.087
R-HSA-1236394	Signaling by ERBB4	8.185499e-01	0.087
R-HSA-9917777	Epigenetic regulation by WDR5-containing histone modifying complexes	8.191683e-01	0.087
R-HSA-8874081	MET activates PTK2 signaling	8.224674e-01	0.085
R-HSA-2122948	Activated NOTCH1 Transmits Signal to the Nucleus	8.224674e-01	0.085
R-HSA-5689901	Metalloprotease DUBs	8.224674e-01	0.085
R-HSA-1855183	Synthesis of IP2, IP, and Ins in the cytosol	8.224674e-01	0.085
R-HSA-3295583	TRP channels	8.224674e-01	0.085
R-HSA-6781827	Transcription-Coupled Nucleotide Excision Repair (TC-NER)	8.247861e-01	0.084
R-HSA-212165	Epigenetic regulation of gene expression	8.262578e-01	0.083
R-HSA-1169091	Activation of NF-kappaB in B cells	8.272206e-01	0.082
R-HSA-1980143	Signaling by NOTCH1	8.308382e-01	0.080
R-HSA-73863	RNA Polymerase I Transcription Termination	8.318124e-01	0.080
R-HSA-8949613	Cristae formation	8.318124e-01	0.080
R-HSA-201451	Signaling by BMP	8.318124e-01	0.080
R-HSA-174414	Processive synthesis on the C-strand of the telomere	8.318124e-01	0.080
R-HSA-202427	Phosphorylation of CD3 and TCR zeta chains	8.318124e-01	0.080
R-HSA-5357956	TNFR1-induced NF-kappa-B signaling pathway	8.318124e-01	0.080
R-HSA-9841251	Mitochondrial unfolded protein response (UPRmt)	8.318124e-01	0.080
R-HSA-5655332	Signaling by FGFR3 in disease	8.318124e-01	0.080
R-HSA-75109	Triglyceride biosynthesis	8.318124e-01	0.080
R-HSA-1483213	Synthesis of PE	8.318124e-01	0.080
R-HSA-9006115	Signaling by NTRK2 (TRKB)	8.318124e-01	0.080
R-HSA-6803204	TP53 Regulates Transcription of Genes Involved in Cytochrome C Release	8.318124e-01	0.080
R-HSA-3858494	Beta-catenin independent WNT signaling	8.324489e-01	0.080
R-HSA-73772	RNA Polymerase I Promoter Escape	8.342095e-01	0.079
R-HSA-8866654	E3 ubiquitin ligases ubiquitinate target proteins	8.342095e-01	0.079
R-HSA-1592230	Mitochondrial biogenesis	8.343569e-01	0.079
R-HSA-9024446	NR1H2 and NR1H3-mediated signaling	8.367099e-01	0.077
R-HSA-9694635	Translation of Structural Proteins	8.367099e-01	0.077
R-HSA-190236	Signaling by FGFR	8.388950e-01	0.076
R-HSA-113418	Formation of the Early Elongation Complex	8.406661e-01	0.075
R-HSA-167158	Formation of the HIV-1 Early Elongation Complex	8.406661e-01	0.075
R-HSA-5205685	PINK1-PRKN Mediated Mitophagy	8.406661e-01	0.075
R-HSA-5654732	Negative regulation of FGFR3 signaling	8.406661e-01	0.075
R-HSA-380994	ATF4 activates genes in response to endoplasmic reticulum stress	8.406661e-01	0.075
R-HSA-5620971	Pyroptosis	8.406661e-01	0.075
R-HSA-174178	APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ...	8.409421e-01	0.075
R-HSA-5250924	B-WICH complex positively regulates rRNA expression	8.409421e-01	0.075
R-HSA-8948751	Regulation of PTEN stability and activity	8.409421e-01	0.075
R-HSA-432722	Golgi Associated Vesicle Biogenesis	8.409421e-01	0.075
R-HSA-948021	Transport to the Golgi and subsequent modification	8.419010e-01	0.075
R-HSA-72649	Translation initiation complex formation	8.474258e-01	0.072
R-HSA-69017	CDK-mediated phosphorylation and removal of Cdc6	8.474258e-01	0.072
R-HSA-5656169	Termination of translesion DNA synthesis	8.490541e-01	0.071
R-HSA-72086	mRNA Capping	8.490541e-01	0.071
R-HSA-5654708	Downstream signaling of activated FGFR3	8.490541e-01	0.071
R-HSA-418360	Platelet calcium homeostasis	8.490541e-01	0.071
R-HSA-5654733	Negative regulation of FGFR4 signaling	8.490541e-01	0.071
R-HSA-392154	Nitric oxide stimulates guanylate cyclase	8.490541e-01	0.071
R-HSA-9753281	Paracetamol ADME	8.536683e-01	0.069
R-HSA-456926	Thrombin signalling through proteinase activated receptors (PARs)	8.570011e-01	0.067
R-HSA-5654716	Downstream signaling of activated FGFR4	8.570011e-01	0.067
R-HSA-112311	Neurotransmitter clearance	8.570011e-01	0.067
R-HSA-9933387	RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression	8.570011e-01	0.067
R-HSA-72702	Ribosomal scanning and start codon recognition	8.596770e-01	0.066
R-HSA-389958	Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding	8.645301e-01	0.063
R-HSA-936440	Negative regulators of DDX58/IFIH1 signaling	8.645301e-01	0.063
R-HSA-9820960	Respiratory syncytial virus (RSV) attachment and entry	8.645301e-01	0.063
R-HSA-2129379	Molecules associated with elastic fibres	8.645301e-01	0.063
R-HSA-9833109	Evasion by RSV of host interferon responses	8.645301e-01	0.063
R-HSA-6782135	Dual incision in TC-NER	8.710219e-01	0.060
R-HSA-72662	Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub...	8.710219e-01	0.060
R-HSA-9833110	RSV-host interactions	8.714486e-01	0.060
R-HSA-1538133	G0 and Early G1	8.716632e-01	0.060
R-HSA-69190	DNA strand elongation	8.716632e-01	0.060
R-HSA-5688426	Deubiquitination	8.756977e-01	0.058
R-HSA-8979227	Triglyceride metabolism	8.763724e-01	0.057
R-HSA-2022090	Assembly of collagen fibrils and other multimeric structures	8.763724e-01	0.057
R-HSA-983169	Class I MHC mediated antigen processing & presentation	8.778972e-01	0.057
R-HSA-397014	Muscle contraction	8.779647e-01	0.057
R-HSA-9668328	Sealing of the nuclear envelope (NE) by ESCRT-III	8.784211e-01	0.056
R-HSA-397795	G-protein beta:gamma signalling	8.784211e-01	0.056
R-HSA-354192	Integrin signaling	8.784211e-01	0.056
R-HSA-1855204	Synthesis of IP3 and IP4 in the cytosol	8.784211e-01	0.056
R-HSA-9733709	Cardiogenesis	8.784211e-01	0.056
R-HSA-2644603	Signaling by NOTCH1 in Cancer	8.815176e-01	0.055
R-HSA-2644602	Signaling by NOTCH1 PEST Domain Mutants in Cancer	8.815176e-01	0.055
R-HSA-2894858	Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer	8.815176e-01	0.055
R-HSA-2644606	Constitutive Signaling by NOTCH1 PEST Domain Mutants	8.815176e-01	0.055
R-HSA-2894862	Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants	8.815176e-01	0.055
R-HSA-69239	Synthesis of DNA	8.835668e-01	0.054
R-HSA-1482788	Acyl chain remodelling of PC	8.848235e-01	0.053
R-HSA-199220	Vitamin B5 (pantothenate) metabolism	8.848235e-01	0.053
R-HSA-5223345	Miscellaneous transport and binding events	8.848235e-01	0.053
R-HSA-189483	Heme degradation	8.848235e-01	0.053
R-HSA-2672351	Stimuli-sensing channels	8.873794e-01	0.052
R-HSA-9679191	Potential therapeutics for SARS	8.895208e-01	0.051
R-HSA-390466	Chaperonin-mediated protein folding	8.904779e-01	0.050
R-HSA-9680350	Signaling by CSF1 (M-CSF) in myeloid cells	8.908891e-01	0.050
R-HSA-190861	Gap junction assembly	8.908891e-01	0.050
R-HSA-9927426	Developmental Lineage of Mammary Gland Alveolar Cells	8.908891e-01	0.050
R-HSA-1980145	Signaling by NOTCH2	8.908891e-01	0.050
R-HSA-349425	Autodegradation of the E3 ubiquitin ligase COP1	8.908891e-01	0.050
R-HSA-5654727	Negative regulation of FGFR2 signaling	8.908891e-01	0.050
R-HSA-110328	Recognition and association of DNA glycosylase with site containing an affected ...	8.908891e-01	0.050
R-HSA-69002	DNA Replication Pre-Initiation	8.910825e-01	0.050
R-HSA-176408	Regulation of APC/C activators between G1/S and early anaphase	8.912187e-01	0.050
R-HSA-8852276	The role of GTSE1 in G2/M progression after G2 checkpoint	8.912187e-01	0.050
R-HSA-1280218	Adaptive Immune System	8.944377e-01	0.048
R-HSA-6790901	rRNA modification in the nucleus and cytosol	8.957878e-01	0.048
R-HSA-69615	G1/S DNA Damage Checkpoints	8.957878e-01	0.048
R-HSA-174113	SCF-beta-TrCP mediated degradation of Emi1	8.966356e-01	0.047
R-HSA-5654696	Downstream signaling of activated FGFR2	8.966356e-01	0.047
R-HSA-1482839	Acyl chain remodelling of PE	8.966356e-01	0.047
R-HSA-381042	PERK regulates gene expression	8.966356e-01	0.047
R-HSA-3296482	Defects in vitamin and cofactor metabolism	8.966356e-01	0.047
R-HSA-9678108	SARS-CoV-1 Infection	8.981817e-01	0.047
R-HSA-927802	Nonsense-Mediated Decay (NMD)	9.015593e-01	0.045
R-HSA-975957	Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)	9.015593e-01	0.045
R-HSA-163560	Triglyceride catabolism	9.020799e-01	0.045
R-HSA-140877	Formation of Fibrin Clot (Clotting Cascade)	9.020799e-01	0.045
R-HSA-202424	Downstream TCR signaling	9.020916e-01	0.045
R-HSA-427359	SIRT1 negatively regulates rRNA expression	9.072376e-01	0.042
R-HSA-933541	TRAF6 mediated IRF7 activation	9.072376e-01	0.042
R-HSA-4641258	Degradation of DVL	9.072376e-01	0.042
R-HSA-6782315	tRNA modification in the nucleus and cytosol	9.084450e-01	0.042
R-HSA-1566948	Elastic fibre formation	9.121240e-01	0.040
R-HSA-983705	Signaling by the B Cell Receptor (BCR)	9.125577e-01	0.040
R-HSA-391251	Protein folding	9.125823e-01	0.040
R-HSA-9772573	Late SARS-CoV-2 Infection Events	9.125823e-01	0.040
R-HSA-983695	Antigen activates B Cell Receptor (BCR) leading to generation of second messenge...	9.158455e-01	0.038
R-HSA-68867	Assembly of the pre-replicative complex	9.158455e-01	0.038
R-HSA-8936459	RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun...	9.160679e-01	0.038
R-HSA-167172	Transcription of the HIV genome	9.160679e-01	0.038
R-HSA-69541	Stabilization of p53	9.167533e-01	0.038
R-HSA-71336	Pentose phosphate pathway	9.167533e-01	0.038
R-HSA-8964043	Plasma lipoprotein clearance	9.167533e-01	0.038
R-HSA-909733	Interferon alpha/beta signaling	9.170516e-01	0.038
R-HSA-1474290	Collagen formation	9.189975e-01	0.037
R-HSA-9670095	Inhibition of DNA recombination at telomere	9.211390e-01	0.036
R-HSA-71240	Tryptophan catabolism	9.211390e-01	0.036
R-HSA-1251985	Nuclear signaling by ERBB4	9.211390e-01	0.036
R-HSA-451927	Interleukin-2 family signaling	9.211390e-01	0.036
R-HSA-2980736	Peptide hormone metabolism	9.226126e-01	0.035
R-HSA-204005	COPII-mediated vesicle transport	9.230915e-01	0.035
R-HSA-75105	Fatty acyl-CoA biosynthesis	9.230915e-01	0.035
R-HSA-5625886	Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene...	9.252939e-01	0.034
R-HSA-110313	Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa...	9.252939e-01	0.034
R-HSA-5676590	NIK-->noncanonical NF-kB signaling	9.252939e-01	0.034
R-HSA-9607240	FLT3 Signaling	9.252939e-01	0.034
R-HSA-174143	APC/C-mediated degradation of cell cycle proteins	9.263920e-01	0.033
R-HSA-453276	Regulation of mitotic cell cycle	9.263920e-01	0.033
R-HSA-5250913	Positive epigenetic regulation of rRNA expression	9.263920e-01	0.033
R-HSA-8978934	Metabolism of cofactors	9.263920e-01	0.033
R-HSA-5607764	CLEC7A (Dectin-1) signaling	9.278172e-01	0.033
R-HSA-5610783	Degradation of GLI2 by the proteasome	9.292301e-01	0.032
R-HSA-5610785	GLI3 is processed to GLI3R by the proteasome	9.292301e-01	0.032
R-HSA-5610780	Degradation of GLI1 by the proteasome	9.292301e-01	0.032
R-HSA-9932298	Degradation of CRY and PER proteins	9.292301e-01	0.032
R-HSA-174417	Telomere C-strand (Lagging Strand) Synthesis	9.292301e-01	0.032
R-HSA-442660	SLC-mediated transport of neurotransmitters	9.292301e-01	0.032
R-HSA-9683701	Translation of Structural Proteins	9.292301e-01	0.032
R-HSA-499943	Interconversion of nucleotide di- and triphosphates	9.295586e-01	0.032
R-HSA-199992	trans-Golgi Network Vesicle Budding	9.295586e-01	0.032
R-HSA-983712	Ion channel transport	9.314135e-01	0.031
R-HSA-9824443	Parasitic Infection Pathways	9.323532e-01	0.030
R-HSA-9658195	Leishmania infection	9.323532e-01	0.030
R-HSA-379716	Cytosolic tRNA aminoacylation	9.329591e-01	0.030
R-HSA-110329	Cleavage of the damaged pyrimidine	9.329591e-01	0.030
R-HSA-73928	Depyrimidination	9.329591e-01	0.030
R-HSA-9013694	Signaling by NOTCH4	9.355093e-01	0.029
R-HSA-192105	Synthesis of bile acids and bile salts	9.357474e-01	0.029
R-HSA-8852135	Protein ubiquitination	9.383029e-01	0.028
R-HSA-6809371	Formation of the cornified envelope	9.395327e-01	0.027
R-HSA-3214858	RMTs methylate histone arginines	9.398387e-01	0.027
R-HSA-2142691	Synthesis of Leukotrienes (LT) and Eoxins (EX)	9.398387e-01	0.027
R-HSA-196741	Cobalamin (Cbl, vitamin B12) transport and metabolism	9.398387e-01	0.027
R-HSA-453279	Mitotic G1 phase and G1/S transition	9.406753e-01	0.027
R-HSA-5689603	UCH proteinases	9.409814e-01	0.026
R-HSA-73854	RNA Polymerase I Promoter Clearance	9.409814e-01	0.026
R-HSA-606279	Deposition of new CENPA-containing nucleosomes at the centromere	9.430093e-01	0.025
R-HSA-774815	Nucleosome assembly	9.430093e-01	0.025
R-HSA-5607761	Dectin-1 mediated noncanonical NF-kB signaling	9.430093e-01	0.025
R-HSA-69601	Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A	9.430093e-01	0.025
R-HSA-69613	p53-Independent G1/S DNA Damage Checkpoint	9.430093e-01	0.025
R-HSA-6783310	Fanconi Anemia Pathway	9.430093e-01	0.025
R-HSA-76009	Platelet Aggregation (Plug Formation)	9.430093e-01	0.025
R-HSA-9841922	MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi...	9.437077e-01	0.025
R-HSA-9851695	Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes	9.437077e-01	0.025
R-HSA-9818564	Epigenetic regulation of gene expression by MLL3 and MLL4 complexes	9.437077e-01	0.025
R-HSA-69206	G1/S Transition	9.437077e-01	0.025
R-HSA-383280	Nuclear Receptor transcription pathway	9.460106e-01	0.024
R-HSA-73864	RNA Polymerase I Transcription	9.460106e-01	0.024
R-HSA-4086400	PCP/CE pathway	9.460106e-01	0.024
R-HSA-191273	Cholesterol biosynthesis	9.460106e-01	0.024
R-HSA-6783783	Interleukin-10 signaling	9.460106e-01	0.024
R-HSA-216083	Integrin cell surface interactions	9.460106e-01	0.024
R-HSA-6781823	Formation of TC-NER Pre-Incision Complex	9.460130e-01	0.024
R-HSA-9861718	Regulation of pyruvate metabolism	9.460130e-01	0.024
R-HSA-114608	Platelet degranulation	9.476178e-01	0.023
R-HSA-174154	APC/C:Cdc20 mediated degradation of Securin	9.488586e-01	0.023
R-HSA-1483191	Synthesis of PC	9.488586e-01	0.023
R-HSA-9833482	PKR-mediated signaling	9.506299e-01	0.022
R-HSA-5250941	Negative epigenetic regulation of rRNA expression	9.506299e-01	0.022
R-HSA-5654738	Signaling by FGFR2	9.506299e-01	0.022
R-HSA-8963899	Plasma lipoprotein remodeling	9.515543e-01	0.022
R-HSA-69306	DNA Replication	9.530828e-01	0.021
R-HSA-69563	p53-Dependent G1 DNA Damage Response	9.541081e-01	0.020
R-HSA-69580	p53-Dependent G1/S DNA damage checkpoint	9.541081e-01	0.020
R-HSA-380108	Chemokine receptors bind chemokines	9.541081e-01	0.020
R-HSA-195721	Signaling by WNT	9.559758e-01	0.020
R-HSA-1989781	PPARA activates gene expression	9.561664e-01	0.019
R-HSA-5655253	Signaling by FGFR2 in disease	9.565275e-01	0.019
R-HSA-9748787	Azathioprine ADME	9.565275e-01	0.019
R-HSA-9707564	Cytoprotection by HMOX1	9.568579e-01	0.019
R-HSA-6798695	Neutrophil degranulation	9.577193e-01	0.019
R-HSA-1234176	Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha	9.588194e-01	0.018
R-HSA-400206	Regulation of lipid metabolism by PPARalpha	9.590640e-01	0.018
R-HSA-76005	Response to elevated platelet cytosolic Ca2+	9.594232e-01	0.018
R-HSA-194068	Bile acid and bile salt metabolism	9.600678e-01	0.018
R-HSA-174184	Cdc20:Phospho-APC/C mediated degradation of Cyclin A	9.609906e-01	0.017
R-HSA-68949	Orc1 removal from chromatin	9.609906e-01	0.017
R-HSA-877300	Interferon gamma signaling	9.617853e-01	0.017
R-HSA-179419	APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th...	9.630475e-01	0.016
R-HSA-375276	Peptide ligand-binding receptors	9.646993e-01	0.016
R-HSA-9754678	SARS-CoV-2 modulates host translation machinery	9.649960e-01	0.015
R-HSA-73929	Base-Excision Repair, AP Site Formation	9.649960e-01	0.015
R-HSA-112316	Neuronal System	9.668354e-01	0.015
R-HSA-176409	APC/C:Cdc20 mediated degradation of mitotic proteins	9.668419e-01	0.015
R-HSA-6811436	COPI-independent Golgi-to-ER retrograde traffic	9.668419e-01	0.015
R-HSA-176814	Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins	9.685906e-01	0.014
R-HSA-5578775	Ion homeostasis	9.685906e-01	0.014
R-HSA-3299685	Detoxification of Reactive Oxygen Species	9.685906e-01	0.014
R-HSA-1236974	ER-Phagosome pathway	9.685975e-01	0.014
R-HSA-9772572	Early SARS-CoV-2 Infection Events	9.718164e-01	0.012
R-HSA-975956	Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)	9.726261e-01	0.012
R-HSA-168256	Immune System	9.731448e-01	0.012
R-HSA-9033241	Peroxisomal protein import	9.733030e-01	0.012
R-HSA-180786	Extension of Telomeres	9.733030e-01	0.012
R-HSA-174824	Plasma lipoprotein assembly, remodeling, and clearance	9.738546e-01	0.012
R-HSA-8873719	RAB geranylgeranylation	9.747113e-01	0.011
R-HSA-379724	tRNA Aminoacylation	9.747113e-01	0.011
R-HSA-977443	GABA receptor activation	9.747113e-01	0.011
R-HSA-9824446	Viral Infection Pathways	9.750987e-01	0.011
R-HSA-5621481	C-type lectin receptors (CLRs)	9.757887e-01	0.011
R-HSA-73886	Chromosome Maintenance	9.765292e-01	0.010
R-HSA-5689880	Ub-specific processing proteases	9.774610e-01	0.010
R-HSA-112315	Transmission across Chemical Synapses	9.775357e-01	0.010
R-HSA-2132295	MHC class II antigen presentation	9.784005e-01	0.009
R-HSA-157579	Telomere Maintenance	9.801797e-01	0.009
R-HSA-1234174	Cellular response to hypoxia	9.807146e-01	0.008
R-HSA-8957275	Post-translational protein phosphorylation	9.810784e-01	0.008
R-HSA-422356	Regulation of insulin secretion	9.810784e-01	0.008
R-HSA-9010553	Regulation of expression of SLITs and ROBOs	9.816706e-01	0.008
R-HSA-196807	Nicotinate metabolism	9.826963e-01	0.008
R-HSA-5610787	Hedgehog 'off' state	9.827585e-01	0.008
R-HSA-382556	ABC-family proteins mediated transport	9.827585e-01	0.008
R-HSA-1650814	Collagen biosynthesis and modifying enzymes	9.836096e-01	0.007
R-HSA-71387	Metabolism of carbohydrates and carbohydrate derivatives	9.848067e-01	0.007
R-HSA-9843940	Regulation of endogenous retroelements by KRAB-ZFP proteins	9.852941e-01	0.006
R-HSA-69202	Cyclin E associated events during G1/S transition	9.852941e-01	0.006
R-HSA-9840310	Glycosphingolipid catabolism	9.852941e-01	0.006
R-HSA-9633012	Response of EIF2AK4 (GCN2) to amino acid deficiency	9.856953e-01	0.006
R-HSA-112314	Neurotransmitter receptors and postsynaptic signal transmission	9.858687e-01	0.006
R-HSA-3000178	ECM proteoglycans	9.860703e-01	0.006
R-HSA-427413	NoRC negatively regulates rRNA expression	9.860703e-01	0.006
R-HSA-3906995	Diseases associated with O-glycosylation of proteins	9.860703e-01	0.006
R-HSA-975634	Retinoid metabolism and transport	9.860703e-01	0.006
R-HSA-189445	Metabolism of porphyrins	9.860703e-01	0.006
R-HSA-163125	Post-translational modification: synthesis of GPI-anchored proteins	9.863498e-01	0.006
R-HSA-5663084	Diseases of carbohydrate metabolism	9.875022e-01	0.005
R-HSA-418346	Platelet homeostasis	9.875724e-01	0.005
R-HSA-1483257	Phospholipid metabolism	9.880220e-01	0.005
R-HSA-1799339	SRP-dependent cotranslational protein targeting to membrane	9.881431e-01	0.005
R-HSA-1222556	ROS and RNS production in phagocytes	9.881620e-01	0.005
R-HSA-156827	L13a-mediated translational silencing of Ceruloplasmin expression	9.886882e-01	0.005
R-HSA-72706	GTP hydrolysis and joining of the 60S ribosomal subunit	9.886882e-01	0.005
R-HSA-1236975	Antigen processing-Cross presentation	9.886882e-01	0.005
R-HSA-8957322	Metabolism of steroids	9.893361e-01	0.005
R-HSA-5358351	Signaling by Hedgehog	9.899166e-01	0.004
R-HSA-1474244	Extracellular matrix organization	9.913989e-01	0.004
R-HSA-381426	Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l...	9.918754e-01	0.004
R-HSA-2151201	Transcriptional activation of mitochondrial biogenesis	9.919026e-01	0.004
R-HSA-6806667	Metabolism of fat-soluble vitamins	9.919026e-01	0.004
R-HSA-428157	Sphingolipid metabolism	9.920003e-01	0.003
R-HSA-196849	Metabolism of water-soluble vitamins and cofactors	9.925641e-01	0.003
R-HSA-5668541	TNFR2 non-canonical NF-kB pathway	9.927355e-01	0.003
R-HSA-72737	Cap-dependent Translation Initiation	9.929552e-01	0.003
R-HSA-72613	Eukaryotic Translation Initiation	9.929552e-01	0.003
R-HSA-416476	G alpha (q) signalling events	9.941234e-01	0.003
R-HSA-163841	Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation	9.941532e-01	0.003
R-HSA-70268	Pyruvate metabolism	9.944622e-01	0.002
R-HSA-9609507	Protein localization	9.949713e-01	0.002
R-HSA-1643685	Disease	9.952061e-01	0.002
R-HSA-9954714	PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA	9.955433e-01	0.002
R-HSA-76002	Platelet activation, signaling and aggregation	9.958795e-01	0.002
R-HSA-156842	Eukaryotic Translation Elongation	9.960019e-01	0.002
R-HSA-2029481	FCGR activation	9.962133e-01	0.002
R-HSA-8951664	Neddylation	9.964530e-01	0.002
R-HSA-9954716	ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri...	9.966031e-01	0.001
R-HSA-5576891	Cardiac conduction	9.968847e-01	0.001
R-HSA-5389840	Mitochondrial translation elongation	9.969528e-01	0.001
R-HSA-5368286	Mitochondrial translation initiation	9.972666e-01	0.001
R-HSA-1483206	Glycerophospholipid biosynthesis	9.977826e-01	0.001
R-HSA-9948299	Ribosome-associated quality control	9.978867e-01	0.001
R-HSA-9937383	Mitochondrial ribosome-associated quality control	9.979169e-01	0.001
R-HSA-6805567	Keratinization	9.981280e-01	0.001
R-HSA-2871837	FCERI mediated NF-kB activation	9.984982e-01	0.001
R-HSA-5419276	Mitochondrial translation termination	9.985762e-01	0.001
R-HSA-6803157	Antimicrobial peptides	9.987229e-01	0.001
R-HSA-196854	Metabolism of vitamins and cofactors	9.988031e-01	0.001
R-HSA-373076	Class A/1 (Rhodopsin-like receptors)	9.989446e-01	0.000
R-HSA-72312	rRNA processing	9.993889e-01	0.000
R-HSA-1660662	Glycosphingolipid metabolism	9.994037e-01	0.000
R-HSA-977606	Regulation of Complement cascade	9.994652e-01	0.000
R-HSA-9664323	FCGR3A-mediated IL10 synthesis	9.995204e-01	0.000
R-HSA-9824439	Bacterial Infection Pathways	9.995464e-01	0.000
R-HSA-425407	SLC-mediated transmembrane transport	9.996492e-01	0.000
R-HSA-1474228	Degradation of the extracellular matrix	9.996724e-01	0.000
R-HSA-5663205	Infectious disease	9.997267e-01	0.000
R-HSA-5368287	Mitochondrial translation	9.997763e-01	0.000
R-HSA-109582	Hemostasis	9.998090e-01	0.000
R-HSA-168249	Innate Immune System	9.998138e-01	0.000
R-HSA-8868773	rRNA processing in the nucleus and cytosol	9.998387e-01	0.000
R-HSA-166658	Complement cascade	9.998553e-01	0.000
R-HSA-446203	Asparagine N-linked glycosylation	9.998622e-01	0.000
R-HSA-2187338	Visual phototransduction	9.998703e-01	0.000
R-HSA-2173782	Binding and Uptake of Ligands by Scavenger Receptors	9.998899e-01	0.000
R-HSA-72766	Translation	9.998944e-01	0.000
R-HSA-2142753	Arachidonate metabolism	9.999012e-01	0.000
R-HSA-202733	Cell surface interactions at the vascular wall	9.999031e-01	0.000
R-HSA-597592	Post-translational protein modification	9.999202e-01	0.000
R-HSA-2454202	Fc epsilon receptor (FCERI) signaling	9.999242e-01	0.000
R-HSA-388396	GPCR downstream signalling	9.999439e-01	0.000
R-HSA-2408522	Selenoamino acid metabolism	9.999487e-01	0.000
R-HSA-6791226	Major pathway of rRNA processing in the nucleolus and cytosol	9.999650e-01	0.000
R-HSA-9748784	Drug ADME	9.999663e-01	0.000
R-HSA-418555	G alpha (s) signalling events	9.999668e-01	0.000
R-HSA-9664433	Leishmania parasite growth and survival	9.999703e-01	0.000
R-HSA-9662851	Anti-inflammatory response favouring Leishmania parasite infection	9.999703e-01	0.000
R-HSA-611105	Respiratory electron transport	9.999774e-01	0.000
R-HSA-418594	G alpha (i) signalling events	9.999781e-01	0.000
R-HSA-198933	Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	9.999807e-01	0.000
R-HSA-3781865	Diseases of glycosylation	9.999837e-01	0.000
R-HSA-15869	Metabolism of nucleotides	9.999865e-01	0.000
R-HSA-372790	Signaling by GPCR	9.999962e-01	0.000
R-HSA-8978868	Fatty acid metabolism	9.999989e-01	0.000
R-HSA-500792	GPCR ligand binding	9.999994e-01	0.000
R-HSA-211945	Phase I - Functionalization of compounds	9.999999e-01	0.000
R-HSA-1428517	Aerobic respiration and respiratory electron transport	9.999999e-01	0.000
R-HSA-382551	Transport of small molecules	1.000000e+00	0.000
R-HSA-5668914	Diseases of metabolism	1.000000e+00	0.000
R-HSA-392499	Metabolism of proteins	1.000000e+00	0.000
R-HSA-556833	Metabolism of lipids	1.000000e+00	0.000
R-HSA-211859	Biological oxidations	1.000000e+00	0.000
R-HSA-71291	Metabolism of amino acids and derivatives	1.000000e+00	0.000
R-HSA-1430728	Metabolism	1.000000e+00	-0.000
R-HSA-9709957	Sensory Perception	1.000000e+00	-0.000

Download

kinase	JSD_mean	pearson_surrounding	kinase_max_IC_position	max_position_JSD
CLK3	0.900	0.366	1	0.857
COT	0.898	0.274	2	0.888
CDC7	0.888	0.186	1	0.858
MOS	0.887	0.277	1	0.869
PIM3	0.886	0.204	-3	0.873
GRK1	0.885	0.326	-2	0.853
NDR2	0.882	0.161	-3	0.871
RSK2	0.881	0.231	-3	0.813
MTOR	0.879	0.094	1	0.788
CLK2	0.879	0.348	-3	0.803
SRPK1	0.878	0.199	-3	0.801
KIS	0.877	0.196	1	0.744
SKMLCK	0.876	0.207	-2	0.904
CAMK1B	0.875	0.126	-3	0.882
IKKB	0.874	0.009	-2	0.773
PIM1	0.874	0.191	-3	0.829
PRPK	0.874	-0.071	-1	0.884
CDKL1	0.873	0.133	-3	0.836
CAMK2G	0.873	0.085	2	0.826
NLK	0.873	0.108	1	0.856
RAF1	0.872	0.000	1	0.819
P90RSK	0.872	0.163	-3	0.816
HIPK4	0.872	0.162	1	0.830
GRK6	0.872	0.223	1	0.841
GRK5	0.871	0.104	-3	0.871
ATR	0.871	0.053	1	0.820
BMPR1B	0.870	0.270	1	0.844
GRK7	0.869	0.255	1	0.775
CAMK2A	0.869	0.235	2	0.826
RSK4	0.869	0.226	-3	0.794
NDR1	0.869	0.077	-3	0.860
DSTYK	0.869	0.001	2	0.901
ERK5	0.868	0.068	1	0.827
CDKL5	0.867	0.115	-3	0.828
PRKD1	0.867	0.095	-3	0.844
CAMK2B	0.867	0.195	2	0.802
DYRK2	0.867	0.198	1	0.765
PDHK4	0.866	-0.180	1	0.834
PRKD2	0.866	0.128	-3	0.803
ICK	0.866	0.146	-3	0.866
CLK4	0.865	0.215	-3	0.816
BMPR2	0.865	-0.128	-2	0.904
CAMLCK	0.865	0.096	-2	0.890
SRPK2	0.865	0.159	-3	0.728
AURC	0.865	0.151	-2	0.715
DAPK2	0.865	0.123	-3	0.884
RSK3	0.865	0.118	-3	0.803
MST4	0.865	0.049	2	0.869
NUAK2	0.865	0.064	-3	0.873
PKACG	0.865	0.121	-2	0.799
GCN2	0.864	-0.188	2	0.813
PKN3	0.864	0.036	-3	0.849
CDK1	0.864	0.188	1	0.714
RIPK3	0.864	-0.004	3	0.712
NIK	0.864	0.028	-3	0.889
P70S6KB	0.864	0.117	-3	0.828
LATS1	0.864	0.209	-3	0.876
GSK3A	0.864	0.372	4	0.671
PRKX	0.864	0.230	-3	0.741
PKN2	0.864	0.073	-3	0.859
LATS2	0.864	0.067	-5	0.797
MAPKAPK2	0.863	0.124	-3	0.768
IKKA	0.863	0.031	-2	0.761
WNK1	0.863	0.016	-2	0.910
CAMK2D	0.863	0.076	-3	0.850
MSK1	0.862	0.194	-3	0.785
TBK1	0.862	-0.135	1	0.700
SRPK3	0.862	0.139	-3	0.774
PKACB	0.862	0.182	-2	0.731
CHAK2	0.861	-0.009	-1	0.872
IKKE	0.861	-0.114	1	0.698
MLK1	0.861	-0.050	2	0.823
GRK4	0.860	0.052	-2	0.868
GSK3B	0.860	0.333	4	0.665
DLK	0.859	0.063	1	0.819
CLK1	0.859	0.196	-3	0.788
PASK	0.859	0.334	-3	0.887
FAM20C	0.859	0.079	2	0.608
HIPK2	0.859	0.206	1	0.690
MSK2	0.859	0.105	-3	0.786
TGFBR2	0.858	-0.058	-2	0.824
JNK2	0.858	0.190	1	0.689
PKCD	0.858	0.044	2	0.795
NEK6	0.858	-0.101	-2	0.875
AMPKA1	0.857	0.011	-3	0.874
HUNK	0.857	-0.092	2	0.834
TGFBR1	0.857	0.124	-2	0.829
ULK2	0.857	-0.243	2	0.785
MAPKAPK3	0.857	0.032	-3	0.801
JNK3	0.856	0.170	1	0.717
DYRK4	0.856	0.222	1	0.700
MARK4	0.856	-0.048	4	0.808
NEK7	0.856	-0.175	-3	0.833
CDK8	0.855	0.082	1	0.725
HIPK1	0.855	0.190	1	0.777
ALK4	0.855	0.077	-2	0.856
PDHK1	0.855	-0.285	1	0.810
PAK1	0.854	0.065	-2	0.830
CDK18	0.854	0.147	1	0.677
ACVR2B	0.854	0.147	-2	0.820
ATM	0.854	0.015	1	0.761
MYLK4	0.853	0.118	-2	0.822
PLK1	0.853	0.049	-2	0.827
MASTL	0.853	-0.181	-2	0.843
CK1E	0.852	0.162	-3	0.654
AMPKA2	0.852	0.022	-3	0.848
GRK2	0.852	0.116	-2	0.751
CDK7	0.852	0.083	1	0.737
TSSK2	0.851	-0.010	-5	0.868
RIPK1	0.851	-0.108	1	0.786
CDK19	0.851	0.089	1	0.692
MLK3	0.851	-0.024	2	0.753
ALK2	0.851	0.116	-2	0.842
AKT2	0.851	0.136	-3	0.743
ACVR2A	0.851	0.104	-2	0.806
CAMK4	0.850	-0.015	-3	0.845
AURA	0.850	0.113	-2	0.685
ANKRD3	0.850	-0.111	1	0.823
BMPR1A	0.850	0.187	1	0.817
CDK5	0.850	0.112	1	0.752
AURB	0.850	0.094	-2	0.712
PKCB	0.850	0.038	2	0.746
CDK13	0.850	0.091	1	0.711
P38B	0.850	0.157	1	0.700
BCKDK	0.849	-0.197	-1	0.815
DRAK1	0.849	0.124	1	0.797
PKR	0.849	-0.004	1	0.815
TSSK1	0.848	-0.000	-3	0.890
PKCG	0.848	0.019	2	0.747
MLK2	0.848	-0.143	2	0.824
ULK1	0.847	-0.231	-3	0.791
P38A	0.847	0.119	1	0.758
P38G	0.847	0.140	1	0.628
DNAPK	0.847	0.072	1	0.693
PKCA	0.847	0.027	2	0.736
PIM2	0.847	0.114	-3	0.787
PKG2	0.847	0.090	-2	0.732
CDK17	0.846	0.124	1	0.632
MNK1	0.846	0.058	-2	0.843
PAK3	0.846	-0.013	-2	0.825
PRKD3	0.846	0.047	-3	0.784
MEK1	0.846	-0.068	2	0.854
MNK2	0.846	0.024	-2	0.834
CK1D	0.846	0.173	-3	0.605
WNK3	0.846	-0.276	1	0.781
ERK1	0.846	0.118	1	0.690
YSK4	0.845	-0.056	1	0.749
CDK3	0.845	0.132	1	0.650
NEK9	0.845	-0.224	2	0.837
CDK10	0.845	0.175	1	0.703
NIM1	0.845	-0.102	3	0.730
DYRK1A	0.845	0.133	1	0.780
IRE1	0.845	-0.121	1	0.767
CK2A2	0.845	0.190	1	0.755
TTBK2	0.845	-0.162	2	0.705
QSK	0.845	-0.005	4	0.776
SGK3	0.844	0.086	-3	0.797
MLK4	0.844	-0.043	2	0.735
DYRK3	0.844	0.167	1	0.775
VRK2	0.843	-0.151	1	0.851
CDK14	0.843	0.139	1	0.714
CDK12	0.843	0.095	1	0.687
PLK3	0.843	-0.011	2	0.792
CDK2	0.843	0.053	1	0.779
CK1A2	0.843	0.166	-3	0.608
DYRK1B	0.843	0.146	1	0.719
CAMK1G	0.842	0.056	-3	0.796
GRK3	0.842	0.126	-2	0.714
SMG1	0.842	-0.034	1	0.770
MST3	0.842	0.085	2	0.857
TLK2	0.842	-0.044	1	0.773
PAK2	0.842	-0.010	-2	0.816
PKCH	0.841	-0.011	2	0.726
PKCZ	0.841	-0.030	2	0.782
PKACA	0.841	0.136	-2	0.679
MELK	0.841	-0.043	-3	0.829
PAK6	0.841	0.051	-2	0.749
NUAK1	0.841	-0.037	-3	0.819
PRP4	0.841	0.076	-3	0.774
ERK2	0.840	0.077	1	0.732
MEKK3	0.840	0.002	1	0.782
BRSK1	0.840	-0.018	-3	0.822
CDK9	0.840	0.062	1	0.716
CK2A1	0.840	0.216	1	0.740
QIK	0.840	-0.111	-3	0.851
DCAMKL1	0.840	0.049	-3	0.823
SIK	0.840	-0.013	-3	0.797
GAK	0.840	0.186	1	0.829
MARK3	0.839	-0.009	4	0.739
P38D	0.839	0.150	1	0.634
HIPK3	0.839	0.110	1	0.758
CDK16	0.838	0.131	1	0.646
JNK1	0.837	0.149	1	0.682
PHKG1	0.837	-0.086	-3	0.853
CK1G1	0.836	0.082	-3	0.643
SMMLCK	0.836	0.067	-3	0.841
DAPK1	0.835	0.169	-3	0.828
DAPK3	0.835	0.133	-3	0.840
IRE2	0.835	-0.144	2	0.742
TAO3	0.835	0.009	1	0.775
MAK	0.834	0.204	-2	0.782
CHAK1	0.834	-0.183	2	0.767
BRAF	0.834	-0.094	-4	0.850
CHK1	0.834	-0.060	-3	0.830
AKT1	0.834	0.095	-3	0.756
NEK2	0.833	-0.181	2	0.813
MARK2	0.833	-0.066	4	0.700
MEK5	0.833	-0.195	2	0.832
P70S6K	0.833	0.055	-3	0.743
BRSK2	0.832	-0.106	-3	0.834
MAPKAPK5	0.831	-0.073	-3	0.744
GCK	0.831	0.107	1	0.791
MEKK2	0.831	-0.112	2	0.804
MPSK1	0.830	0.022	1	0.769
ZAK	0.830	-0.150	1	0.754
MARK1	0.830	-0.068	4	0.755
DCAMKL2	0.829	-0.013	-3	0.838
CAMK1D	0.829	0.062	-3	0.732
TLK1	0.829	-0.111	-2	0.851
PERK	0.829	-0.199	-2	0.859
NEK5	0.828	-0.153	1	0.793
SGK1	0.828	0.133	-3	0.667
SNRK	0.828	-0.205	2	0.685
MEKK1	0.827	-0.220	1	0.771
PLK4	0.827	-0.166	2	0.638
PKCE	0.827	0.053	2	0.730
WNK4	0.827	-0.149	-2	0.897
PLK2	0.826	0.063	-3	0.779
PINK1	0.826	-0.204	1	0.829
NEK11	0.825	-0.107	1	0.768
SSTK	0.825	-0.046	4	0.760
PKCT	0.825	-0.047	2	0.733
AKT3	0.824	0.111	-3	0.685
HPK1	0.824	0.071	1	0.776
MOK	0.823	0.148	1	0.787
TAK1	0.823	0.037	1	0.800
LKB1	0.823	-0.079	-3	0.825
PKCI	0.823	-0.030	2	0.750
HRI	0.823	-0.281	-2	0.863
ERK7	0.823	0.027	2	0.560
MRCKA	0.822	0.105	-3	0.788
IRAK4	0.822	-0.183	1	0.764
ROCK2	0.821	0.107	-3	0.823
PAK5	0.821	0.005	-2	0.689
NEK8	0.820	-0.173	2	0.820
CAMKK1	0.820	-0.175	-2	0.782
MST2	0.820	-0.055	1	0.783
PAK4	0.820	0.028	-2	0.696
PDHK3_TYR	0.820	0.357	4	0.897
TAO2	0.819	-0.132	2	0.850
PDK1	0.819	-0.096	1	0.759
EEF2K	0.819	-0.039	3	0.793
MRCKB	0.819	0.084	-3	0.776
CAMKK2	0.819	-0.133	-2	0.778
CDK6	0.819	0.071	1	0.689
TNIK	0.818	-0.037	3	0.816
PHKG2	0.818	-0.097	-3	0.824
CDK4	0.817	0.075	1	0.677
CHK2	0.817	0.049	-3	0.687
MINK	0.817	-0.063	1	0.764
KHS2	0.817	0.061	1	0.776
DMPK1	0.817	0.144	-3	0.800
LRRK2	0.816	-0.109	2	0.850
PDHK4_TYR	0.815	0.304	2	0.902
CK1A	0.815	0.159	-3	0.522
HGK	0.815	-0.098	3	0.818
SBK	0.814	0.093	-3	0.625
TTBK1	0.814	-0.210	2	0.623
KHS1	0.813	-0.000	1	0.755
SLK	0.813	-0.054	-2	0.746
BUB1	0.812	0.061	-5	0.829
VRK1	0.812	-0.144	2	0.840
MEKK6	0.812	-0.173	1	0.769
CAMK1A	0.812	0.039	-3	0.701
MAP2K6_TYR	0.812	0.248	-1	0.910
MAP3K15	0.811	-0.162	1	0.734
BMPR2_TYR	0.811	0.241	-1	0.921
PKN1	0.811	-0.022	-3	0.760
NEK4	0.811	-0.217	1	0.756
LOK	0.811	-0.097	-2	0.800
STK33	0.811	-0.124	2	0.627
MST1	0.810	-0.099	1	0.762
YANK3	0.809	0.016	2	0.422
CRIK	0.808	0.114	-3	0.750
MAP2K4_TYR	0.808	0.117	-1	0.901
PBK	0.808	-0.031	1	0.737
IRAK1	0.808	-0.348	-1	0.771
NEK1	0.807	-0.193	1	0.763
PDHK1_TYR	0.807	0.155	-1	0.923
TESK1_TYR	0.806	-0.011	3	0.838
ROCK1	0.805	0.074	-3	0.788
TTK	0.803	-0.038	-2	0.847
OSR1	0.802	-0.067	2	0.810
YSK1	0.802	-0.154	2	0.811
HASPIN	0.802	0.000	-1	0.730
MAP2K7_TYR	0.801	-0.127	2	0.869
PKMYT1_TYR	0.800	-0.082	3	0.806
ALPHAK3	0.800	0.016	-1	0.810
PKG1	0.797	0.004	-2	0.649
MEK2	0.797	-0.336	2	0.813
PINK1_TYR	0.797	-0.141	1	0.823
RIPK2	0.797	-0.313	1	0.699
LIMK2_TYR	0.796	-0.052	-3	0.880
EPHA6	0.796	0.051	-1	0.900
TXK	0.793	0.133	1	0.847
EPHB4	0.792	0.003	-1	0.865
MYO3B	0.791	-0.113	2	0.824
BIKE	0.790	-0.038	1	0.705
ASK1	0.788	-0.213	1	0.722
RET	0.788	-0.193	1	0.772
EPHA4	0.788	0.027	2	0.804
MYO3A	0.788	-0.135	1	0.757
FGR	0.787	-0.046	1	0.827
CK1G3	0.787	0.106	-3	0.478
LIMK1_TYR	0.786	-0.272	2	0.849
DDR1	0.785	-0.152	4	0.807
YES1	0.784	-0.070	-1	0.863
INSRR	0.784	-0.068	3	0.690
MST1R	0.784	-0.231	3	0.748
NEK3	0.784	-0.318	1	0.716
SRMS	0.784	-0.015	1	0.839
ABL2	0.783	-0.078	-1	0.824
FER	0.783	-0.128	1	0.848
JAK3	0.782	-0.126	1	0.756
TAO1	0.782	-0.189	1	0.689
TYRO3	0.782	-0.235	3	0.730
CSF1R	0.782	-0.172	3	0.724
EPHB1	0.781	-0.047	1	0.825
ITK	0.781	-0.033	-1	0.821
ROS1	0.780	-0.248	3	0.702
BLK	0.780	0.022	-1	0.870
LCK	0.780	-0.023	-1	0.867
ABL1	0.779	-0.098	-1	0.813
TYK2	0.779	-0.353	1	0.762
FYN	0.779	0.071	-1	0.855
TNK2	0.779	-0.105	3	0.696
FGFR2	0.779	-0.141	3	0.755
PTK2	0.778	0.165	-1	0.863
EPHB2	0.778	-0.040	-1	0.845
JAK2	0.778	-0.298	1	0.761
CK1G2	0.778	0.128	-3	0.566
HCK	0.778	-0.113	-1	0.858
KIT	0.778	-0.133	3	0.732
FLT1	0.777	-0.015	-1	0.876
BMX	0.777	-0.009	-1	0.747
EPHB3	0.777	-0.088	-1	0.845
KDR	0.777	-0.120	3	0.695
MET	0.775	-0.087	3	0.721
YANK2	0.775	-0.015	2	0.432
SYK	0.774	0.156	-1	0.838
STLK3	0.774	-0.249	1	0.717
AAK1	0.773	0.002	1	0.607
EPHA7	0.773	-0.052	2	0.797
MERTK	0.772	-0.124	3	0.712
DDR2	0.772	-0.010	3	0.683
NEK10_TYR	0.772	-0.184	1	0.660
EPHA3	0.771	-0.095	2	0.772
TEC	0.771	-0.103	-1	0.742
WEE1_TYR	0.771	-0.115	-1	0.767
FGFR3	0.770	-0.115	3	0.724
PDGFRB	0.770	-0.288	3	0.737
TNK1	0.769	-0.211	3	0.715
FLT3	0.769	-0.256	3	0.725
AXL	0.768	-0.213	3	0.715
TEK	0.768	-0.243	3	0.671
EPHA5	0.768	-0.027	2	0.787
TNNI3K_TYR	0.767	-0.182	1	0.772
ERBB2	0.767	-0.163	1	0.738
PTK2B	0.767	-0.040	-1	0.780
FGFR1	0.767	-0.261	3	0.701
JAK1	0.766	-0.209	1	0.704
NTRK1	0.765	-0.231	-1	0.837
EPHA8	0.764	-0.057	-1	0.843
BTK	0.763	-0.266	-1	0.771
SRC	0.763	-0.064	-1	0.838
FRK	0.763	-0.142	-1	0.857
LYN	0.763	-0.129	3	0.656
PTK6	0.763	-0.267	-1	0.736
LTK	0.763	-0.222	3	0.674
FLT4	0.762	-0.210	3	0.701
ALK	0.762	-0.248	3	0.646
EGFR	0.762	-0.082	1	0.651
MATK	0.761	-0.137	-1	0.753
INSR	0.760	-0.218	3	0.667
EPHA1	0.760	-0.206	3	0.696
PDGFRA	0.759	-0.383	3	0.732
NTRK3	0.758	-0.190	-1	0.789
FGFR4	0.758	-0.105	-1	0.795
EPHA2	0.757	-0.040	-1	0.816
NTRK2	0.756	-0.306	3	0.692
ERBB4	0.756	-0.013	1	0.687
CSK	0.756	-0.169	2	0.796
ZAP70	0.749	0.031	-1	0.760
IGF1R	0.749	-0.165	3	0.612
MUSK	0.739	-0.243	1	0.636
FES	0.735	-0.152	-1	0.720