Motif 1188 (n=932)
Position-wise Probabilities
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uniprot | genes | site | source | protein | function |
---|---|---|---|---|---|
A0A087WTJ2 | GIMAP1-GIMAP5 | T8 | ochoa | GIMAP1-GIMAP5 readthrough | None |
A0A087WV48 | None | S9 | ochoa | Peptidylprolyl isomerase | None |
A0A1W2PR48 | TLE7 | S9 | ochoa | Transducin-like enhancer protein 7 | None |
A0A1W2PRX2 | None | S9 | ochoa | Adenylosuccinate lyase | None |
A0PJW8 | DAPL1 | S10 | ochoa | Death-associated protein-like 1 (Early epithelial differentiation-associated protein) | May play a role in the early stages of epithelial differentiation or in apoptosis. {ECO:0000250}. |
A1A5D9 | BICDL2 | S8 | ochoa | BICD family-like cargo adapter 2 (Bicaudal D-related protein 2) (BICD-related protein 2) (BICDR-2) (Coiled-coil domain-containing protein 64B) | None |
A1KXE4 | FAM168B | S9 | ochoa | Myelin-associated neurite-outgrowth inhibitor (Mani) (p20) | Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. |
A1KXE4 | FAM168B | S10 | ochoa | Myelin-associated neurite-outgrowth inhibitor (Mani) (p20) | Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. |
A2RU30 | TESPA1 | T9 | ochoa | Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1) | Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}. |
A2RU30 | TESPA1 | S10 | ochoa | Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1) | Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}. |
A6NFI3 | ZNF316 | S10 | ochoa | Zinc finger protein 316 | May be involved in transcriptional regulation. {ECO:0000250}. |
A6NKN8 | PCP4L1 | T8 | ochoa | Purkinje cell protein 4-like protein 1 (PCP4-like protein 1) | None |
A6NKN8 | PCP4L1 | S9 | ochoa | Purkinje cell protein 4-like protein 1 (PCP4-like protein 1) | None |
A8MTQ0 | NOTO | S9 | ochoa | Homeobox protein notochord | Transcription regulator acting downstream of both FOXA2 and Brachyury (T) during notochord development. Required for node morphogenesis. Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function. Plays a role in regulating axial versus paraxial cell fate. Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node (By similarity). {ECO:0000250|UniProtKB:Q5TIS6}. |
B5ME19 | EIF3CL | S9 | ochoa | Eukaryotic translation initiation factor 3 subunit C-like protein | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. {ECO:0000250|UniProtKB:Q99613}. |
B7ZBB8 | PPP1R3G | S9 | ochoa | Protein phosphatase 1 regulatory subunit 3G | Glycogen-targeting subunit for protein phosphatase 1 (PP1). Involved in the regulation of hepatic glycogenesis in a manner coupled to the fasting-feeding cycle and distinct from other glycogen-targeting subunits (By similarity). {ECO:0000250}. |
C9J1V9 | EEF1E1-BLOC1S5 | S8 | ochoa | EEF1E1-BLOC1S5 readthrough (NMD candidate) (HCG2043275) | None |
C9JAW5 | None | S8 | ochoa | HIG1 domain-containing protein | None |
C9JI98 | TMEM238 | S10 | ochoa | Transmembrane protein 238 | None |
C9JQL5 | None | S10 | ochoa | Putative dispanin subfamily A member 2d (DSPA2d) | None |
C9JRZ8 | AKR1B15 | S8 | ochoa | Aldo-keto reductase family 1 member B15 (EC 1.1.1.-) (EC 1.1.1.300) (EC 1.1.1.54) (Estradiol 17-beta-dehydrogenase AKR1B15) (Farnesol dehydrogenase) (EC 1.1.1.216) (Testosterone 17beta-dehydrogenase) (EC 1.1.1.64) | [Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds (PubMed:21276782, PubMed:26222439). In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs (PubMed:25577493). Displays strong enzymatic activity toward all-trans-retinal and 9-cis-retinal (PubMed:26222439). May play a physiological role in retinoid metabolism (PubMed:26222439). {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493, ECO:0000269|PubMed:26222439}.; FUNCTION: [Isoform 2]: No oxidoreductase activity observed with the tested substrates. {ECO:0000269|PubMed:25577493}. |
C9JRZ8 | AKR1B15 | T9 | ochoa | Aldo-keto reductase family 1 member B15 (EC 1.1.1.-) (EC 1.1.1.300) (EC 1.1.1.54) (Estradiol 17-beta-dehydrogenase AKR1B15) (Farnesol dehydrogenase) (EC 1.1.1.216) (Testosterone 17beta-dehydrogenase) (EC 1.1.1.64) | [Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds (PubMed:21276782, PubMed:26222439). In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs (PubMed:25577493). Displays strong enzymatic activity toward all-trans-retinal and 9-cis-retinal (PubMed:26222439). May play a physiological role in retinoid metabolism (PubMed:26222439). {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493, ECO:0000269|PubMed:26222439}.; FUNCTION: [Isoform 2]: No oxidoreductase activity observed with the tested substrates. {ECO:0000269|PubMed:25577493}. |
D6RBG4 | SRP19 | S8 | ochoa | Signal recognition particle 19 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). Binds directly to 7SL RNA. Mediates binding of SRP54 to the SRP complex. {ECO:0000256|ARBA:ARBA00045518}. |
J3KQ70 | INO80B-WBP1 | S9 | ochoa | HCG2039827, isoform CRA_e (INO80B-WBP1 readthrough (NMD candidate)) | None |
J3QQQ9 | None | S9 | ochoa | KOW domain-containing protein | None |
O00178 | GTPBP1 | S8 | ochoa | GTP-binding protein 1 (G-protein 1) (GP-1) (GP1) | Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250|UniProtKB:D2XV59}. |
O00233 | PSMD9 | S9 | ochoa | 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) | Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process. {ECO:0000269|PubMed:19490896}. |
O00458 | IFRD1 | T9 | ochoa | Interferon-related developmental regulator 1 (Nerve growth factor-inducible protein PC4) | Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity). {ECO:0000250}. |
O00512 | BCL9 | S10 | ochoa | B-cell CLL/lymphoma 9 protein (B-cell lymphoma 9 protein) (Bcl-9) (Protein legless homolog) | Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11955446}. |
O14579 | COPE | S10 | ochoa | Coatomer subunit epsilon (Epsilon-coat protein) (Epsilon-COP) | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}. |
O14713 | ITGB1BP1 | S10 | ochoa|psp | Integrin beta-1-binding protein 1 (Integrin cytoplasmic domain-associated protein 1) (ICAP-1) | Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292, ECO:0000269|Ref.19}. |
O14730 | RIOK3 | S8 | ochoa | Serine/threonine-protein kinase RIO3 (EC 2.7.11.1) (RIO kinase 3) (sudD homolog) | Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses. May act as an adapter protein essential for the recruitment of TBK1 to IRF3 (PubMed:24807708). Phosphorylates IFIH1 on 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and resulting in attenuated IFIH1-signaling (PubMed:25865883). Can inhibit CASP10 isoform 7-mediated activation of the NF-kappaB signaling pathway (PubMed:19557502). May play a role in the biogenesis of the 40S ribosomal subunit. Involved in the processing of 21S pre-rRNA to the mature 18S rRNA (PubMed:22418843). {ECO:0000269|PubMed:19557502, ECO:0000269|PubMed:22418843, ECO:0000269|PubMed:24807708, ECO:0000269|PubMed:25865883}. |
O15014 | ZNF609 | S8 | ochoa | Zinc finger protein 609 | Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others. {ECO:0000250|UniProtKB:Q8BZ47}.; FUNCTION: [Isoform 2]: Involved in the regulation of myoblast proliferation during myogenesis. {ECO:0000269|PubMed:28344082}. |
O15020 | SPTBN2 | T8 | ochoa | Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein) | Probably plays an important role in neuronal membrane skeleton. |
O15037 | KHNYN | S10 | ochoa | Protein KHNYN (KH and NYN domain-containing protein) | None |
O15234 | CASC3 | S10 | ochoa | Protein CASC3 (Cancer susceptibility candidate gene 3 protein) (Metastatic lymph node gene 51 protein) (MLN 51) (Protein barentsz) (Btz) | Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. |
O15372 | EIF3H | T8 | ochoa | Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
O15372 | EIF3H | S10 | ochoa | Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03007, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
O15530 | PDPK1 | Y9 | psp | 3-phosphoinositide-dependent protein kinase 1 (hPDK1) (EC 2.7.11.1) | Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9445477, PubMed:9707564, PubMed:9768361). Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), TSSK3, protein kinase PKN (PKN1 and PKN2) (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9707564, PubMed:9768361). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage (PubMed:10226025, PubMed:12167717, PubMed:9094314). Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta (PubMed:17327236). Activates PPARG transcriptional activity and promotes adipocyte differentiation (By similarity). Activates the NF-kappa-B pathway via phosphorylation of IKKB (PubMed:16207722). The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II (PubMed:14585963). Controls proliferation, survival, and growth of developing pancreatic cells (By similarity). Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells (By similarity). Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis (PubMed:17371830). Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response (By similarity). Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses (By similarity). Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity). {ECO:0000250|UniProtKB:Q9Z2A0, ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:12167717, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:14604990, ECO:0000269|PubMed:16207722, ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:17371830, ECO:0000269|PubMed:18835241, ECO:0000269|PubMed:9094314, ECO:0000269|PubMed:9368760, ECO:0000269|PubMed:9445476, ECO:0000269|PubMed:9445477, ECO:0000269|PubMed:9707564, ECO:0000269|PubMed:9768361}.; FUNCTION: [Isoform 3]: Catalytically inactive. {ECO:0000269|PubMed:9445477}. |
O43255 | SIAH2 | S10 | ochoa | E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (hSiah2) | E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11483518, PubMed:19224863, PubMed:9334332). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes (PubMed:11483518, PubMed:19224863, PubMed:22878263, PubMed:9334332). Has some overlapping function with SIAH1 (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493). Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (PubMed:26392558). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558, ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}. |
O43294 | TGFB1I1 | S9 | ochoa | Transforming growth factor beta-1-induced transcript 1 protein (Androgen receptor coactivator 55 kDa protein) (Androgen receptor-associated protein of 55 kDa) (Hydrogen peroxide-inducible clone 5 protein) (Hic-5) | Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:12445807, ECO:0000269|PubMed:12700349, ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15561701, ECO:0000269|PubMed:16141357, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9032249}. |
O43299 | AP5Z1 | S8 | ochoa | AP-5 complex subunit zeta-1 (Adaptor-related protein complex 5 zeta subunit) (Zeta5) | As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}. |
O43310 | CTIF | S10 | ochoa | CBP80/20-dependent translation initiation factor | Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:19648179}. |
O43324 | EEF1E1 | S8 | ochoa | Eukaryotic translation elongation factor 1 epsilon-1 (Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3) (Elongation factor p18) (Multisynthase complex auxiliary component p18) | Positive modulator of ATM response to DNA damage. {ECO:0000250|UniProtKB:Q9D1M4}. |
O43396 | TXNL1 | S9 | ochoa | Thioredoxin-like protein 1 (32 kDa thioredoxin-related protein) | Active thioredoxin with a redox potential of about -250 mV. {ECO:0000269|PubMed:19349277}. |
O43491 | EPB41L2 | S9 | 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}. |
O43543 | XRCC2 | S10 | ochoa | DNA repair protein XRCC2 (X-ray repair cross-complementing protein 2) | Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:21276791, ECO:0000269|PubMed:23149936, ECO:0000269|PubMed:27233470}. |
O43583 | DENR | S8 | ochoa | Density-regulated protein (DRP) (Protein DRP1) (Smooth muscle cell-associated protein 3) (SMAP-3) | Translation regulator forming a complex with MCTS1 to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post-termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation. This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:37875108}. |
O43583 | DENR | S9 | ochoa | Density-regulated protein (DRP) (Protein DRP1) (Smooth muscle cell-associated protein 3) (SMAP-3) | Translation regulator forming a complex with MCTS1 to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post-termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation. This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:20713520, ECO:0000269|PubMed:37875108}. |
O43598 | DNPH1 | S10 | ochoa | 5-hydroxymethyl-dUMP N-hydrolase (EC 3.2.2.-) (2'-deoxynucleoside 5'-phosphate N-hydrolase 1) (c-Myc-responsive protein RCL) | Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118). {ECO:0000269|PubMed:33833118}. |
O43609 | SPRY1 | S9 | ochoa | Protein sprouty homolog 1 (Spry-1) | Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9QXV9}. |
O43711 | TLX3 | T9 | ochoa | T-cell leukemia homeobox protein 3 (Homeobox protein Hox-11L2) | None |
O43772 | SLC25A20 | S9 | ochoa | Mitochondrial carnitine/acylcarnitine carrier protein (Carnitine/acylcarnitine translocase) (CAC) (CACT) (Solute carrier family 25 member 20) | Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism (Probable) (PubMed:12892634, PubMed:18307102). Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange) (PubMed:18307102). {ECO:0000269|PubMed:12892634, ECO:0000269|PubMed:18307102, ECO:0000305|PubMed:18307102, ECO:0000305|PubMed:20347717}. |
O43776 | NARS1 | S9 | ochoa | Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Asparaginyl-tRNA synthetase 1) | Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (PubMed:32738225, PubMed:32788587, PubMed:9421509). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells (PubMed:12235211, PubMed:30171954). Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells (PubMed:32788587). {ECO:0000269|PubMed:12235211, ECO:0000269|PubMed:30171954, ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509}. |
O43929 | ORC4 | S8 | ochoa | Origin recognition complex subunit 4 | Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}. |
O43929 | ORC4 | S10 | ochoa | Origin recognition complex subunit 4 | Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}. |
O60218 | AKR1B10 | S8 | ochoa | Aldo-keto reductase family 1 member B10 (EC 1.1.1.300) (EC 1.1.1.54) (ARL-1) (Aldose reductase-like) (Aldose reductase-related protein) (ARP) (hARP) (Small intestine reductase) (SI reductase) | Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:12732097, PubMed:18087047, PubMed:19013440, PubMed:19563777, PubMed:9565553). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097). {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047, ECO:0000269|PubMed:19013440, ECO:0000269|PubMed:19563777, ECO:0000269|PubMed:9565553}. |
O60218 | AKR1B10 | T9 | ochoa | Aldo-keto reductase family 1 member B10 (EC 1.1.1.300) (EC 1.1.1.54) (ARL-1) (Aldose reductase-like) (Aldose reductase-related protein) (ARP) (hARP) (Small intestine reductase) (SI reductase) | Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:12732097, PubMed:18087047, PubMed:19013440, PubMed:19563777, PubMed:9565553). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097). {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:18087047, ECO:0000269|PubMed:19013440, ECO:0000269|PubMed:19563777, ECO:0000269|PubMed:9565553}. |
O60220 | TIMM8A | S8 | ochoa | Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1) (X-linked deafness dystonia protein) | Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}. |
O60260 | PRKN | S9 | psp | E3 ubiquitin-protein ligase parkin (Parkin) (EC 2.3.2.31) (Parkin RBR E3 ubiquitin-protein ligase) (Parkinson juvenile disease protein 2) (Parkinson disease protein 2) | Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539). {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23685073, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:33499712}. |
O60260 | PRKN | S10 | psp | E3 ubiquitin-protein ligase parkin (Parkin) (EC 2.3.2.31) (Parkin RBR E3 ubiquitin-protein ligase) (Parkinson juvenile disease protein 2) (Parkinson disease protein 2) | Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539). {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23685073, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:33499712}. |
O60287 | URB1 | S9 | ochoa | Nucleolar pre-ribosomal-associated protein 1 (Nucleolar protein 254 kDa) (URB1 ribosome biogenesis 1 homolog) | None |
O60479 | DLX3 | S10 | psp | Homeobox protein DLX-3 | Transcriptional activator (By similarity). Activates transcription of GNRHR, via binding to the downstream activin regulatory element (DARE) in the gene promoter (By similarity). {ECO:0000250|UniProtKB:Q64205}. |
O60547 | GMDS | S10 | ochoa | GDP-mannose 4,6 dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (GMD) | Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. {ECO:0000269|PubMed:9525924, ECO:0000269|PubMed:9603974}. |
O60716 | CTNND1 | S8 | ochoa | Catenin delta-1 (Cadherin-associated Src substrate) (CAS) (p120 catenin) (p120(ctn)) (p120(cas)) | Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:14610055, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:18343367, ECO:0000269|PubMed:20371349}. |
O60739 | EIF1B | S9 | ochoa | Eukaryotic translation initiation factor 1b (eIF1b) (Protein translation factor SUI1 homolog GC20) | Probably involved in translation. |
O60759 | CYTIP | S10 | ochoa | Cytohesin-interacting protein (Cytohesin binder and regulator) (CYBR) (Cytohesin-associated scaffolding protein) (CASP) (Cytohesin-binding protein HE) (Cbp HE) (Pleckstrin homology Sec7 and coiled-coil domains-binding protein) | By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm. |
O60762 | DPM1 | S9 | ochoa | Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase subunit 1) | Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. {ECO:0000269|PubMed:10835346}. |
O60784 | TOM1 | S10 | ochoa | Target of Myb1 membrane trafficking protein (Target of Myb protein 1) | Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (PubMed:14563850, PubMed:15047686, PubMed:23023224, PubMed:25588840, PubMed:26320582, PubMed:31371777). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (PubMed:23023224). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (PubMed:23023224). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (PubMed:31371777). Binds to polyubiquitinated proteins via its GAT domain (PubMed:14563850). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (PubMed:15047686). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (PubMed:14563850, PubMed:15047686). Mediates clathrin recruitment to early endosomes by ZFYVE16 (PubMed:15657082). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (PubMed:26320582). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation (PubMed:25588840). PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation (PubMed:25588840). Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (PubMed:15047686, PubMed:26320582). {ECO:0000269|PubMed:14563850, ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:15657082, ECO:0000269|PubMed:23023224, ECO:0000269|PubMed:25588840, ECO:0000269|PubMed:26320582, ECO:0000269|PubMed:31371777}. |
O60841 | EIF5B | S9 | ochoa | Eukaryotic translation initiation factor 5B (eIF-5B) (EC 3.6.5.3) (Translation initiation factor IF-2) | Plays a role in translation initiation (PubMed:10659855, PubMed:35732735). Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:10659855, PubMed:35732735). Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex (PubMed:12569173, PubMed:35732735). Is released after formation of the 80S initiation complex (PubMed:35732735). Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit (PubMed:10659855). {ECO:0000269|PubMed:10659855, ECO:0000269|PubMed:12569173, ECO:0000269|PubMed:35732735}. |
O60927 | PPP1R11 | S9 | ochoa | E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Hemochromatosis candidate gene V protein) (HCG V) (Protein phosphatase 1 regulatory subunit 11) (Protein phosphatase inhibitor 3) | Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2 (PubMed:27805901). Inhibitor of protein phosphatase 1 (PubMed:9843442). {ECO:0000269|PubMed:27805901, ECO:0000269|PubMed:9843442}. |
O75061 | DNAJC6 | S10 | ochoa | Auxilin (EC 3.1.3.-) (DnaJ homolog subfamily C member 6) | May act as a protein phosphatase and/or a lipid phosphatase. Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intracellular trafficking (PubMed:18489706). Firstly, binds tightly to the clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion. The HSPA8:ATP complex then binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8 per triskelion leading to ATP hydrolysis stimulation and causing a conformational change in the HSPA8. This cycle is repeated three times to drive to a complex containing the clathrin-auxilin cage associated to three HSPA8:ADP complex. The ATP hydrolysis of the third HSPA8:ATP complex leads to a concerted dismantling of the cage into component triskelia. Then, dissociates from the released triskelia and be recycled to initiate another cycle of HSPA8's recruitment. Also acts during the early steps of clathrin-coated vesicle (CCV) formation through its interaction with the GTP bound form of DNM1 (By similarity). {ECO:0000250|UniProtKB:Q27974, ECO:0000269|PubMed:18489706}. |
O75122 | CLASP2 | S8 | 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}. |
O75147 | OBSL1 | S10 | ochoa | Obscurin-like protein 1 | Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}. |
O75182 | SIN3B | S8 | ochoa | Paired amphipathic helix protein Sin3b (Histone deacetylase complex subunit Sin3b) (Transcriptional corepressor Sin3b) | Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). {ECO:0000250|UniProtKB:Q62141, ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:37137925}. |
O75386 | TULP3 | S9 | ochoa | Tubby-related protein 3 (Tubby-like protein 3) | Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. During adipogenesis, regulates ciliary trafficking of FFAR4 in preadipocytes. {ECO:0000269|PubMed:11375483, ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:31761534}. |
O75391 | SPAG7 | S10 | ochoa | Sperm-associated antigen 7 | None |
O75410 | TACC1 | S10 | 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}. |
O75431 | MTX2 | S10 | ochoa | Metaxin-2 (Mitochondrial outer membrane import complex protein 2) | Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:10381257}. |
O75469 | NR1I2 | S8 | psp | Nuclear receptor subfamily 1 group I member 2 (Orphan nuclear receptor PAR1) (Orphan nuclear receptor PXR) (Pregnane X receptor) (Steroid and xenobiotic receptor) (SXR) | Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes. {ECO:0000269|PubMed:11297522, ECO:0000269|PubMed:11668216, ECO:0000269|PubMed:12578355, ECO:0000269|PubMed:18768384, ECO:0000269|PubMed:19297428, ECO:0000269|PubMed:9727070}. |
O75530 | EED | T8 | ochoa | Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1) | Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:28229514, ECO:0000269|PubMed:9584199}. |
O75563 | SKAP2 | S8 | ochoa | Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (Retinoic acid-induced protein 70) (SKAP55 homolog) (SKAP-55HOM) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) | May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}. |
O75563 | SKAP2 | S9 | ochoa | Src kinase-associated phosphoprotein 2 (Pyk2/RAFTK-associated protein) (Retinoic acid-induced protein 70) (SKAP55 homolog) (SKAP-55HOM) (SKAP-HOM) (Src family-associated phosphoprotein 2) (Src kinase-associated phosphoprotein 55-related protein) (Src-associated adapter protein with PH and SH3 domains) | May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}. |
O75643 | SNRNP200 | S8 | ochoa | U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13) (Activating signal cointegrator 1 complex subunit 3-like 1) (BRR2 homolog) (U5 snRNP-specific 200 kDa protein) (U5-200KD) | Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (PubMed:35241646). Plays a role in pre-mRNA splicing as a core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:35241646, ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711, ECO:0000305|PubMed:33509932}. |
O75821 | EIF3G | S8 | ochoa | Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44) | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}. |
O75909 | CCNK | S8 | ochoa | Cyclin-K | Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:9632813}. |
O75909 | CCNK | S9 | ochoa | Cyclin-K | Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:9632813}. |
O75937 | DNAJC8 | T9 | ochoa | DnaJ homolog subfamily C member 8 (Splicing protein spf31) | Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells (PubMed:27133716). {ECO:0000269|PubMed:27133716}. |
O75937 | DNAJC8 | S10 | ochoa | DnaJ homolog subfamily C member 8 (Splicing protein spf31) | Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells (PubMed:27133716). {ECO:0000269|PubMed:27133716}. |
O76080 | ZFAND5 | T8 | 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}. |
O94763 | URI1 | T8 | ochoa | Unconventional prefoldin RPB5 interactor 1 (Protein NNX3) (Protein phosphatase 1 regulatory subunit 19) (RNA polymerase II subunit 5-mediating protein) (RPB5-mediating protein) | Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination. |
O94768 | STK17B | S10 | ochoa | Serine/threonine-protein kinase 17B (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 2) | Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269|PubMed:9786912}. |
O94782 | USP1 | S9 | ochoa | Ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (hUBP) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) [Cleaved into: Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment] | Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2 (PubMed:15694335). Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA (PubMed:16531995, PubMed:20147293). Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity (PubMed:18082604, PubMed:26388029). {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:26388029}. |
O94887 | FARP2 | Y8 | 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}. |
O94888 | UBXN7 | S10 | ochoa | UBX domain-containing protein 7 | Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}. |
O95067 | CCNB2 | S10 | ochoa | G2/mitotic-specific cyclin-B2 | Essential for the control of the cell cycle at the G2/M (mitosis) transition. |
O95140 | MFN2 | S10 | ochoa | Mitofusin-2 (EC 3.6.5.-) (Transmembrane GTPase MFN2) | Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity). {ECO:0000250|UniProtKB:Q80U63, ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:19889647, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:28114303, ECO:0000305}. |
O95171 | SCEL | S10 | ochoa | Sciellin | May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope. |
O95197 | RTN3 | T8 | ochoa | Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII) | May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules (PubMed:25612671). Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:25612671}.; FUNCTION: (Microbial infection) Plays a positive role in viral replication and pathogenesis of enteroviruses. {ECO:0000269|PubMed:17182608}. |
O95197 | RTN3 | S10 | ochoa | Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII) | May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules (PubMed:25612671). Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:25612671}.; FUNCTION: (Microbial infection) Plays a positive role in viral replication and pathogenesis of enteroviruses. {ECO:0000269|PubMed:17182608}. |
O95199 | RCBTB2 | S9 | ochoa | RCC1 and BTB domain-containing protein 2 (Chromosome condensation 1-like) (CHC1-L) (RCC1-like G exchanging factor) (Regulator of chromosome condensation and BTB domain-containing protein 2) | None |
O95218 | ZRANB2 | S9 | ochoa | Zinc finger Ran-binding domain-containing protein 2 (Zinc finger protein 265) (Zinc finger, splicing) | Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). May interfere with constitutive 5'-splice site selection. {ECO:0000269|PubMed:11448987, ECO:0000269|PubMed:21256132}. |
O95238 | SPDEF | S9 | ochoa | SAM pointed domain-containing Ets transcription factor (Prostate epithelium-specific Ets transcription factor) (Prostate-specific Ets) (Prostate-derived Ets factor) | May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter. {ECO:0000269|PubMed:10625666}. |
O95238 | SPDEF | S10 | ochoa | SAM pointed domain-containing Ets transcription factor (Prostate epithelium-specific Ets transcription factor) (Prostate-specific Ets) (Prostate-derived Ets factor) | May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter. {ECO:0000269|PubMed:10625666}. |
O95251 | KAT7 | S10 | 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}. |
O95295 | SNAPIN | S10 | ochoa | SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells (PubMed:17182842, PubMed:18167355). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}. |
O95379 | TNFAIP8 | S8 | ochoa | Tumor necrosis factor alpha-induced protein 8 (TNF alpha-induced protein 8) (Head and neck tumor and metastasis-related protein) (MDC-3.13) (NF-kappa-B-inducible DED-containing protein) (NDED) (SCC-S2) (TNF-induced protein GG2-1) | Acts as a negative mediator of apoptosis and may play a role in tumor progression. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation. {ECO:0000269|PubMed:10644768, ECO:0000269|PubMed:11346652, ECO:0000269|PubMed:14724590}. |
O95562 | SFT2D2 | S9 | ochoa | Vesicle transport protein SFT2B (SFT2 domain-containing protein 2) | May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}. |
O95622 | ADCY5 | S8 | ochoa | Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (AC5) | Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642, PubMed:24700542, PubMed:26206488). Mediates signaling downstream of ADRB1 (PubMed:24700542). Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (PubMed:24740569). {ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:24740569, ECO:0000269|PubMed:26206488}. |
O95707 | POP4 | S10 | ochoa | Ribonuclease P protein subunit p29 (hPOP4) | Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:10352175, ECO:0000269|PubMed:30454648}. |
O95786 | RIGI | S8 | ochoa|psp | Antiviral innate immune response receptor RIG-I (ATP-dependent RNA helicase DDX58) (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (RNA sensor RIG-I) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I) | Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms (PubMed:28469175, PubMed:31006531). Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.74). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:15208624, ECO:0000269|PubMed:15708988, ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19122199, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21742966, ECO:0000269|PubMed:24366338, ECO:0000269|PubMed:28469175, ECO:0000269|PubMed:29117565, ECO:0000269|PubMed:31006531, ECO:0000269|PubMed:34935440, ECO:0000269|PubMed:35263596, ECO:0000269|PubMed:36793726, ECO:0000269|Ref.74, ECO:0000303|PubMed:21616437, ECO:0000303|PubMed:21884169}. |
O95801 | TTC4 | S10 | ochoa | Tetratricopeptide repeat protein 4 (TPR repeat protein 4) | May act as a co-chaperone for HSP90AB1 (PubMed:18320024). Promotes Sendai virus (SeV)-induced host cell innate immune responses (PubMed:29251827). {ECO:0000269|PubMed:18320024, ECO:0000269|PubMed:29251827}. |
O95935 | TBX18 | S8 | ochoa | T-box transcription factor TBX18 (T-box protein 18) | Acts as a transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart and coronary vessels, the ureter and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area. {ECO:0000250|UniProtKB:Q9EPZ6, ECO:0000269|PubMed:26235987}. |
O96006 | ZBED1 | S9 | ochoa | E3 SUMO-protein ligase ZBED1 (EC 2.3.2.-) (DNA replication-related element-binding factor) (Putative Ac-like transposable element) (Zinc finger BED domain-containing protein 1) (dREF homolog) | Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha transcription repression, increased recruitment of RNA polymerase II to gene promoters and positive regulation of transcription including H1-5 and ribosomal proteins such as: RPS6, RPL10A, and RPL12 (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). The resulting increased transcriptional activity drives cell proliferation (PubMed:12663651, PubMed:17220279). Binds to 5'-TGTCG[CT]GA[CT]A-3' consensus sequences in gene promoters of ribosomal proteins (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:17220279, ECO:0000269|PubMed:27068747}.; FUNCTION: (Microbial infection) Binds to human adenovirus gene promoters and contributes to transcriptional repression and virus growth inhibition during early stages of infection. {ECO:0000269|PubMed:25210186}. |
O96018 | APBA3 | S9 | ochoa | Amyloid-beta A4 precursor protein-binding family A member 3 (Adapter protein X11gamma) (Neuron-specific X11L2 protein) (Neuronal Munc18-1-interacting protein 3) (Mint-3) | May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}. |
O96028 | NSD2 | S8 | ochoa | Histone-lysine N-methyltransferase NSD2 (EC 2.1.1.357) (Multiple myeloma SET domain-containing protein) (MMSET) (Nuclear SET domain-containing protein 2) (Protein trithorax-5) (Wolf-Hirschhorn syndrome candidate 1 protein) | Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity). During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity). Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617). During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity). During B-cell development, required for the generation of the B1 lineage (By similarity). During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity). Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity). By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity). {ECO:0000250|UniProtKB:Q8BVE8, ECO:0000269|PubMed:16115125, ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:27571355, ECO:0000269|PubMed:29728617, ECO:0000269|PubMed:33941880}.; FUNCTION: [Isoform 1]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:22099308}.; FUNCTION: [Isoform 4]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:22099308). Methylation of histone H3 at 'Lys-27' is controversial (PubMed:18172012, PubMed:22099308). Mono-, di- or tri-methylates histone H3 at 'Lys-27' (H3K27me, H3K27me2 and H3K27me3) (PubMed:18172012). Does not methylate histone H3 at 'Lys-27' (PubMed:22099308). May act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment (PubMed:11152655, PubMed:18172012). {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:18172012, ECO:0000269|PubMed:22099308}. |
P01100 | FOS | Y10 | psp | Protein c-Fos (Cellular oncogene fos) (Fos proto-oncogene, AP-1 transcription factor subunit) (G0/G1 switch regulatory protein 7) (Proto-oncogene c-Fos) (Transcription factor AP-1 subunit c-Fos) | Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. {ECO:0000269|PubMed:16055710, ECO:0000269|PubMed:17160021, ECO:0000269|PubMed:22105363, ECO:0000269|PubMed:7588633, ECO:0000269|PubMed:9732876}. |
P02730 | SLC4A1 | Y8 | psp | Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233) | Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305). {ECO:0000269|PubMed:12692305, ECO:0000269|PubMed:14630931}. |
P02786 | TFRC | S10 | ochoa | Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (T9) (p90) (CD antigen CD71) [Cleaved into: Transferrin receptor protein 1, serum form (sTfR)] | Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity). {ECO:0000250|UniProtKB:Q62351, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:26642240, ECO:0000269|PubMed:3568132}.; FUNCTION: (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus. {ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:18268337}.; FUNCTION: (Microbial infection) Acts as a host entry factor for rabies virus that hijacks the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762, ECO:0000269|PubMed:36779763}.; FUNCTION: (Microbial infection) Acts as a host entry factor for SARS-CoV, MERS-CoV and SARS-CoV-2 viruses that hijack the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762}. |
P04075 | ALDOA | T9 | ochoa | Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Lung cancer antigen NY-LU-1) (Muscle-type aldolase) | Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:14766013). In addition, may also function as scaffolding protein (By similarity). {ECO:0000250, ECO:0000269|PubMed:14766013}. |
P04080 | CSTB | T9 | ochoa | Cystatin-B (CPI-B) (Liver thiol proteinase inhibitor) (Stefin-B) | This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. |
P04150 | NR3C1 | T8 | ochoa | Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) | Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:25775514, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:28139699, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9590696}.; FUNCTION: [Isoform Alpha]: Has transcriptional activation and repression activity (PubMed:11435610, PubMed:15769988, PubMed:15866175, PubMed:17635946, PubMed:19141540, PubMed:19248771, PubMed:20484466, PubMed:21664385, PubMed:23820903). Mediates glucocorticoid-induced apoptosis (PubMed:23303127). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:21664385, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903, ECO:0000269|PubMed:25847991}.; FUNCTION: [Isoform Beta]: Acts as a dominant negative inhibitor of isoform Alpha (PubMed:20484466, PubMed:7769088, PubMed:8621628). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (PubMed:19248771, PubMed:26711253). Loses this transcription modulator function on its own (PubMed:20484466). Has no hormone-binding activity (PubMed:8621628). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (PubMed:26711253). Directly regulates STAT1 expression in isoform Alpha-independent manner (PubMed:26711253). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:26711253, ECO:0000269|PubMed:7769088, ECO:0000269|PubMed:8621628}.; FUNCTION: [Isoform Alpha-2]: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism (PubMed:20484466).; FUNCTION: [Isoform GR-P]: Increases activity of isoform Alpha. {ECO:0000269|PubMed:11358809}.; FUNCTION: [Isoform Alpha-B]: More effective than isoform Alpha in transcriptional activation, but not repression activity. {ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform 10]: Has transcriptional activation activity. {ECO:0000269|PubMed:20484466}.; FUNCTION: [Isoform Alpha-C1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C3]: Has highest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). Mediates glucocorticoid-induced apoptosis (PubMed:23303127, PubMed:23820903). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}.; FUNCTION: [Isoform Alpha-D1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D3]: Has lowest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}. |
P04233 | CD74 | S8 | ochoa | HLA class II histocompatibility antigen gamma chain (HLA-DR antigens-associated invariant chain) (Ia antigen-associated invariant chain) (Ii) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)] | Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF.; FUNCTION: [Class-II-associated invariant chain peptide]: Binds to the peptide-binding site of MHC class II alpha/beta heterodimers forming an alpha-beta-CLIP complex, thereby preventing the loading of antigenic peptides to the MHC class II complex until its release by HLA-DM in the endosome. {ECO:0000269|PubMed:1448172}.; FUNCTION: [Isoform p41]: Stabilizes the conformation of mature CTSL by binding to its active site and serving as a chaperone to help maintain a pool of mature enzyme in endocytic compartments and extracellular space of antigen-presenting cells (APCs). Has antiviral activity by stymieing the endosomal entry of Ebola virus and coronaviruses, including SARS-CoV-2 (PubMed:32855215). Disrupts cathepsin-mediated Ebola virus glycoprotein processing, which prevents viral fusion and entry. This antiviral activity is specific to p41 isoform (PubMed:32855215). {ECO:0000250|UniProtKB:P04441, ECO:0000269|PubMed:32855215}. |
P04553 | PRM1 | S9 | psp | Sperm protamine P1 (Cysteine-rich protamine) | Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. |
P04637 | TP53 | S9 | ochoa|psp | Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53) | Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:38653238, PubMed:9840937). Negatively regulates cell division by controlling expression of a set of genes required for this process (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:9840937). One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (PubMed:12524540, PubMed:17189187). Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:24652652, ECO:0000269|PubMed:35618207, ECO:0000269|PubMed:36634798, ECO:0000269|PubMed:38653238, ECO:0000269|PubMed:9840937}. |
P04792 | HSPB1 | S9 | 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}. |
P05114 | HMGN1 | S8 | ochoa|psp | Non-histone chromosomal protein HMG-14 (High mobility group nucleosome-binding domain-containing protein 1) | Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity). {ECO:0000250}. |
P05412 | JUN | T8 | psp | Transcription factor Jun (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39) | Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306). {ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:12618758, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24623306}.; FUNCTION: (Microbial infection) Upon Epstein-Barr virus (EBV) infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 expression. {ECO:0000269|PubMed:31341047}. |
P05783 | KRT18 | T8 | ochoa | Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) | Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}. |
P05783 | KRT18 | S10 | ochoa | Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) | Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}. |
P06454 | PTMA | T8 | ochoa | Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha-1] | Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. |
P06454 | PTMA | S9 | ochoa | Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha-1] | Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. |
P06454 | PTMA | S10 | ochoa | Prothymosin alpha [Cleaved into: Prothymosin alpha, N-terminally processed; Thymosin alpha-1] | Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. |
P06730 | EIF4E | T8 | ochoa | Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) | Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). 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 (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:29987188}. |
P06730 | EIF4E | T9 | ochoa | Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) | Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). 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 (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:29987188}. |
P06748 | NPM1 | S10 | ochoa|psp | Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) | Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25956029}. |
P07451 | CA3 | S9 | ochoa | Carbonic anhydrase 3 (EC 4.2.1.1) (Carbonate dehydratase III) (Carbonic anhydrase III) (CA-III) | Reversible hydration of carbon dioxide. {ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712}. |
P08195 | SLC3A2 | S9 | ochoa | 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}. |
P08670 | VIM | S8 | ochoa|psp | Vimentin | Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250|UniProtKB:A0A8C0N8E3, ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}. |
P08670 | VIM | S9 | ochoa|psp | Vimentin | Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250|UniProtKB:A0A8C0N8E3, ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}. |
P08670 | VIM | S10 | ochoa|psp | Vimentin | Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). {ECO:0000250|UniProtKB:A0A8C0N8E3, ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}. |
P08727 | KRT19 | S10 | psp | Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19) | Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. |
P09132 | SRP19 | S8 | ochoa | Signal recognition particle 19 kDa protein (SRP19) | 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) (By similarity). Binds directly to 7SL RNA (By similarity). Mediates binding of SRP54 to the SRP complex (By similarity). {ECO:0000250|UniProtKB:J9PAS6}. |
P09211 | GSTP1 | Y8 | ochoa|psp | Glutathione S-transferase P (EC 2.5.1.18) (GST class-pi) (GSTP1-1) | Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000269|PubMed:21046276, ECO:0000269|PubMed:21668448, ECO:0000269|PubMed:9084911}. |
P09234 | SNRPC | Y8 | ochoa | U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) | Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. {ECO:0000255|HAMAP-Rule:MF_03153, ECO:0000269|PubMed:1826349, ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:2136774, ECO:0000269|PubMed:8798632}. |
P09382 | LGALS1 | S8 | ochoa | Galectin-1 (Gal-1) (14 kDa laminin-binding protein) (HLBP14) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (HBL) (HPL) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (Putative MAPK-activating protein PM12) (S-Lac lectin 1) | Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Plays a negative role in Th17 cell differentiation via activation of the receptor CD69 (PubMed:24752896). {ECO:0000269|PubMed:14617626, ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:24752896, ECO:0000269|PubMed:24945728}. |
P09543 | CNP | S9 | ochoa|psp | 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) | Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P06623, ECO:0000250|UniProtKB:P16330}. |
P0C264 | SBK3 | T8 | ochoa | Uncharacterized serine/threonine-protein kinase SBK3 (EC 2.7.11.1) (SH3 domain-binding kinase family member 3) (Sugen kinase 110) | None |
P0C5K6 | VENTXP1 | S9 | ochoa | Putative tumor antigen NA88-A (Cancer/testis antigen 18) (CT18) | None |
P0CG47 | UBB | T9 | ochoa | Polyubiquitin-B [Cleaved into: Ubiquitin] | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127, ECO:0000303|PubMed:19754430}. |
P0CG48 | UBC | T9 | ochoa | Polyubiquitin-C [Cleaved into: Ubiquitin] | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. During ubiquitination, the acceptor ubiquitin is positioned in the active site via direct interaction with the E2 ubiquitin-conjugating enzymes such as UBE2R2 (PubMed:38326650). As a monoubiquitin, its C-terminal glycine is recognized as a C-degron by Cul2-RING (CRL2) E3 ubiquitin-protein ligase complexes (PubMed:39548056). {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127, ECO:0000269|PubMed:38326650, ECO:0000269|PubMed:39548056, ECO:0000303|PubMed:19754430}. |
P10073 | ZSCAN22 | S9 | ochoa | Zinc finger and SCAN domain-containing protein 22 (Krueppel-related zinc finger protein 2) (Protein HKR2) (Zinc finger protein 50) | May be involved in transcriptional regulation. |
P10074 | ZBTB48 | S9 | ochoa | Zinc finger and BTB domain-containing protein 48 (Krueppel-related zinc finger protein 3) (hKR3) (Telomere zinc finger-associated protein) (TZAP) (Telomere-binding protein and transcriptional activator ZBTB48) (Zinc finger protein 855) | Plays a critical role in transcriptional regulation and chromatin remodeling. Acts as a regulator of telomere length (PubMed:28082411, PubMed:28500257). Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat (PubMed:28082411, PubMed:28500257). Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regulator of telomere length by initiating telomere trimming, a process that prevents the accumulation of aberrantly long telomeres (PubMed:28082411). Also acts as a transcription regulator that binds to promoter regions (PubMed:24382891, PubMed:28500257, PubMed:7969177). Regulates expression of a small subset of genes, including MTFP1 (PubMed:28500257). Acts as a negative regulator of cell proliferation by specifically activating expression of ARF, a tumor suppressor isoform of CDKN2A (PubMed:24382891). Acts as a transcription regulator of CIITA, the major factor regulating MHC class II gene expression (PubMed:39562739). In addition, regulates cellular m6A/m6Am methylation on RNA by facilitating the recruitment of the RNA demethylase, FTO, to target mRNAs (PubMed:39300486). {ECO:0000269|PubMed:24382891, ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257, ECO:0000269|PubMed:39300486, ECO:0000269|PubMed:39562739, ECO:0000269|PubMed:7969177}. |
P10301 | RRAS | T9 | ochoa | Ras-related protein R-Ras (EC 3.6.5.2) (p23) | GTP-binding protein with GTPase activity, likely involved in the regulation of MAPK signaling pathway and thereby controlling multiple cellular processes (PubMed:39809765). Regulates the organization of the actin cytoskeleton (PubMed:16537651, PubMed:18270267). With OSPBL3, modulates integrin beta-1 (ITGB1) activity (PubMed:18270267). {ECO:0000269|PubMed:16537651, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:39809765}. |
P10599 | TXN | T9 | ochoa | Thioredoxin (Trx) (ATL-derived factor) (ADF) (Surface-associated sulphydryl protein) (SASP) (allergen Hom s Trx) | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity (PubMed:16408020, PubMed:17606900). Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (PubMed:11118054, PubMed:9108029). {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17182577, ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:19032234, ECO:0000269|PubMed:2176490, ECO:0000269|PubMed:9108029}.; FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). |
P11216 | PYGB | S8 | ochoa | Glycogen phosphorylase, brain form (EC 2.4.1.1) | Glycogen phosphorylase that regulates glycogen mobilization (PubMed:27402852). Phosphorylase is an important allosteric enzyme in carbohydrate metabolism (PubMed:3346228). Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates (PubMed:3346228). However, all known phosphorylases share catalytic and structural properties (PubMed:3346228). {ECO:0000269|PubMed:27402852, ECO:0000303|PubMed:3346228}. |
P11387 | TOP1 | S10 | ochoa|psp | DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) | Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter. {ECO:0000250|UniProtKB:Q13472, ECO:0000269|PubMed:14594810, ECO:0000269|PubMed:16033260, ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:22904072, ECO:0000269|PubMed:2833744}. |
P11413 | G6PD | S8 | ochoa|psp | Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:35122041, ECO:0000269|PubMed:38066190, ECO:0000269|PubMed:743300}. |
P13051 | UNG | Y8 | ochoa | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) | Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine (PubMed:12958596, PubMed:15967827, PubMed:17101234, PubMed:22521144, PubMed:7671300, PubMed:8900285, PubMed:9016624, PubMed:9776759). Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication. The resultant AP sites temporarily stall replication, allowing time to repair the lesion (PubMed:22521144). Mediates mutagenic uracil processing involved in antibody affinity maturation. Processes AICDA-induced U:G base mispairs at variable immunoglobulin (Ig) regions leading to the generation of transversion mutations (PubMed:12958596). Operates at switch sites of Ig constant regions where it mediates Ig isotype class switch recombination. Excises AICDA-induced uracil residues forming AP sites that are subsequently nicked by APEX1 endonuclease. The accumulation of staggered nicks in opposite strands results in double strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity) (PubMed:12958596). {ECO:0000250|UniProtKB:P97931, ECO:0000269|PubMed:12958596, ECO:0000269|PubMed:15967827, ECO:0000269|PubMed:17101234, ECO:0000269|PubMed:22521144, ECO:0000269|PubMed:7671300, ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9016624, ECO:0000269|PubMed:9776759}. |
P13051 | UNG | S9 | ochoa | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) | Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine (PubMed:12958596, PubMed:15967827, PubMed:17101234, PubMed:22521144, PubMed:7671300, PubMed:8900285, PubMed:9016624, PubMed:9776759). Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication. The resultant AP sites temporarily stall replication, allowing time to repair the lesion (PubMed:22521144). Mediates mutagenic uracil processing involved in antibody affinity maturation. Processes AICDA-induced U:G base mispairs at variable immunoglobulin (Ig) regions leading to the generation of transversion mutations (PubMed:12958596). Operates at switch sites of Ig constant regions where it mediates Ig isotype class switch recombination. Excises AICDA-induced uracil residues forming AP sites that are subsequently nicked by APEX1 endonuclease. The accumulation of staggered nicks in opposite strands results in double strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity) (PubMed:12958596). {ECO:0000250|UniProtKB:P97931, ECO:0000269|PubMed:12958596, ECO:0000269|PubMed:15967827, ECO:0000269|PubMed:17101234, ECO:0000269|PubMed:22521144, ECO:0000269|PubMed:7671300, ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9016624, ECO:0000269|PubMed:9776759}. |
P13807 | GYS1 | S8 | 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 | S10 | 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}. |
P14136 | GFAP | S8 | psp | Glial fibrillary acidic protein (GFAP) | GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. |
P14635 | CCNB1 | S9 | ochoa | G2/mitotic-specific cyclin-B1 | Essential for the control of the cell cycle at the G2/M (mitosis) transition. {ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:17495533, ECO:0000269|PubMed:27030811}. |
P14868 | DARS1 | S10 | ochoa | Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Cell proliferation-inducing gene 40 protein) | Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. {ECO:0000250|UniProtKB:P15178}. |
P15927 | RPA2 | S8 | psp | Replication protein A 32 kDa subunit (RP-A p32) (Replication factor A protein 2) (RF-A protein 2) (Replication protein A 34 kDa subunit) (RP-A p34) | 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. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. 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. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. 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. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542). {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}. |
P16401 | H1-5 | T9 | ochoa | Histone H1.5 (Histone H1a) (Histone H1b) (Histone H1s-3) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
P16989 | YBX3 | T8 | ochoa | Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB) | Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. |
P16989 | YBX3 | T9 | ochoa | Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB) | Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. |
P17028 | ZNF24 | S10 | ochoa | Zinc finger protein 24 (Retinoic acid suppression protein A) (RSG-A) (Zinc finger and SCAN domain-containing protein 3) (Zinc finger protein 191) (Zinc finger protein KOX17) | Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro. {ECO:0000250, ECO:0000269|PubMed:10585455}. |
P17029 | ZKSCAN1 | T10 | ochoa | Zinc finger protein with KRAB and SCAN domains 1 (Zinc finger protein 139) (Zinc finger protein 36) (Zinc finger protein KOX18) | May be involved in transcriptional regulation. |
P17096 | HMGA1 | S8 | ochoa | High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1) (High mobility group protein R) | HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. |
P17096 | HMGA1 | S9 | ochoa | High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1) (High mobility group protein R) | HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. |
P17252 | PRKCA | S10 | ochoa | Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13) | Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). {ECO:0000250|UniProtKB:P20444, ECO:0000269|PubMed:10848585, ECO:0000269|PubMed:11909826, ECO:0000269|PubMed:12724315, ECO:0000269|PubMed:12832403, ECO:0000269|PubMed:15016832, ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:18056764, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:21576361, ECO:0000269|PubMed:21806543, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:25313067, ECO:0000269|PubMed:28028151, ECO:0000269|PubMed:36040231, ECO:0000269|PubMed:9738012, ECO:0000269|PubMed:9830023, ECO:0000269|PubMed:9873035, ECO:0000269|PubMed:9927633}. |
P17480 | UBTF | T9 | ochoa | Nucleolar transcription factor 1 (Autoantigen NOR-90) (Upstream-binding factor 1) (UBF-1) | Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I (Pol I) through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element and can activate Pol I promoter escape. {ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16858408, ECO:0000269|PubMed:28777933, ECO:0000269|PubMed:7982918}. |
P17600 | SYN1 | S9 | ochoa|psp | Synapsin-1 (Brain protein 4.1) (Synapsin I) | Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity). {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951, ECO:0000269|PubMed:21441247, ECO:0000269|PubMed:23406870}. |
P17661 | DES | S8 | 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}. |
P17980 | PSMC3 | S9 | ochoa | 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000269|PubMed:1317798}. |
P18615 | NELFE | S9 | ochoa | Negative elongation factor E (NELF-E) (RNA-binding protein RD) | Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (PubMed:10199401, PubMed:27256882). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (PubMed:11940650, PubMed:12612062, PubMed:27256882). Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA (PubMed:18303858, PubMed:27256882, PubMed:27282391). {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:11940650, ECO:0000269|PubMed:12612062, ECO:0000269|PubMed:18303858, ECO:0000269|PubMed:27256882, ECO:0000269|PubMed:27282391}.; FUNCTION: (Microbial infection) The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. {ECO:0000269|PubMed:23884411}. |
P19388 | POLR2E | Y8 | ochoa | DNA-directed RNA polymerases I, II, and III subunit RPABC1 (RNA polymerases I, II, and III subunit ABC1) (DNA-directed RNA polymerase II 23 kDa polypeptide) (DNA-directed RNA polymerase II subunit E) (RPB5 homolog) (XAP4) | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPABC1 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. {ECO:0000250|UniProtKB:P20434, ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492, ECO:0000269|PubMed:9852112}. |
P22102 | GART | S10 | ochoa | Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase); Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART)] | Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway. {ECO:0000305|PubMed:12450384, ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:20631005, ECO:0000305|PubMed:2183217}. |
P22681 | CBL | S8 | ochoa | E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL) | E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250|UniProtKB:P22682, ECO:0000269|PubMed:10514377, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:17094949, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:17974561, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:28381567}. |
P22681 | CBL | S9 | ochoa | E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL) | E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). {ECO:0000250|UniProtKB:P22682, ECO:0000269|PubMed:10514377, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:17094949, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:17974561, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:28381567}. |
P23246 | SFPQ | S8 | psp | Splicing factor, proline- and glutamine-rich (100 kDa DNA-pairing protein) (hPOMp100) (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor) | DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA (PubMed:25765647). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as a transcriptional activator (PubMed:25765647). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as a transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF1-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity). Required for the assembly of nuclear speckles (PubMed:25765647). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). {ECO:0000250|UniProtKB:Q8VIJ6, ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:25765647, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}. |
P23381 | WARS1 | S8 | ochoa | Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Interferon-induced protein 53) (IFP53) (Tryptophanyl-tRNA synthetase) (TrpRS) (hWRS) [Cleaved into: T1-TrpRS; T2-TrpRS] | Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). {ECO:0000269|PubMed:1373391, ECO:0000269|PubMed:1761529, ECO:0000269|PubMed:28369220}.; FUNCTION: [Isoform 1]: Has no angiostatic activity. {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626}.; FUNCTION: [T2-TrpRS]: Possesses an angiostatic activity but has no aminoacylation activity (PubMed:11773625, PubMed:11773626, PubMed:14630953). Inhibits fluid shear stress-activated responses of endothelial cells (PubMed:14630953). Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (PubMed:14630953). {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626, ECO:0000269|PubMed:14630953}.; FUNCTION: [Isoform 2]: Has an angiostatic activity. {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626}. |
P23528 | CFL1 | S8 | ochoa | Cofilin-1 (18 kDa phosphoprotein) (p18) (Cofilin, non-muscle isoform) | Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11812157). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity). {ECO:0000250|UniProtKB:P18760, ECO:0000269|PubMed:11812157, ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:23633677}. |
P24534 | EEF1B2 | S8 | ochoa | Elongation factor 1-beta (EF-1-beta) (eEF-1B alpha) | Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1) (By similarity). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A (By similarity). {ECO:0000250|UniProtKB:P32471}. |
P24928 | POLR2A | S8 | ochoa | DNA-directed RNA polymerase II subunit RPB1 (RNA polymerase II subunit B1) (EC 2.7.7.6) (3'-5' exoribonuclease) (EC 3.1.13.-) (DNA-directed RNA polymerase II subunit A) (DNA-directed RNA polymerase III largest subunit) (RNA-directed RNA polymerase II subunit RPB1) (EC 2.7.7.48) | Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:28108474, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:8381534, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534). Through its unique C-terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA (By similarity) (PubMed:24207025, PubMed:26124092). {ECO:0000250|UniProtKB:G3MZY8, ECO:0000250|UniProtKB:P08775, ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26124092, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:28108474, ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:8381534, ECO:0000269|PubMed:9852112}.; FUNCTION: RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription. {ECO:0000269|PubMed:23395899}.; FUNCTION: (Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicase and transcriptase for the viral RNA circular genome. {ECO:0000269|PubMed:18032511}. |
P25490 | YY1 | Y8 | psp | Transcriptional repressor protein YY1 (Delta transcription factor) (INO80 complex subunit S) (NF-E1) (Yin and yang 1) (YY-1) | Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence (PubMed:1655281). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed (PubMed:11158321). Involved in DNA repair (PubMed:18026119, PubMed:28575647). In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation (PubMed:28575647). Recruits the PR-DUB complex to specific gene-regulatory regions (PubMed:20805357). {ECO:0000269|PubMed:11158321, ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:1655281, ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:20805357, ECO:0000269|PubMed:24326773, ECO:0000269|PubMed:25787250, ECO:0000269|PubMed:28575647}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements. {ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119}. |
P25787 | PSMA2 | S9 | ochoa | Proteasome subunit alpha type-2 (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3) (Proteasome subunit alpha-2) (alpha-2) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
P26639 | TARS1 | S8 | ochoa | Threonine--tRNA ligase 1, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase 1) | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity). {ECO:0000250|UniProtKB:Q9D0R2, ECO:0000269|PubMed:25824639, ECO:0000269|PubMed:31374204}. |
P26639 | TARS1 | S10 | ochoa | Threonine--tRNA ligase 1, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase 1) | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity). {ECO:0000250|UniProtKB:Q9D0R2, ECO:0000269|PubMed:25824639, ECO:0000269|PubMed:31374204}. |
P26641 | EEF1G | Y9 | ochoa | Elongation factor 1-gamma (EF-1-gamma) (eEF-1B gamma) | Probably plays a role in anchoring the complex to other cellular components. |
P26715 | KLRC1 | Y8 | psp | NKG2-A/NKG2-B type II integral membrane protein (CD159 antigen-like family member A) (NK cell receptor A) (NKG2-A/B-activating NK receptor) (CD antigen CD159a) | Immune inhibitory receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self (PubMed:18083576, PubMed:37264229, PubMed:9430220, PubMed:9486650). Upon HLA-E-peptide binding, transmits intracellular signals through two immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHP-1 and INPPL1/SHP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules (PubMed:12165520, PubMed:9485206). Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions (PubMed:30860984, PubMed:9430220, PubMed:9485206, PubMed:9486650). Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity (PubMed:12387742). On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens (PubMed:18064301). In HLA-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion (PubMed:30503213, PubMed:30860984). {ECO:0000269|PubMed:12165520, ECO:0000269|PubMed:12387742, ECO:0000269|PubMed:18064301, ECO:0000269|PubMed:18083576, ECO:0000269|PubMed:30503213, ECO:0000269|PubMed:30860984, ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:9430220, ECO:0000269|PubMed:9485206, ECO:0000269|PubMed:9486650}.; FUNCTION: (Microbial infection) Viruses like human cytomegalovirus have evolved an escape mechanism whereby virus-induced down-regulation of host MHC class I molecules is coupled to the binding of viral peptides to HLA-E, restoring HLA-E expression and inducing HLA-E-dependent NK cell immune tolerance to infected cells. Recognizes HLA-E in complex with human cytomegalovirus UL40-derived peptide (VMAPRTLIL) and inhibits NK cell cytotoxicity. {ECO:0000269|PubMed:10669413, ECO:0000269|PubMed:23335510}.; FUNCTION: (Microbial infection) May recognize HLA-E in complex with HIV-1 gag/Capsid protein p24-derived peptide (AISPRTLNA) on infected cells and may inhibit NK cell cytotoxicity, a mechanism that allows HIV-1 to escape immune recognition. {ECO:0000269|PubMed:15751767}.; FUNCTION: (Microbial infection) Upon SARS-CoV-2 infection, may contribute to functional exhaustion of cytotoxic NK cells and CD8-positive T cells (PubMed:32203188, PubMed:32859121). On NK cells, may recognize HLA-E in complex with SARS-CoV-2 S/Spike protein S1-derived peptide (LQPRTFLL) expressed on the surface of lung epithelial cells, inducing NK cell exhaustion and dampening antiviral immune surveillance (PubMed:32859121). {ECO:0000269|PubMed:32203188, ECO:0000269|PubMed:32859121}. |
P27105 | STOM | S10 | ochoa|psp | Stomatin (Erythrocyte band 7 integral membrane protein) (Erythrocyte membrane protein band 7.2) (Protein 7.2b) | Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity. |
P27707 | DCK | S8 | ochoa | Deoxycytidine kinase (dCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) | Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine (PubMed:12808445, PubMed:18377927, PubMed:19159229, PubMed:1996353, PubMed:20614893, PubMed:20637175). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents (PubMed:12808445). {ECO:0000269|PubMed:12808445, ECO:0000269|PubMed:18377927, ECO:0000269|PubMed:19159229, ECO:0000269|PubMed:1996353, ECO:0000269|PubMed:20614893, ECO:0000269|PubMed:20637175}. |
P27708 | CAD | S10 | ochoa | Multifunctional protein CAD (Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase) [Includes: Glutamine-dependent carbamoyl phosphate synthase (EC 6.3.5.5); Glutamine amidotransferase (GATase) (GLNase) (EC 3.5.1.2); Ammonium-dependent carbamoyl phosphate synthase (CPS) (CPSase) (EC 6.3.4.16); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)] | Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000269|PubMed:24332717}. |
P28066 | PSMA5 | Y8 | ochoa | Proteasome subunit alpha type-5 (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome subunit alpha-5) (alpha-5) (Proteasome zeta chain) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
P28290 | ITPRID2 | S8 | 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 |
P28347 | TEAD1 | S9 | ochoa | Transcriptional enhancer factor TEF-1 (NTEF-1) (Protein GT-IIC) (TEA domain family member 1) (TEAD-1) (Transcription factor 13) (TCF-13) | Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, 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. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. |
P29350 | PTPN6 | S10 | ochoa | Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase) (Protein-tyrosine phosphatase 1C) (PTP-1C) (Protein-tyrosine phosphatase SHP-1) (SH-PTP1) | Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis (PubMed:14739280, PubMed:29925997). Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:21258366, PubMed:9733788). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:11907092, PubMed:14739280, PubMed:37932456, PubMed:38166031). Modulates the signaling of several cytokine receptors including IL-4 receptor (PubMed:9065461). Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling (PubMed:34811497, PubMed:38532423). Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Also acts as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A (PubMed:37595871). {ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:11266449, ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:29925997, ECO:0000269|PubMed:34811497, ECO:0000269|PubMed:37595871, ECO:0000269|PubMed:37932456, ECO:0000269|PubMed:38166031, ECO:0000269|PubMed:38532423, ECO:0000269|PubMed:9065461, ECO:0000269|PubMed:9733788}. |
P29590 | PML | S8 | ochoa|psp | 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}. |
P30153 | PPP2R1A | S9 | ochoa | Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2Aa) (Medium tumor antigen-associated 61 kDa protein) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha) | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:15525651, PubMed:16580887, PubMed:33243860, PubMed:33633399, PubMed:34004147, PubMed:8694763). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (PubMed:16580887). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:18782753, PubMed:33633399). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753, PubMed:33633399). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex (PubMed:33243860, PubMed:34004147). The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, acts as a scaffolding subunit for PPP2CA, which catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, thereby preventing transcriptional elongation (PubMed:33243860, PubMed:34004147). Regulates the recruitment of the SKA complex to kinetochores (PubMed:28982702). {ECO:0000250|UniProtKB:Q76MZ3, ECO:0000269|PubMed:15525651, ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:28982702, ECO:0000269|PubMed:33243860, ECO:0000269|PubMed:33633399, ECO:0000269|PubMed:34004147, ECO:0000269|PubMed:8694763}. |
P30154 | PPP2R1B | T9 | ochoa | Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta) | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. |
P30519 | HMOX2 | S8 | ochoa | Heme oxygenase 2 (HO-2) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 2 soluble form] | [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:7890772}.; FUNCTION: [Heme oxygenase 2 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000269|PubMed:7890772}. |
P30566 | ADSL | S9 | ochoa | Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) | Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. {ECO:0000269|PubMed:10888601}. |
P31321 | PRKAR1B | S9 | ochoa | cAMP-dependent protein kinase type I-beta regulatory subunit | Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:20819953}. |
P32298 | GRK4 | S10 | psp | G protein-coupled receptor kinase 4 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK4) (ITI1) | Specifically phosphorylates the activated forms of G protein-coupled receptors. GRK4-alpha can phosphorylate rhodopsin and its activity is inhibited by calmodulin; the other three isoforms do not phosphorylate rhodopsin and do not interact with calmodulin. GRK4-alpha and GRK4-gamma phosphorylate DRD3. Phosphorylates ADRB2. {ECO:0000269|PubMed:19520868, ECO:0000269|PubMed:8626439}. |
P35240 | NF2 | S10 | ochoa|psp | Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomerlin) (Schwannomin) | Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}. |
P35249 | RFC4 | S9 | ochoa | Replication factor C subunit 4 (Activator 1 37 kDa subunit) (A1 37 kDa subunit) (Activator 1 subunit 4) (Replication factor C 37 kDa subunit) (RF-C 37 kDa subunit) (RFC37) | Subunit of the replication factor C (RFC) complex which acts during elongation of primed DNA templates by DNA polymerases delta and epsilon, and is necessary for ATP-dependent loading of proliferating cell nuclear antigen (PCNA) onto primed DNA. The RFC4 subunit probably functions as a scaffold on which the other complex components can assemble. {ECO:0000269|PubMed:39106866, ECO:0000269|PubMed:9488738}. |
P35269 | GTF2F1 | S8 | ochoa | General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74) | TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269|PubMed:10428810}. |
P35579 | MYH9 | Y9 | ochoa | Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000269|PubMed:20944748, ECO:0000269|PubMed:39048823}. |
P35712 | SOX6 | S8 | ochoa | Transcription factor SOX-6 | Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation (Probable). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis. Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts. Binds to the proximal promoter region of the myelin protein MPZ gene, and is thereby involved in the differentiation of oligodendroglia in the developing spinal tube. Binds to the gene promoter of MBP and acts as a transcriptional repressor (By similarity). {ECO:0000250|UniProtKB:P40645, ECO:0000305|PubMed:32442410}. |
P35749 | MYH11 | S8 | ochoa | Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) | Muscle contraction. |
P36021 | SLC16A2 | S8 | ochoa | Monocarboxylate transporter 8 (MCT 8) (Monocarboxylate transporter 7) (MCT 7) (Solute carrier family 16 member 2) (X-linked PEST-containing transporter) | Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient. Major substrates are the iodothyronines T3 and T4 and to a lesser extent rT3 and 3,3-diiodothyronine (3,3'-T2) (PubMed:16887882, PubMed:18337592, PubMed:20628049, PubMed:23550058, PubMed:26426690, PubMed:27805744, PubMed:31436139). Acts as an important mediator of thyroid hormone transport, especially T3, through the blood-brain barrier (Probable) (PubMed:28526555). {ECO:0000269|PubMed:16887882, ECO:0000269|PubMed:18337592, ECO:0000269|PubMed:20628049, ECO:0000269|PubMed:23550058, ECO:0000269|PubMed:26426690, ECO:0000269|PubMed:27805744, ECO:0000269|PubMed:28526555, ECO:0000269|PubMed:31436139, ECO:0000305|PubMed:18636565}. |
P37802 | TAGLN2 | Y8 | ochoa | Transgelin-2 (Epididymis tissue protein Li 7e) (SM22-alpha homolog) | None |
P38919 | EIF4A3 | T9 | ochoa | Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic initiation factor 4A-like NUK-34) (Eukaryotic translation initiation factor 4A isoform 3) (Nuclear matrix protein 265) (NMP 265) (hNMP 265) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed] | ATP-dependent RNA helicase (PubMed:16170325). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:16170325, PubMed:16209946, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly (PubMed:22203037). Involved in craniofacial development (PubMed:24360810). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:20479275, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:24360810, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. |
P38919 | EIF4A3 | S10 | ochoa | Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic initiation factor 4A-like NUK-34) (Eukaryotic translation initiation factor 4A isoform 3) (Nuclear matrix protein 265) (NMP 265) (hNMP 265) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed] | ATP-dependent RNA helicase (PubMed:16170325). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:16170325, PubMed:16209946, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly (PubMed:22203037). Involved in craniofacial development (PubMed:24360810). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:20479275, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:24360810, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. |
P40121 | CAPG | S8 | ochoa | Macrophage-capping protein (Actin regulatory protein CAP-G) | Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. |
P40121 | CAPG | S10 | ochoa | Macrophage-capping protein (Actin regulatory protein CAP-G) | Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. |
P40855 | PEX19 | S9 | ochoa | Peroxisomal biogenesis factor 19 (33 kDa housekeeping protein) (Peroxin-19) (Peroxisomal farnesylated protein) | Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53. {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11883941, ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061}. |
P41273 | TNFSF9 | S8 | ochoa | Tumor necrosis factor ligand superfamily member 9 (4-1BB ligand) (4-1BBL) | Cytokine that binds to TNFRSF9. Induces the proliferation of activated peripheral blood T-cells. May have a role in activation-induced cell death (AICD). May play a role in cognate interactions between T-cells and B-cells/macrophages. {ECO:0000269|PubMed:20032458}. |
P41567 | EIF1 | S9 | ochoa | Eukaryotic translation initiation factor 1 (eIF1) (A121) (Protein translation factor SUI1 homolog) (Sui1iso1) | Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:12435632, PubMed:14600024, PubMed:9732867). Together with eIF1A (EIF1AX), EIF1 facilitates scanning and is essential for start codon recognition on the basis of AUG nucleotide context and location relative to the 5'-cap (PubMed:12435632, PubMed:14600024, PubMed:9732867). Participates to initiation codon selection by influencing the conformation of the 40S ribosomal subunit and the positions of bound mRNA and initiator tRNA; this is possible after its binding to the interface surface of the platform of the 40S ribosomal subunit close to the P-site (PubMed:14600024). Together with eIF1A (EIF1AX), also regulates the opening and closing of the mRNA binding channel, which ensures mRNA recruitment, scanning and the fidelity of initiation codon selection (PubMed:9732867). Continuously monitors and protects against premature and partial base-pairing of codons in the 5'-UTR with the anticodon of initiator tRNA (PubMed:12435632, PubMed:9732867). Together with eIF1A (EIF1AX), acts for ribosomal scanning, promotion of the assembly of 48S complex at the initiation codon (43S PIC becomes 48S PIC after the start codon is reached), and dissociation of aberrant complexes (PubMed:9732867). Interacts with EIF4G1, which in a mutual exclusive interaction associates either with EIF1 or with EIF4E on a common binding site (PubMed:29987188). EIF4G1-EIF1 complex promotes ribosome scanning (on both short and long 5'UTR), leaky scanning (on short 5'UTR) which is the bypass of the initial start codon, and discrimination against cap-proximal AUG (PubMed:29987188). Is probably maintained within the 43S PIC in open conformation thanks to eIF1A-EIF5 interaction (PubMed:24319994). Once the correct start codon is reached, EIF1 is physically excluded from the decoding site, shifting the PIC into the closed conformation and arresting it at the start codon (PubMed:22813744). {ECO:0000269|PubMed:12435632, ECO:0000269|PubMed:14600024, ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:29987188, ECO:0000269|PubMed:9732867}. |
P41743 | PRKCI | S8 | ochoa | Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (PRKC-lambda/iota) (aPKC-lambda/iota) (nPKC-iota) | Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). {ECO:0000250|UniProtKB:F1M7Y5, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326, ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978, ECO:0000269|PubMed:9346882}. |
P41743 | PRKCI | T9 | ochoa | Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (PRKC-lambda/iota) (aPKC-lambda/iota) (nPKC-iota) | Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). {ECO:0000250|UniProtKB:F1M7Y5, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326, ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978, ECO:0000269|PubMed:9346882}. |
P42566 | EPS15 | S8 | 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}. |
P42575 | CASP2 | S8 | ochoa | Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12] | Is a regulator of the cascade of caspases responsible for apoptosis execution (PubMed:11156409, PubMed:15073321, PubMed:8087842). Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (PubMed:15073321). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (PubMed:15073321). {ECO:0000269|PubMed:11156409, ECO:0000269|PubMed:15073321, ECO:0000269|PubMed:8087842}.; FUNCTION: [Isoform 1]: Acts as a positive regulator of apoptosis. {ECO:0000269|PubMed:8087842}.; FUNCTION: [Isoform 2]: Acts as a negative regulator of apoptosis. {ECO:0000269|PubMed:8087842}.; FUNCTION: [Isoform 3]: May function as an endogenous apoptosis inhibitor that antagonizes caspase activation and cell death. {ECO:0000269|PubMed:11156409}. |
P42771 | CDKN2A | S8 | psp | Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (Multiple tumor suppressor 1) (MTS-1) (p16-INK4a) (p16-INK4) (p16INK4A) | Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. {ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:7972006}. |
P43243 | MATR3 | S8 | ochoa | Matrin-3 | May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:32245947}. |
P43243 | MATR3 | S9 | 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}. |
P45973 | CBX5 | T8 | ochoa | Chromobox protein homolog 5 (Antigen p25) (Heterochromatin protein 1 homolog alpha) (HP1 alpha) | Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph) (PubMed:19783980). May contribute to the association of heterochromatin with the inner nuclear membrane by interactions with the lamin-B receptor (LBR) (PubMed:19783980). Involved in the formation of kinetochore through interaction with the MIS12 complex subunit NSL1 (PubMed:19783980, PubMed:20231385). Required for the formation of the inner centromere (PubMed:20231385). {ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20231385}. |
P46527 | CDKN1B | S10 | ochoa|psp | Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) | Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. {ECO:0000269|PubMed:10831586, ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:19075005, ECO:0000269|PubMed:28666995}. |
P46939 | UTRN | S10 | ochoa | Utrophin (Dystrophin-related protein 1) (DRP-1) | May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. |
P47755 | CAPZA2 | S9 | ochoa | F-actin-capping protein subunit alpha-2 (CapZ alpha-2) | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. |
P48378 | RFX2 | S10 | ochoa | DNA-binding protein RFX2 (Regulatory factor X 2) | Transcription factor that acts as a key regulator of spermatogenesis. Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (By similarity). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters (PubMed:10330134). Probably activates transcription of the testis-specific histone gene H1-6 (By similarity). {ECO:0000250|UniProtKB:P48379, ECO:0000269|PubMed:10330134}. |
P48382 | RFX5 | S10 | ochoa | DNA-binding protein RFX5 (Regulatory factor X 5) | Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters. |
P48426 | PIP4K2A | S9 | ochoa | Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (PIP5KIII) (Phosphatidylinositol 5-Phosphate 4-Kinase) (PI5P4Kalpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(4)P-5-kinase B isoform) (PtdIns(4)P-5-kinase C isoform) (PtdIns(5)P-4-kinase isoform 2-alpha) | Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:23326584, PubMed:9367159). Has both ATP- and GTP-dependent kinase activities (PubMed:26774281). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (PubMed:18364242). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). Required for lysosome-peroxisome membrane contacts and intracellular cholesterol transport through modulating peroxisomal PtdIns(4,5)P2 level (PubMed:29353240). In collaboration with PIP4K2B, has a role in mediating autophagy in times of nutrient stress (By similarity). Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism (PubMed:31091439). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (By similarity). Negatively regulates insulin signaling through a catalytic-independent mechanism (PubMed:31091439). PIP4Ks interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (PubMed:31091439). {ECO:0000250|UniProtKB:O70172, ECO:0000250|UniProtKB:Q9R0I8, ECO:0000269|PubMed:18364242, ECO:0000269|PubMed:23326584, ECO:0000269|PubMed:26774281, ECO:0000269|PubMed:29353240, ECO:0000269|PubMed:31091439, ECO:0000269|PubMed:9367159}. |
P48426 | PIP4K2A | S10 | ochoa | Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (PIP5KIII) (Phosphatidylinositol 5-Phosphate 4-Kinase) (PI5P4Kalpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(4)P-5-kinase B isoform) (PtdIns(4)P-5-kinase C isoform) (PtdIns(5)P-4-kinase isoform 2-alpha) | Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:23326584, PubMed:9367159). Has both ATP- and GTP-dependent kinase activities (PubMed:26774281). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (PubMed:18364242). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). Required for lysosome-peroxisome membrane contacts and intracellular cholesterol transport through modulating peroxisomal PtdIns(4,5)P2 level (PubMed:29353240). In collaboration with PIP4K2B, has a role in mediating autophagy in times of nutrient stress (By similarity). Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism (PubMed:31091439). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (By similarity). Negatively regulates insulin signaling through a catalytic-independent mechanism (PubMed:31091439). PIP4Ks interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (PubMed:31091439). {ECO:0000250|UniProtKB:O70172, ECO:0000250|UniProtKB:Q9R0I8, ECO:0000269|PubMed:18364242, ECO:0000269|PubMed:23326584, ECO:0000269|PubMed:26774281, ECO:0000269|PubMed:29353240, ECO:0000269|PubMed:31091439, ECO:0000269|PubMed:9367159}. |
P48506 | GCLC | S8 | ochoa | Glutamate--cysteine ligase catalytic subunit (EC 6.3.2.2) (GCS heavy chain) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) | Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis. {ECO:0000269|PubMed:9675072}. |
P48651 | PTDSS1 | T9 | ochoa | Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) | Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (PubMed:19014349, PubMed:24241535). Catalyzes mainly the conversion of phosphatidylcholine (PubMed:19014349, PubMed:24241535). Also converts, in vitro and to a lesser extent, phosphatidylethanolamine (PubMed:19014349, PubMed:24241535). {ECO:0000269|PubMed:19014349, ECO:0000269|PubMed:24241535}. |
P49137 | MAPKAPK2 | S9 | psp | MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1) | Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:11844797, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:12565831, ECO:0000269|PubMed:14499342, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:16456544, ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:26616734, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8280084, ECO:0000269|PubMed:8774846}. |
P49321 | NASP | T8 | 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}. |
P49356 | FNTB | T8 | ochoa | Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) | Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}. |
P49356 | FNTB | Y9 | ochoa | Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) | Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}. |
P49593 | PPM1F | S9 | ochoa | Protein phosphatase 1F (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Partner of PIX 2) (Protein fem-2 homolog) (hFem-2) | Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis. |
P49593 | PPM1F | S10 | ochoa | Protein phosphatase 1F (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Partner of PIX 2) (Protein fem-2 homolog) (hFem-2) | Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis. |
P49736 | MCM2 | T9 | ochoa | DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28) | Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677). {ECO:0000269|PubMed:26196677, ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232, ECO:0000269|PubMed:8175912}. |
P49810 | PSEN2 | S9 | psp | Presenilin-2 (PS-2) (EC 3.4.23.-) (AD3LP) (AD5) (E5-1) (STM-2) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit] | Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis (PubMed:16959576). Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria (PubMed:21285369). {ECO:0000269|PubMed:10497236, ECO:0000269|PubMed:10652302, ECO:0000269|PubMed:16959576, ECO:0000269|PubMed:21285369}. |
P49841 | GSK3B | T8 | ochoa | Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1) | Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:8397507). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:8397507). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (PubMed:8397507). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (PubMed:12554650). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (PubMed:1846781). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (PubMed:9072970). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (PubMed:14690523). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (PubMed:14690523). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (PubMed:9819408). Is necessary for the establishment of neuronal polarity and axon outgrowth (PubMed:20067585). Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (PubMed:18348280). Phosphorylates ZC3HAV1 which enhances its antiviral activity (PubMed:22514281). Phosphorylates SNAI1, leading to its ubiquitination and proteasomal degradation (PubMed:15448698, PubMed:15647282, PubMed:25827072, PubMed:29059170). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (PubMed:20932480). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 (PubMed:19946213, PubMed:28903391). Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (PubMed:19946213). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation (PubMed:28903391). Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (PubMed:18846110). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (PubMed:17050006, PubMed:28992046). Phosphorylates mTORC2 complex component RICTOR at 'Ser-1235' in response to endoplasmic stress, inhibiting mTORC2 (PubMed:21343617). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity). Phosphorylates interleukin-22 receptor subunit IL22RA1, preventing its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P18266, ECO:0000250|UniProtKB:Q9WV60, ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20067585, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25827072, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:29059170, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}. |
P49841 | GSK3B | S9 | ochoa|psp | Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1) | Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:8397507). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:8397507). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (PubMed:8397507). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (PubMed:12554650). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (PubMed:1846781). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (PubMed:9072970). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (PubMed:14690523). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (PubMed:14690523). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (PubMed:9819408). Is necessary for the establishment of neuronal polarity and axon outgrowth (PubMed:20067585). Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (PubMed:18348280). Phosphorylates ZC3HAV1 which enhances its antiviral activity (PubMed:22514281). Phosphorylates SNAI1, leading to its ubiquitination and proteasomal degradation (PubMed:15448698, PubMed:15647282, PubMed:25827072, PubMed:29059170). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (PubMed:20932480). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 (PubMed:19946213, PubMed:28903391). Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (PubMed:19946213). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation (PubMed:28903391). Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (PubMed:18846110). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (PubMed:17050006, PubMed:28992046). Phosphorylates mTORC2 complex component RICTOR at 'Ser-1235' in response to endoplasmic stress, inhibiting mTORC2 (PubMed:21343617). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity). Phosphorylates interleukin-22 receptor subunit IL22RA1, preventing its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P18266, ECO:0000250|UniProtKB:Q9WV60, ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20067585, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25827072, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:29059170, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}. |
P49914 | MTHFS | S8 | ochoa | 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase) | Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltetrahydrofolate. {ECO:0000269|PubMed:8522195}. |
P49915 | GMPS | S8 | ochoa | GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) | Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate. {ECO:0000269|PubMed:8089153}. |
P50150 | GNG4 | S9 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. {ECO:0000305}. |
P50151 | GNG10 | S8 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but not with beta-3. |
P50402 | EMD | S8 | 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}. |
P50579 | METAP2 | S10 | ochoa | Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (p67) (p67eIF2) (Peptidase M) | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. |
P50851 | LRBA | S10 | 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}. |
P50991 | CCT4 | S9 | ochoa|psp | T-complex protein 1 subunit delta (TCP-1-delta) (EC 3.6.1.-) (CCT-delta) (Chaperonin containing T-complex polypeptide 1 subunit 4) (Stimulator of TAR RNA-binding) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
P51003 | PAPOLA | S10 | ochoa | Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha) | Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000269|PubMed:19224921}. |
P51798 | CLCN7 | S9 | ochoa | H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7) | Slowly voltage-gated channel mediating the exchange of chloride ions against protons (PubMed:18449189, PubMed:21527911). Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH (PubMed:18449189, PubMed:21527911, PubMed:31155284). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity). {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911, ECO:0000269|PubMed:31155284}. |
P51965 | UBE2E1 | S9 | ochoa | Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1) | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. Catalyzes monoubiquitination of other proteins in both an E3-dependent and E3-independent manner (PubMed:27237050). {ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27237050}. |
P52292 | KPNA2 | T9 | ochoa|psp | Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha) | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:7604027, PubMed:7754385). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with KPNA1 and Transportin-1/TNPO1 (PubMed:35446349). {ECO:0000269|PubMed:28991411, ECO:0000269|PubMed:32130408, ECO:0000269|PubMed:35446349, ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:7754385}. |
P52701 | MSH6 | S9 | ochoa | DNA mismatch repair protein Msh6 (hMSH6) (G/T mismatch-binding protein) (GTBP) (GTMBP) (MutS protein homolog 6) (MutS-alpha 160 kDa subunit) (p160) | Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}. |
P52732 | KIF11 | S8 | ochoa | Kinesin-like protein KIF11 (Kinesin-like protein 1) (Kinesin-like spindle protein HKSP) (Kinesin-related motor protein Eg5) (Thyroid receptor-interacting protein 5) (TR-interacting protein 5) (TRIP-5) | Motor protein required for establishing a bipolar spindle and thus contributing to chromosome congression during mitosis (PubMed:19001501, PubMed:37728657). Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769). {ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:23857769}. |
P52907 | CAPZA1 | S9 | ochoa|psp | F-actin-capping protein subunit alpha-1 (CapZ alpha-1) | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (PubMed:22891260). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250|UniProtKB:A0PFK5, ECO:0000269|PubMed:22891260}. |
P53367 | ARFIP1 | S9 | ochoa | Arfaptin-1 (ADP-ribosylation factor-interacting protein 1) | Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network (PubMed:22981988). Mechanistically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold (PubMed:22981988, PubMed:9038142). Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs (PubMed:22981988). In turn, ARFs induce fission (PubMed:22981988). Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells (PubMed:22981988). {ECO:0000269|PubMed:22981988, ECO:0000269|PubMed:9038142}. |
P53567 | CEBPG | S9 | ochoa | CCAAT/enhancer-binding protein gamma (C/EBP gamma) | Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53568, ECO:0000269|PubMed:7665092}. |
P53674 | CRYBB1 | S8 | ochoa | Beta-crystallin B1 (Beta-B1 crystallin) | Crystallins are the dominant structural components of the vertebrate eye lens. |
P53999 | SUB1 | S9 | ochoa | Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14) | General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269|PubMed:16605275, ECO:0000269|PubMed:16689930, ECO:0000269|PubMed:7628453, ECO:0000269|PubMed:8062391, ECO:0000269|PubMed:8062392, ECO:0000269|PubMed:9360603, ECO:0000269|PubMed:9482861}. |
P53999 | SUB1 | S10 | 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}. |
P54619 | PRKAG1 | S9 | ochoa | 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:21680840, PubMed:24563466). 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:21680840, PubMed:24563466). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:21680840, PubMed:24563466). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:21680840, PubMed:24563466). Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits (PubMed:21680840, PubMed:24563466). ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit (PubMed:21680840, PubMed:24563466). ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (PubMed:21680840, PubMed:24563466). {ECO:0000269|PubMed:21680840, ECO:0000269|PubMed:24563466}. |
P54619 | PRKAG1 | S10 | ochoa | 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) | AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:21680840, PubMed:24563466). 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:21680840, PubMed:24563466). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:21680840, PubMed:24563466). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:21680840, PubMed:24563466). Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits (PubMed:21680840, PubMed:24563466). ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit (PubMed:21680840, PubMed:24563466). ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (PubMed:21680840, PubMed:24563466). {ECO:0000269|PubMed:21680840, ECO:0000269|PubMed:24563466}. |
P54707 | ATP12A | Y9 | ochoa | Potassium-transporting ATPase alpha chain 2 (HK alpha 2) (Non-gastric H(+)/K(+) ATPase subunit alpha) (EC 7.2.2.19) (Non-gastric Na(+)/K(+) ATPase subunit alpha) (EC 7.2.2.13) (Proton pump) (Sodium pump) | The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+) ATPase pump which transports K(+) ions in exchange for Na(+) and/or H(+) ions across the apical membrane of epithelial cells. Uses ATP as an energy source to pump K(+) ions into the cell while transporting Na(+) and/or H(+) ions to the extracellular compartment (PubMed:11341842, PubMed:7485470, PubMed:8853415, PubMed:9774385). Involved in the maintenance of electrolyte homeostasis through K(+) ion absorption in kidney and colon (By similarity). In the airway epithelium, may play a primary role in mucus acidification regulating its viscosity and clearance (PubMed:29391451). {ECO:0000250|UniProtKB:Q9Z1W8, ECO:0000269|PubMed:11341842, ECO:0000269|PubMed:29391451, ECO:0000269|PubMed:7485470, ECO:0000269|PubMed:8853415, ECO:0000269|PubMed:9774385}. |
P54709 | ATP1B3 | S8 | ochoa | Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) (ATPB-3) (CD antigen CD298) | This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known. |
P55010 | EIF5 | S8 | ochoa | Eukaryotic translation initiation factor 5 (eIF-5) | Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744). {ECO:0000269|PubMed:11166181, ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:24319994}. |
P55010 | EIF5 | S10 | ochoa | Eukaryotic translation initiation factor 5 (eIF-5) | Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744). {ECO:0000269|PubMed:11166181, ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:24319994}. |
P55055 | NR1H2 | S8 | ochoa | Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor NER) (Nuclear receptor subfamily 1 group H member 2) (Ubiquitously-expressed nuclear receptor) | Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}. |
P55209 | NAP1L1 | S10 | ochoa | Nucleosome assembly protein 1-like 1 (NAP-1-related protein) (hNRP) | Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity). {ECO:0000250|UniProtKB:P28656, ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:24798879, ECO:0000269|PubMed:26841755, ECO:0000269|PubMed:28369616}.; FUNCTION: (Microbial infection) Positively regulates Epstein-Barr virus reactivation in epithelial cells through the induction of viral BZLF1 expression. {ECO:0000269|PubMed:23691099}.; FUNCTION: (Microbial infection) Together with human herpesvirus 8 protein LANA1, assists the proper assembly of the nucleosome on the replicated viral DNA. {ECO:0000269|PubMed:27599637}. |
P56211 | ARPP19 | S10 | ochoa | cAMP-regulated phosphoprotein 19 (ARPP-19) | Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis (PubMed:38123684). Inhibition of PP2A is enhanced when ARPP19 is phosphorylated (PubMed:38123684). When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (PubMed:21164014). May indirectly enhance GAP-43 expression (By similarity). {ECO:0000250|UniProtKB:Q712U5, ECO:0000269|PubMed:21164014, ECO:0000269|PubMed:38123684}. |
P56693 | SOX10 | S8 | ochoa | Transcription factor SOX-10 | Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (PubMed:21965087). Transcriptional activator of MBP, via binding to the gene promoter (By similarity). {ECO:0000250|UniProtKB:O55170, ECO:0000250|UniProtKB:Q04888, ECO:0000269|PubMed:21965087}. |
P57075 | UBASH3A | Y9 | ochoa | Ubiquitin-associated and SH3 domain-containing protein A (Cbl-interacting protein 4) (CLIP4) (Suppressor of T-cell receptor signaling 2) (STS-2) (T-cell ubiquitin ligand 1) (TULA-1) | Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. Exhibits negligible protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain. {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17382318, ECO:0000269|PubMed:18189269}. |
P57740 | NUP107 | S10 | ochoa | Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107) | Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:12552102, PubMed:15229283, PubMed:30179222). Required for the assembly of peripheral proteins into the NPC (PubMed:12552102, PubMed:15229283). May anchor NUP62 to the NPC (PubMed:15229283). Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:12552102, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:30179222}. |
P58005 | SESN3 | S9 | ochoa | Sestrin-3 (EC 1.11.1.-) | May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway (PubMed:25263562). May also regulate the insulin-receptor signaling pathway through activation of TORC2 (By similarity). This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). {ECO:0000250|UniProtKB:P58004, ECO:0000250|UniProtKB:Q9CYP7, ECO:0000269|PubMed:25263562}. |
P58340 | MLF1 | S8 | ochoa | Myeloid leukemia factor 1 (Myelodysplasia-myeloid leukemia factor 1) | Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus. {ECO:0000269|PubMed:15861129}. |
P59768 | GNG2 | S8 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I) | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems (PubMed:29925951, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:35714614, PubMed:35835867, PubMed:36087581, PubMed:36989299, PubMed:37327704, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118, PubMed:38552625). The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (PubMed:29925951, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:35714614, PubMed:35835867, PubMed:36087581, PubMed:36989299, PubMed:37327704, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118, PubMed:38552625). {ECO:0000269|PubMed:29925951, ECO:0000269|PubMed:33762731, ECO:0000269|PubMed:34239069, ECO:0000269|PubMed:35610220, ECO:0000269|PubMed:35714614, ECO:0000269|PubMed:35835867, ECO:0000269|PubMed:36087581, ECO:0000269|PubMed:36989299, ECO:0000269|PubMed:37327704, ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37935377, ECO:0000269|PubMed:37963465, ECO:0000269|PubMed:38168118, ECO:0000269|PubMed:38552625}. |
P60468 | SEC61B | T9 | ochoa | Protein transport protein Sec61 subunit beta | Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:19121997). {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:19121997, ECO:0000269|PubMed:32820719, ECO:0000269|PubMed:36261522}. |
P60520 | GABARAPL2 | S10 | ochoa | Gamma-aminobutyric acid receptor-associated protein-like 2 (GABA(A) receptor-associated protein-like 2) (Ganglioside expression factor 2) (GEF-2) (General protein transport factor p16) (Golgi-associated ATPase enhancer of 16 kDa) (GATE-16) (MAP1 light chain 3-related protein) | Ubiquitin-like modifier involved in intra-Golgi traffic (By similarity). Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation (By similarity). It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy (PubMed:20418806, PubMed:23209295). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:20418806, PubMed:23209295). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295). {ECO:0000250|UniProtKB:P60519, ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}. |
P60866 | RPS20 | T9 | ochoa | Small ribosomal subunit protein uS10 (40S ribosomal protein S20) | Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). {ECO:0000269|PubMed:23636399}. |
P61254 | RPL26 | S9 | ochoa | Large ribosomal subunit protein uL24 (60S ribosomal protein L26) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:26100019}. |
P61266 | STX1B | S10 | ochoa | Syntaxin-1B (Syntaxin-1B1) (Syntaxin-1B2) | Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). {ECO:0000250}. |
P61457 | PCBD1 | S9 | ochoa | Pterin-4-alpha-carbinolamine dehydratase (PHS) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Dimerization cofactor of hepatocyte nuclear factor 1-alpha) (DCoH) (Dimerization cofactor of HNF1) (Phenylalanine hydroxylase-stimulating protein) (Pterin carbinolamine dehydratase) (PCD) | Involved in tetrahydrobiopterin biosynthesis (By similarity). Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription (By similarity). Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also acts as a coactivator for HNF1B-dependent transcription (PubMed:24204001). {ECO:0000250|UniProtKB:P61459, ECO:0000269|PubMed:24204001}. |
P61923 | COPZ1 | S9 | ochoa | Coatomer subunit zeta-1 (Zeta-1-coat protein) (Zeta-1 COP) | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). {ECO:0000250|UniProtKB:P53600}. |
P62070 | RRAS2 | S10 | ochoa | Ras-related protein R-Ras2 (EC 3.6.5.2) (Ras-like protein TC21) (Teratocarcinoma oncogene) | GTP-binding protein with GTPase activity, involved in the regulation of MAPK signaling pathway and thereby controlling multiple cellular processes (PubMed:31130282, PubMed:31130285, PubMed:39809765). Regulates craniofacial development (PubMed:31130282, PubMed:31130285). {ECO:0000269|PubMed:31130282, ECO:0000269|PubMed:31130285, ECO:0000269|PubMed:39809765}. |
P62249 | RPS16 | S9 | ochoa | Small ribosomal subunit protein uS9 (40S ribosomal protein S16) | Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. |
P62258 | YWHAE | Y9 | ochoa | 14-3-3 protein epsilon (14-3-3E) | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:21189250). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35343654). Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326). Plays a positive role in the antiviral signaling pathway upstream of TBK1 via interaction with RIGI (PubMed:37555661). Mechanistically, directs RIGI redistribution from the cytosol to mitochondrial associated membranes where it mediates MAVS-dependent innate immune signaling during viral infection (PubMed:22607805). Plays a role in proliferation inhibition and cell cycle arrest by exporting HNRNPC from the nucleus to the cytoplasm to be degraded by ubiquitination (PubMed:37599448). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:21189250, ECO:0000269|PubMed:22607805, ECO:0000269|PubMed:35343654, ECO:0000269|PubMed:37555661, ECO:0000269|PubMed:37599448}. |
P62273 | RPS29 | S9 | ochoa | Small ribosomal subunit protein uS14 (40S ribosomal protein S29) | Component of the small ribosomal subunit (PubMed:23636399, PubMed:25901680, PubMed:25957688). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688}. |
P62316 | SNRPD2 | S9 | ochoa | Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) | Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:32494006}. |
P62491 | RAB11A | Y8 | ochoa | Ras-related protein Rab-11A (Rab-11) (EC 3.6.5.2) (YL8) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:15601896, PubMed:15689490, PubMed:17462998, PubMed:19542231, PubMed:20026645, PubMed:20890297, PubMed:21282656, PubMed:26032412). The small Rab GTPase RAB11A regulates endocytic recycling (PubMed:20026645). Forms a functional Rab11/RAB11FIP3/dynein complex 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). Acts as a major regulator of membrane delivery during cytokinesis (PubMed:15601896). Together with MYO5B and RAB8A participates in epithelial cell polarization (PubMed:21282656). Together with Rabin8/RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells (PubMed:17462998). Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane (PubMed:19542231). Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane (PubMed:15689490). Regulates the recycling of FCGRT (receptor of Fc region of monomeric IgG) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes (By similarity). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879, PubMed:31204173). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-endososomal dependent export route via interaction with WDR44 (PubMed:32344433). {ECO:0000250|UniProtKB:P62490, ECO:0000250|UniProtKB:P62492, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26032412, ECO:0000269|PubMed:31204173, ECO:0000269|PubMed:32344433}. |
P62820 | RAB1A | Y8 | ochoa | Ras-related protein Rab-1A (EC 3.6.5.2) (YPT1-related protein) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion (PubMed:21303926). Required to modulate the compacted morphology of the Golgi (PubMed:26209634). Regulates the level of CASR present at the cell membrane (PubMed:20861236). Plays a role in cell adhesion and cell migration, via its role in protein trafficking (PubMed:20639577). Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria (PubMed:22939626). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport (By similarity). {ECO:0000250|UniProtKB:P62821, ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236, ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:26209634}. |
P62877 | RBX1 | T9 | ochoa | E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)] | E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:10230407, PubMed:10579999, PubMed:11961546, PubMed:15983046, PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:22748924, PubMed:23455478, PubMed:27565346, PubMed:29769719, PubMed:32355176, PubMed:33417871, PubMed:38326650, PubMed:39504960, PubMed:39667934, PubMed:38316879). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (PubMed:27565346). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex mediates ubiquitination of Pol II subunit POLR2A at 'Lys-1268', a critical TC-NER checkpoint (PubMed:32355176, PubMed:34526721). Core component of the Cul7-RING(FBXW8) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35982156). Core component of a Cul9-RING ubiquitin ligase complex composed of CUL9 and RBX1, which mediates mono-ubiquitination of p53/TP53 (PubMed:38605244). Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:11027288, ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:29769719, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:33417871, ECO:0000269|PubMed:34526721, ECO:0000269|PubMed:35982156, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:38326650, ECO:0000269|PubMed:38605244, ECO:0000269|PubMed:39504960, ECO:0000269|PubMed:39667934}. |
P62888 | RPL30 | S10 | ochoa | Large ribosomal subunit protein eL30 (60S ribosomal protein L30) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
P62942 | FKBP1A | S9 | ochoa | Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase) | Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173, ECO:0000269|PubMed:9233797}. |
P62979 | RPS27A | T9 | ochoa | Ubiquitin-ribosomal protein eS31 fusion protein (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127, ECO:0000303|PubMed:19754430}.; FUNCTION: [Small ribosomal subunit protein eS31]: Component of the 40S subunit of the ribosome (PubMed:23636399, PubMed:9582194). 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:23636399, PubMed:34516797). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797, ECO:0000305|PubMed:9582194}. |
P62987 | UBA52 | T9 | ochoa | Ubiquitin-ribosomal protein eL40 fusion protein (CEP52) (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40 (60S ribosomal protein L40) (rpL40)] | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127, ECO:0000303|PubMed:19754430}.; FUNCTION: [Large ribosomal subunit protein eL40]: Component of the 60S subunit of the ribosome (PubMed:23169626, PubMed:23636399, PubMed:32669547, PubMed:39048817, PubMed:39103523). Ribosomal protein L40 is essential for translation of a subset of cellular transcripts, and especially for cap-dependent translation of vesicular stomatitis virus mRNAs (PubMed:23169626, PubMed:23636399, PubMed:32669547, PubMed:39048817, PubMed:39103523). {ECO:0000269|PubMed:23169626, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000269|PubMed:39048817, ECO:0000269|PubMed:39103523}. |
P62995 | TRA2B | Y9 | ochoa | Transformer-2 protein homolog beta (TRA-2 beta) (TRA2-beta) (hTRA2-beta) (Splicing factor, arginine/serine-rich 10) (Transformer-2 protein homolog B) | Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:9546399}. |
P63010 | AP2B1 | T8 | ochoa | AP-2 complex subunit beta (AP105B) (Adaptor protein complex AP-2 subunit beta) (Adaptor-related protein complex 2 subunit beta) (Beta-2-adaptin) (Beta-adaptin) (Clathrin assembly protein complex 2 beta large chain) (Plasma membrane adaptor HA2/AP2 adaptin beta subunit) | Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}. |
P63165 | SUMO1 | S9 | ochoa | Small ubiquitin-related modifier 1 (SUMO-1) (GAP-modifying protein 1) (GMP1) (SMT3 homolog 3) (Sentrin) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (Ubiquitin-like protein UBL1) | Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}. |
P63241 | EIF5A | T9 | ochoa | Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (eIF-5A1) (Eukaryotic initiation factor 5A isoform 1) (eIF-5A) (Rev-binding factor) (eIF-4D) | Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:33547280). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (PubMed:16987817). With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis (PubMed:15371445). Also regulates TNF-alpha-mediated apoptosis (PubMed:15452064, PubMed:17187778). Mediates effects of polyamines on neuronal process extension and survival (PubMed:17360499). Is required for autophagy by assisting the ribosome in translating the ATG3 protein at a specific amino acid sequence, the 'ASP-ASP-Gly' motif, leading to the increase of the efficiency of ATG3 translation and facilitation of LC3B lipidation and autophagosome formation (PubMed:29712776). {ECO:0000250|UniProtKB:P23301, ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064, ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:17360499, ECO:0000269|PubMed:29712776, ECO:0000269|PubMed:33547280}.; FUNCTION: (Microbial infection) Cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. {ECO:0000269|PubMed:8253832}. |
P63252 | KCNJ2 | S10 | ochoa | Inward rectifier potassium channel 2 (Cardiac inward rectifier potassium channel) (Inward rectifier K(+) channel Kir2.1) (IRK-1) (hIRK1) (Potassium channel, inwardly rectifying subfamily J member 2) | Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it (PubMed:36149965, PubMed:7590287, PubMed:9490857). Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages (PubMed:7590287, PubMed:7696590). The inward rectification is mainly due to the blockage of outward current by internal magnesium (PubMed:9490857). Can be blocked by extracellular barium or cesium (PubMed:7590287, PubMed:7696590). Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues (PubMed:7590287, PubMed:7696590, PubMed:7840300). {ECO:0000269|PubMed:11371347, ECO:0000269|PubMed:15761194, ECO:0000269|PubMed:15922306, ECO:0000269|PubMed:16571646, ECO:0000269|PubMed:17324964, ECO:0000269|PubMed:36149965, ECO:0000269|PubMed:7590287, ECO:0000269|PubMed:7696590, ECO:0000269|PubMed:7840300, ECO:0000269|PubMed:8821791, ECO:0000269|PubMed:9490857, ECO:0000269|PubMed:9533862}. |
P68871 | HBB | S10 | ochoa | Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: LVV-hemorphin-7; Spinorphin] | Involved in oxygen transport from the lung to the various peripheral tissues. {ECO:0000269|PubMed:28066926}.; FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.; FUNCTION: [Spinorphin]: Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation. |
P78347 | GTF2I | T8 | ochoa | General transcription factor II-I (GTFII-I) (TFII-I) (Bruton tyrosine kinase-associated protein 135) (BAP-135) (BTK-associated protein 135) (SRF-Phox1-interacting protein) (SPIN) (Williams-Beuren syndrome chromosomal region 6 protein) | Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}. |
P78358 | CTAG1A | T8 | ochoa | Cancer/testis antigen 1 (Autoimmunogenic cancer/testis antigen NY-ESO-1) (Cancer/testis antigen 6.1) (CT6.1) (L antigen family member 2) (LAGE-2) | None |
P78362 | SRPK2 | S8 | ochoa | SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal] | Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:18559500, PubMed:21056976, PubMed:9472028). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (PubMed:21205200). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018). Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles (PubMed:16122776). {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21205200, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. |
P78362 | SRPK2 | S9 | ochoa | SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal] | Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:18559500, PubMed:21056976, PubMed:9472028). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (PubMed:21205200). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018). Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles (PubMed:16122776). {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21205200, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. |
P78362 | SRPK2 | S10 | ochoa | SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal] | Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:18559500, PubMed:21056976, PubMed:9472028). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (PubMed:21205200). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018). Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles (PubMed:16122776). {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21205200, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. |
P78417 | GSTO1 | S8 | ochoa | Glutathione S-transferase omega-1 (GSTO-1) (EC 2.5.1.18) (Glutathione S-transferase omega 1-1) (GSTO 1-1) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (S-(Phenacyl)glutathione reductase) (SPG-R) | Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Also has glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529}. |
P78508 | KCNJ10 | Y8 | psp | ATP-sensitive inward rectifier potassium channel 10 (ATP-dependent inwardly rectifying potassium channel Kir4.1) (Inward rectifier K(+) channel Kir1.2) (Potassium channel, inwardly rectifying subfamily J member 10) | May be responsible for potassium buffering action of glial cells in the brain (By similarity). Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it (PubMed:8995301). Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages (PubMed:8995301). The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (PubMed:8995301). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (PubMed:24561201). {ECO:0000250|UniProtKB:P49655, ECO:0000269|PubMed:8995301, ECO:0000305|PubMed:24561201}. |
P78508 | KCNJ10 | Y9 | psp | ATP-sensitive inward rectifier potassium channel 10 (ATP-dependent inwardly rectifying potassium channel Kir4.1) (Inward rectifier K(+) channel Kir1.2) (Potassium channel, inwardly rectifying subfamily J member 10) | May be responsible for potassium buffering action of glial cells in the brain (By similarity). Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it (PubMed:8995301). Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages (PubMed:8995301). The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (PubMed:8995301). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (PubMed:24561201). {ECO:0000250|UniProtKB:P49655, ECO:0000269|PubMed:8995301, ECO:0000305|PubMed:24561201}. |
P78563 | ADARB1 | S10 | ochoa | Double-stranded RNA-specific editase 1 (EC 3.5.4.37) (RNA-editing deaminase 1) (RNA-editing enzyme 1) (dsRNA adenosine deaminase) | Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis. {ECO:0000269|PubMed:18178553, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159}.; FUNCTION: [Isoform 1]: Has a lower catalytic activity than isoform 2. {ECO:0000269|PubMed:9149227}.; FUNCTION: [Isoform 2]: Has a higher catalytic activity than isoform 1. {ECO:0000269|PubMed:9149227}. |
P80297 | MT1X | S8 | ochoa | Metallothionein-1X (MT-1X) (Metallothionein-IX) (MT-IX) | Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. May be involved in FAM168A anti-apoptotic signaling (PubMed:23251525). {ECO:0000269|PubMed:23251525}. |
P83369 | LSM11 | S10 | ochoa | U7 snRNA-associated Sm-like protein LSm11 | Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing (PubMed:11574479, PubMed:16914750, PubMed:33230297). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed (PubMed:11574479, PubMed:16914750). Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to the Sm-binding site of U7 snRNA (PubMed:11574479, PubMed:16914750). {ECO:0000250|UniProtKB:Q8BUV6, ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:16914750, ECO:0000269|PubMed:33230297}. |
P83731 | RPL24 | S9 | ochoa | Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (60S ribosomal protein L30) | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. |
P84022 | SMAD3 | T8 | ochoa|psp | Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3) | Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:15588252, ECO:0000269|PubMed:16156666, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19218245, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9732876, ECO:0000269|PubMed:9892009}. |
P86790 | CCZ1B | S10 | ochoa | Vacuolar fusion protein CCZ1 homolog B (Vacuolar fusion protein CCZ1 homolog-like) | None |
P86791 | CCZ1 | S10 | ochoa | Vacuolar fusion protein CCZ1 homolog | Acts in concert with MON1A, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form (PubMed:23084991). {ECO:0000269|PubMed:23084991}. |
Q00341 | HDLBP | T8 | 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. |
Q00537 | CDK17 | S9 | ochoa | Cyclin-dependent kinase 17 (EC 2.7.11.22) (Cell division protein kinase 17) (PCTAIRE-motif protein kinase 2) (Serine/threonine-protein kinase PCTAIRE-2) | May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). {ECO:0000250}. |
Q01167 | FOXK2 | S9 | ochoa | Forkhead box protein K2 (G/T-mismatch specific binding protein) (nGTBP) (Interleukin enhancer-binding factor 1) | Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (PubMed:22083952, PubMed:25451922). Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity). Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity). Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity). Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription (PubMed:22083952). Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence (PubMed:20097901). Binds to NFAT-like motifs (purine-rich) in the IL2 promoter (PubMed:1339390). Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus (PubMed:25805136). Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements (PubMed:1909027). Accessory component of the polycomb repressive deubiquitinase (PR-DUB) complex; recruits the PR-DUB complex to specific FOXK2-bound genes (PubMed:24634419, PubMed:30664650). {ECO:0000250|UniProtKB:Q3UCQ1, ECO:0000269|PubMed:1339390, ECO:0000269|PubMed:1909027, ECO:0000269|PubMed:20097901, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24634419, ECO:0000269|PubMed:25451922, ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:30664650}. |
Q01628 | IFITM3 | S10 | ochoa | Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Interferon-inducible protein 1-8U) | IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed:33270927). {ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:33270927}. |
Q01629 | IFITM2 | S9 | ochoa | Interferon-induced transmembrane protein 2 (Dispanin subfamily A member 2c) (DSPA2c) (Interferon-inducible protein 1-8D) | IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol (PubMed:26354436, PubMed:33563656). Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927, PubMed:33563656). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33563656). Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). {ECO:0000269|PubMed:19544527, ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:33270927, ECO:0000269|PubMed:33563656}. |
Q02790 | FKBP4 | T9 | ochoa | Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (51 kDa FK506-binding protein) (FKBP51) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed] | Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Also acts as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. {ECO:0000269|PubMed:1279700, ECO:0000269|PubMed:1376003, ECO:0000269|PubMed:19945390, ECO:0000269|PubMed:21730050, ECO:0000269|PubMed:2378870}. |
Q03135 | CAV1 | S9 | ochoa | Caveolin-1 | May act as a scaffolding protein within caveolar membranes (PubMed:11751885). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19262564). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (PubMed:25893292). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity). {ECO:0000250|UniProtKB:P49817, ECO:0000269|PubMed:11751885, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:25893292}. |
Q03468 | ERCC6 | S9 | ochoa | DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB) | Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes (PubMed:16246722, PubMed:20541997, PubMed:22483866, PubMed:26620705, PubMed:32355176, PubMed:34526721, PubMed:38316879, PubMed:38600235, PubMed:38600236). Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment (PubMed:32355176, PubMed:34526721, PubMed:38600235, PubMed:38600236). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (PubMed:15548521). Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (PubMed:16246722, PubMed:9565609). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (PubMed:25820262). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (PubMed:25820262). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing premature entry of cells into mitosis following the induction of DNA DSBs (PubMed:25820262). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (PubMed:29203878). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (PubMed:28292928). Also involved in UV-induced translocation of ERCC8 to the nuclear matrix (PubMed:26620705). Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (PubMed:24874740). {ECO:0000269|PubMed:15548521, ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:20541997, ECO:0000269|PubMed:22483866, ECO:0000269|PubMed:24874740, ECO:0000269|PubMed:25820262, ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:28292928, ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:34526721, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:38600235, ECO:0000269|PubMed:38600236, ECO:0000269|PubMed:9565609}. |
Q03468 | ERCC6 | S10 | ochoa|psp | DNA excision repair protein ERCC-6 (EC 3.6.4.-) (ATP-dependent helicase ERCC6) (Cockayne syndrome protein CSB) | Essential factor involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes (PubMed:16246722, PubMed:20541997, PubMed:22483866, PubMed:26620705, PubMed:32355176, PubMed:34526721, PubMed:38316879, PubMed:38600235, PubMed:38600236). Plays a central role in the initiation of the TC-NER process: specifically recognizes and binds RNA polymerase II stalled at a lesion, and mediates recruitment of ERCC8/CSA, initiating DNA damage excision by TFIIH recruitment (PubMed:32355176, PubMed:34526721, PubMed:38600235, PubMed:38600236). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (PubMed:15548521). Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (PubMed:16246722, PubMed:9565609). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (PubMed:25820262). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (PubMed:25820262). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing premature entry of cells into mitosis following the induction of DNA DSBs (PubMed:25820262). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (PubMed:29203878). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (PubMed:28292928). Also involved in UV-induced translocation of ERCC8 to the nuclear matrix (PubMed:26620705). Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (PubMed:24874740). {ECO:0000269|PubMed:15548521, ECO:0000269|PubMed:16246722, ECO:0000269|PubMed:20541997, ECO:0000269|PubMed:22483866, ECO:0000269|PubMed:24874740, ECO:0000269|PubMed:25820262, ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:28292928, ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:34526721, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:38600235, ECO:0000269|PubMed:38600236, ECO:0000269|PubMed:9565609}. |
Q03721 | KCNC4 | S8 | psp | Voltage-gated potassium channel KCNC4 (KSHIIIC) (Potassium voltage-gated channel subfamily C member 4) (Voltage-gated potassium channel subunit Kv3.4) | Voltage-gated potassium channel that opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient (PubMed:7993631). The channel displays rapid activation and inactivation kinetics (PubMed:7993631). {ECO:0000269|PubMed:7993631}. |
Q03721 | KCNC4 | S9 | psp | Voltage-gated potassium channel KCNC4 (KSHIIIC) (Potassium voltage-gated channel subfamily C member 4) (Voltage-gated potassium channel subunit Kv3.4) | Voltage-gated potassium channel that opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical gradient (PubMed:7993631). The channel displays rapid activation and inactivation kinetics (PubMed:7993631). {ECO:0000269|PubMed:7993631}. |
Q04609 | FOLH1 | T8 | ochoa | Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Cell growth-inhibiting gene 27 protein) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen) (PSM) (PSMA) (Pteroylpoly-gamma-glutamate carboxypeptidase) | Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. |
Q04609 | FOLH1 | S10 | ochoa | Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Cell growth-inhibiting gene 27 protein) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen) (PSM) (PSMA) (Pteroylpoly-gamma-glutamate carboxypeptidase) | Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. |
Q04941 | PLP2 | S8 | ochoa | Proteolipid protein 2 (Differentiation-dependent protein A4) (Intestinal membrane A4 protein) | May play a role in cell differentiation in the intestinal epithelium. |
Q05329 | GAD2 | S10 | psp | Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform) | Catalyzes the production of GABA. {ECO:0000305|PubMed:8999827}. |
Q05D32 | CTDSPL2 | S9 | ochoa | CTD small phosphatase-like protein 2 (CTDSP-like 2) (EC 3.1.3.-) | Probable phosphatase. {ECO:0000250}. |
Q08117 | TLE5 | S9 | ochoa | TLE family member 5 (Amino-terminal enhancer of split) (Amino enhancer of split) (Gp130-associated protein GAM) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG) (TLE family member 5, transcriptional modulator) | Transcriptional corepressor. Acts as a dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development. {ECO:0000269|PubMed:10660609, ECO:0000269|PubMed:10748198}. |
Q10589 | BST2 | Y8 | ochoa | Bone marrow stromal antigen 2 (BST-2) (HM1.24 antigen) (Tetherin) (CD antigen CD317) | IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted (PubMed:18200009, PubMed:18342597, PubMed:19036818, PubMed:19879838, PubMed:20019814, PubMed:20399176, PubMed:20419159, PubMed:20940320, PubMed:21529378, PubMed:22520941, PubMed:37922253). Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, paramyxoviridae: nipah virus, and coronaviridae: SARS-CoV (PubMed:18200009, PubMed:18342597, PubMed:19179289, PubMed:19879838, PubMed:20399176, PubMed:20419159, PubMed:20686043, PubMed:20943977, PubMed:21529378, PubMed:21621240, PubMed:22520941, PubMed:26378163, PubMed:31199522). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration (PubMed:22065321). Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (PubMed:19564354, PubMed:26172439). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities (PubMed:23028328, PubMed:26172439). Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu (PubMed:23028328, PubMed:26172439). Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2 (PubMed:23028328). {ECO:0000269|PubMed:18200009, ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19036818, ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21529378, ECO:0000269|PubMed:21621240, ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:22520941, ECO:0000269|PubMed:23028328, ECO:0000269|PubMed:26172439, ECO:0000269|PubMed:26378163, ECO:0000269|PubMed:31199522, ECO:0000269|PubMed:37922253}. |
Q12797 | ASPH | S9 | ochoa | Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) | [Isoform 1]: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269|PubMed:11773073}.; FUNCTION: [Isoform 8]: Membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269|PubMed:22586105}. |
Q12797 | ASPH | S10 | ochoa | Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) | [Isoform 1]: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269|PubMed:11773073}.; FUNCTION: [Isoform 8]: Membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269|PubMed:22586105}. |
Q12891 | HYAL2 | T8 | ochoa | Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2) (Lung carcinoma protein 2) (LuCa-2) | Catalyzes hyaluronan degradation into small fragments that are endocytosed and degraded in lysosomes by HYAL1 and exoglycosidases (PubMed:9712871). Essential for the breakdown of extracellular matrix hyaluronan (PubMed:28081210). {ECO:0000269|PubMed:28081210, ECO:0000269|PubMed:9712871}. |
Q12948 | FOXC1 | S8 | ochoa | Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3) | DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development (PubMed:11782474, PubMed:14506133, PubMed:14578375, PubMed:15277473, PubMed:15299087, PubMed:15684392, PubMed:16449236, PubMed:16492674, PubMed:17210863, PubMed:19279310, PubMed:19793056, PubMed:25786029, PubMed:27804176, PubMed:27907090). Acts either as a transcriptional activator or repressor (PubMed:11782474). Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes (PubMed:11782474, PubMed:12533514, PubMed:14506133, PubMed:19793056, PubMed:27804176, PubMed:7957066). Upon DNA-binding, promotes DNA bending (PubMed:14506133, PubMed:7957066). Acts as a transcriptional coactivator (PubMed:26565916). Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification (By similarity). Also acts as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells (PubMed:26565916). Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye (PubMed:17993506). Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity (By similarity). Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals (PubMed:12408963). Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion (PubMed:20406990, PubMed:22991501). Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation (PubMed:27907090). Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). May function as a tumor suppressor (PubMed:12408963). {ECO:0000250|UniProtKB:Q61572, ECO:0000269|PubMed:11782474, ECO:0000269|PubMed:12408963, ECO:0000269|PubMed:12533514, ECO:0000269|PubMed:14506133, ECO:0000269|PubMed:14578375, ECO:0000269|PubMed:15277473, ECO:0000269|PubMed:15299087, ECO:0000269|PubMed:15684392, ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:16492674, ECO:0000269|PubMed:17210863, ECO:0000269|PubMed:17993506, ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:19793056, ECO:0000269|PubMed:20406990, ECO:0000269|PubMed:22991501, ECO:0000269|PubMed:25786029, ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:27804176, ECO:0000269|PubMed:27907090, ECO:0000269|PubMed:7957066}. |
Q12948 | FOXC1 | S9 | ochoa | Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3) | DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development (PubMed:11782474, PubMed:14506133, PubMed:14578375, PubMed:15277473, PubMed:15299087, PubMed:15684392, PubMed:16449236, PubMed:16492674, PubMed:17210863, PubMed:19279310, PubMed:19793056, PubMed:25786029, PubMed:27804176, PubMed:27907090). Acts either as a transcriptional activator or repressor (PubMed:11782474). Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes (PubMed:11782474, PubMed:12533514, PubMed:14506133, PubMed:19793056, PubMed:27804176, PubMed:7957066). Upon DNA-binding, promotes DNA bending (PubMed:14506133, PubMed:7957066). Acts as a transcriptional coactivator (PubMed:26565916). Stimulates Indian hedgehog (Ihh)-induced target gene expression mediated by the transcription factor GLI2, and hence regulates endochondral ossification (By similarity). Also acts as a transcriptional coregulator by increasing DNA-binding capacity of GLI2 in breast cancer cells (PubMed:26565916). Regulates FOXO1 through binding to a conserved element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1 as an important regulator of cell viability and resistance to oxidative stress in the eye (PubMed:17993506). Cooperates with transcription factor FOXC2 in regulating expression of genes that maintain podocyte integrity (By similarity). Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals (PubMed:12408963). Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion (PubMed:20406990, PubMed:22991501). Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). Plays a role in the gene regulatory network essential for epidermal keratinocyte terminal differentiation (PubMed:27907090). Essential developmental transcriptional factor required for mesoderm-derived tissues, such as the somites, skin, bone and cartilage. Positively regulates CXCL12 and stem cell factor expression in bone marrow mesenchymal progenitor cells, and hence plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner. Involved in chemokine CXCL12-induced endothelial cell migration through the control of CXCR4 expression (By similarity). May function as a tumor suppressor (PubMed:12408963). {ECO:0000250|UniProtKB:Q61572, ECO:0000269|PubMed:11782474, ECO:0000269|PubMed:12408963, ECO:0000269|PubMed:12533514, ECO:0000269|PubMed:14506133, ECO:0000269|PubMed:14578375, ECO:0000269|PubMed:15277473, ECO:0000269|PubMed:15299087, ECO:0000269|PubMed:15684392, ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:16492674, ECO:0000269|PubMed:17210863, ECO:0000269|PubMed:17993506, ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:19793056, ECO:0000269|PubMed:20406990, ECO:0000269|PubMed:22991501, ECO:0000269|PubMed:25786029, ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:27804176, ECO:0000269|PubMed:27907090, ECO:0000269|PubMed:7957066}. |
Q12965 | MYO1E | Y9 | ochoa | Unconventional myosin-Ie (Myosin-Ic) (Unconventional myosin 1E) | Actin-based motor molecule with ATPase activity (PubMed:11940582, PubMed:36316095). Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated vesicles (PubMed:36316095). Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. {ECO:0000269|PubMed:11940582, ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:20860408, ECO:0000269|PubMed:36316095}. |
Q13077 | TRAF1 | S8 | ochoa | TNF receptor-associated factor 1 (Epstein-Barr virus-induced protein 6) | Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2. {ECO:0000269|PubMed:10692572, ECO:0000269|PubMed:16323247, ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:19287455, ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093}. |
Q13114 | TRAF3 | S9 | ochoa | TNF receptor-associated factor 3 (EC 2.3.2.27) (CD40 receptor-associated factor 1) (CRAF1) (CD40-binding protein) (CD40BP) (LMP1-associated protein 1) (LAP1) (RING-type E3 ubiquitin transferase TRAF3) | Cytoplasmic E3 ubiquitin ligase that regulates various signaling pathways, such as the NF-kappa-B, mitogen-activated protein kinase (MAPK) and interferon regulatory factor (IRF) pathways, and thus controls a lot of biological processes in both immune and non-immune cell types (PubMed:33148796, PubMed:33608556). In TLR and RLR signaling pathways, acts as an E3 ubiquitin ligase promoting the synthesis of 'Lys-63'-linked polyubiquitin chains on several substrates such as ASC that lead to the activation of the type I interferon response or the inflammasome (PubMed:25847972, PubMed:27980081). Following the activation of certain TLRs such as TLR4, acts as a negative NF-kappa-B regulator, possibly to avoid unregulated inflammatory response, and its degradation via 'Lys-48'-linked polyubiquitination is required for MAPK activation and production of inflammatory cytokines. Alternatively, when TLR4 orchestrates bacterial expulsion, TRAF3 undergoes 'Lys-33'-linked polyubiquitination and subsequently binds to RALGDS, mobilizing the exocyst complex to rapidly expel intracellular bacteria back for clearance (PubMed:27438768). Also acts as a constitutive negative regulator of the alternative NF-kappa-B pathway, which controls B-cell survival and lymphoid organ development. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14. {ECO:0000269|PubMed:15084608, ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20097753, ECO:0000269|PubMed:20185819, ECO:0000269|PubMed:25847972, ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:32562145, ECO:0000269|PubMed:33148796, ECO:0000269|PubMed:33608556, ECO:0000269|PubMed:34011520}. |
Q13123 | IK | S10 | ochoa | Protein Red (Cytokine IK) (IK factor) (Protein RER) | Involved in pre-mRNA splicing as a component of the spliceosome (PubMed:28781166). Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable). Required for normal mitotic cell cycle progression (PubMed:22351768, PubMed:24252166). Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint (PubMed:22351768). Required for normal accumulation of SMU1 (PubMed:24945353). {ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:24252166, ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166, ECO:0000305}.; FUNCTION: (Microbial infection) Required, together with SMU1, for normal splicing of influenza A virus NS1 pre-mRNA, which is required for the production of the exportin NS2 and for the production of influenza A virus particles. Not required for the production of VSV virus particles. {ECO:0000269|PubMed:24945353}. |
Q13190 | STX5 | S9 | ochoa | Syntaxin-5 | Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. {ECO:0000250|UniProtKB:Q08851}.; FUNCTION: [Isoform 2]: Required for Golgi to endoplasmic reticulum retrogade transport, and for intra-Golgi transport. {ECO:0000269|PubMed:34711829}.; FUNCTION: (Microbial infection) Required for the efficient production of infectious virion during human cytomegalovirus infection. Mechanistically, participates in the formation of the cytoplasmic viral assembly compartment where tegument acquisition and envelopment occur. {ECO:0000269|PubMed:27795424}. |
Q13206 | DDX10 | S10 | ochoa | Probable ATP-dependent RNA helicase DDX10 (EC 3.6.4.13) (DEAD box protein 10) | Putative ATP-dependent RNA helicase that plays various role in innate immunity or inflammation. Plays a role in the enhancement of AIM2-induced inflammasome activation by interacting with AIM2 and stabilizing its protein level (PubMed:32519665). Negatively regulates viral infection by promoting interferon beta production and interferon stimulated genes/ISGs expression (PubMed:36779599). {ECO:0000269|PubMed:32519665, ECO:0000269|PubMed:36779599}. |
Q13263 | TRIM28 | S9 | ochoa | Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28) | Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). {ECO:0000250|UniProtKB:Q62318, ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11959841, ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:16107876, ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17079232, ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18060868, ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:20424263, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23543754, ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:27029610, ECO:0000269|PubMed:8769649, ECO:0000269|PubMed:9016654}.; FUNCTION: (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1. {ECO:0000269|PubMed:24741090}. |
Q13303 | KCNAB2 | S9 | ochoa|psp | Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (hKvbeta2) | Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits (PubMed:11825900, PubMed:7649300). The beta-2/KCNAB2 cytoplasmic subunit promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:11825900, PubMed:7649300). Promotes the inactivation of Kv1.4/KCNA4 and Kv1.5/KCNA5 alpha subunit-containing channels (PubMed:11825900, PubMed:7649300). Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH-dependent reduction of a wide range of aldehyde and ketone substrates (By similarity). Substrate specificity includes methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro, no physiological substrate identified yet) (By similarity). The binding of oxidized and reduced nucleotide alters Kv channel gating and may contribute to dynamic fine tuning of cell excitability (By similarity). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). {ECO:0000250|UniProtKB:P62482, ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:7649300}. |
Q13319 | CDK5R2 | S8 | psp | Cyclin-dependent kinase 5 activator 2 (CDK5 activator 2) (Cyclin-dependent kinase 5 regulatory subunit 2) (p39) (p39I) | Activator of CDK5/TPKII. |
Q13322 | GRB10 | S9 | ochoa | Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Insulin receptor-binding protein Grb-IR) | Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin-stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2. {ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:15060076, ECO:0000269|PubMed:16434550, ECO:0000269|PubMed:17376403}. |
Q13439 | GOLGA4 | S10 | 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}. |
Q13485 | SMAD4 | T9 | ochoa|psp | Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4) | In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling (PubMed:25514493). Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:9389648}. |
Q13496 | MTM1 | Y9 | ochoa | Myotubularin (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) | Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (PubMed:10900271, PubMed:11001925, PubMed:12646134, PubMed:14722070). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides (PubMed:9537414). Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome (PubMed:14722070). Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture (PubMed:21135508). Plays a role in mitochondrial morphology and positioning (PubMed:21135508). Required for skeletal muscle maintenance but not for myogenesis (PubMed:21135508). In skeletal muscles, stabilizes MTMR12 protein levels (PubMed:23818870). {ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925, ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:14722070, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:23818870, ECO:0000269|PubMed:9537414}. |
Q13505 | MTX1 | S9 | ochoa | Metaxin-1 (Mitochondrial outer membrane import complex protein 1) | Involved in transport of proteins into the mitochondrion. Essential for embryonic development (By similarity). {ECO:0000250}. |
Q13523 | PRP4K | S8 | 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}. |
Q13541 | EIF4EBP1 | S8 | ochoa|psp | Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) | Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:7935836}. |
Q13614 | MTMR2 | S9 | ochoa | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 (EC 3.1.3.95) (Myotubularin-related protein 2) (Phosphatidylinositol-3-phosphate phosphatase) | 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:11733541, PubMed:12668758, PubMed:14690594, PubMed:21372139). Regulates the level of these phosphoinositides critical for various biological processes including autophagy initiation and autophagosome maturation (PubMed:35580604). {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:14690594, ECO:0000269|PubMed:21372139, ECO:0000269|PubMed:35580604}. |
Q13615 | MTMR3 | S8 | 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}. |
Q13619 | CUL4A | S10 | ochoa | Cullin-4A (CUL-4A) | Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620, PubMed:30166453, PubMed:33854232, PubMed:33854239). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). DCX(DET1-COP1) directs ubiquitination of JUN (PubMed:14739464). DCX(DDB2) directs ubiquitination of XPC (PubMed:15811626). DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition (PubMed:16678110, PubMed:17041588, PubMed:24209620). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of p53/TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:14578910, PubMed:15448697, PubMed:15548678). DCX(DTL) directs autoubiquitination of DTL (PubMed:23478445). In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip (PubMed:16537899). Is involved in ubiquitination of HOXA9 (PubMed:14609952). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). The DCX(ERCC8) complex (also named CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). 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). With CUL4B, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:14609952, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15548678, ECO:0000269|PubMed:15811626, ECO:0000269|PubMed:16537899, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24209620, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:26711351, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}. |
Q13642 | FHL1 | Y9 | ochoa | Four and a half LIM domains protein 1 (FHL-1) (Skeletal muscle LIM-protein 1) (SLIM) (SLIM-1) | May have an involvement in muscle development or hypertrophy. |
Q14134 | TRIM29 | S9 | ochoa | Tripartite motif-containing protein 29 (Ataxia telangiectasia group D-associated protein) | Plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in the lysosome where it induces its 'Lys-48' ubiquitination and subsequent degradation. In turn, the expression of type I interferons and the production of pro-inflammatory cytokines are inhibited. Additionally, induces the 'Lys-48' ubiquitination of STING1 in a similar way, leading to its degradation. {ECO:0000269|PubMed:27695001, ECO:0000269|PubMed:29038422}. |
Q14151 | SAFB2 | S8 | ochoa | Scaffold attachment factor B2 (SAF-B2) | Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation. |
Q14161 | GIT2 | S8 | 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}. |
Q14194 | CRMP1 | S8 | ochoa | Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Inactive dihydropyrimidinase) (Unc-33-like phosphoprotein 3) (ULIP-3) | Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (PubMed:25358863). Plays a role in axon guidance (PubMed:25358863). During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone (PubMed:25358863). Involved in invasive growth and cell migration (PubMed:11562390). May participate in cytokinesis (PubMed:19799413). {ECO:0000269|PubMed:11562390, ECO:0000269|PubMed:19799413, ECO:0000269|PubMed:25358863}. |
Q14202 | ZMYM3 | S8 | ochoa | Zinc finger MYM-type protein 3 (Zinc finger protein 261) | Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}. |
Q14315 | FLNC | S8 | ochoa | Filamin-C (FLN-C) (FLNc) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin) | Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity). {ECO:0000250|UniProtKB:Q8VHX6, ECO:0000269|PubMed:34405687}. |
Q14469 | HES1 | S10 | ochoa | Transcription factor HES-1 (Class B basic helix-loop-helix protein 39) (bHLHb39) (Hairy and enhancer of split 1) (Hairy homolog) (Hairy-like protein) (hHL) | Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-CANNTG-3' with low affinity (By similarity). May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage. {ECO:0000250, ECO:0000269|PubMed:18550849}. |
Q14687 | GSE1 | S10 | ochoa | Genetic suppressor element 1 | None |
Q14694 | USP10 | Y8 | ochoa | Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10) | Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR (PubMed:11439350, PubMed:18632802, PubMed:31981475). Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53 (PubMed:20096447). Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response (PubMed:20096447). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes (PubMed:21962518). In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13 (PubMed:21962518). Does not deubiquitinate MDM2 (PubMed:20096447). Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits (PubMed:27022092, PubMed:31981475, PubMed:34348161, PubMed:34469731). Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid-liquid phase separation (LLPS) and assembly of stress granules (PubMed:11439350, PubMed:27022092, PubMed:32302570). Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome (PubMed:31981475, PubMed:34348161, PubMed:34469731). Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling (PubMed:34469731). Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling (PubMed:19398555). Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Deubiquitinates TBX21 leading to its stabilization (PubMed:24845384). Plays a negative role in the RLR signaling pathway upon RNA virus infection by blocking the RIGI-mediated MAVS activation. Mechanistically, removes the unanchored 'Lys-63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, essential for its activation (PubMed:37582970). {ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:24845384, ECO:0000269|PubMed:25861989, ECO:0000269|PubMed:27022092, ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:32302570, ECO:0000269|PubMed:34348161, ECO:0000269|PubMed:34469731, ECO:0000269|PubMed:37582970}. |
Q14749 | GNMT | T8 | psp | Glycine N-methyltransferase (EC 2.1.1.20) | Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. {ECO:0000269|PubMed:14651980, ECO:0000269|PubMed:14739680, ECO:0000269|PubMed:17660255, ECO:0000269|PubMed:8281755}. |
Q14749 | GNMT | S10 | psp | Glycine N-methyltransferase (EC 2.1.1.20) | Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. {ECO:0000269|PubMed:14651980, ECO:0000269|PubMed:14739680, ECO:0000269|PubMed:17660255, ECO:0000269|PubMed:8281755}. |
Q14790 | CASP8 | Y8 | psp | Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10] | Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099). {ECO:0000250|UniProtKB:O89110, ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:18216014, ECO:0000269|PubMed:23516580, ECO:0000269|PubMed:27109099, ECO:0000269|PubMed:31827280, ECO:0000269|PubMed:31827281, ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:34012073, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:8681376, ECO:0000269|PubMed:8681377, ECO:0000269|PubMed:8755496, ECO:0000269|PubMed:8962078, ECO:0000269|PubMed:9006941, ECO:0000269|PubMed:9184224}.; FUNCTION: [Isoform 5]: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. {ECO:0000305|PubMed:8681376}.; FUNCTION: [Isoform 6]: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. {ECO:0000305|PubMed:8681376}.; FUNCTION: [Isoform 7]: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade (PubMed:12010809). {ECO:0000269|PubMed:12010809, ECO:0000305|PubMed:8681376}.; FUNCTION: [Isoform 8]: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. {ECO:0000305|PubMed:8681376}. |
Q15004 | PCLAF | S8 | ochoa | PCNA-associated factor (Hepatitis C virus NS5A-transactivated protein 9) (HCV NS5A-transactivated protein 9) (Overexpressed in anaplastic thyroid carcinoma 1) (OEATC-1) (PCNA-associated factor of 15 kDa) (PAF15) (p15PAF) (PCNA-clamp-associated factor) | PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork-blocking lesions. Also acts as a regulator of centrosome number. {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}. |
Q15020 | SART3 | S8 | ochoa | Spliceosome associated factor 3, U4/U6 recycling protein (Squamous cell carcinoma antigen recognized by T-cells 3) (SART-3) (Tat-interacting protein of 110 kDa) (Tip110) (p110 nuclear RNA-binding protein) | U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.; FUNCTION: Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication. {ECO:0000269|PubMed:11959860}. |
Q15020 | SART3 | S10 | ochoa | Spliceosome associated factor 3, U4/U6 recycling protein (Squamous cell carcinoma antigen recognized by T-cells 3) (SART-3) (Tat-interacting protein of 110 kDa) (Tip110) (p110 nuclear RNA-binding protein) | U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.; FUNCTION: Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication. {ECO:0000269|PubMed:11959860}. |
Q15042 | RAB3GAP1 | S9 | ochoa | Rab3 GTPase-activating protein catalytic subunit (RAB3 GTPase-activating protein 130 kDa subunit) (Rab3-GAP p130) (Rab3-GAP) | Catalytic subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18 (PubMed:10859313, PubMed:24891604, PubMed:9030515). As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (PubMed:10859313). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (PubMed:15696165). The Rab3GAP complex, acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604). Recruits and stabilizes RAB18 at the cis-Golgi membrane in fibroblasts where RAB18 is most likely activated (PubMed:26063829). Also involved in RAB18 recruitment at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604). Required for normal eye and brain development (PubMed:15696165, PubMed:23420520). May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (PubMed:9030515, PubMed:9852129). {ECO:0000269|PubMed:10859313, ECO:0000269|PubMed:15696165, ECO:0000269|PubMed:23420520, ECO:0000269|PubMed:24891604, ECO:0000269|PubMed:26063829, ECO:0000269|PubMed:9030515, ECO:0000269|PubMed:9852129}. |
Q15078 | CDK5R1 | S8 | psp | Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)] | p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:24235147}. |
Q15208 | STK38 | S10 | psp | Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) | Serine/threonine-protein kinase that acts as a negative regulator of MAP3K1/2 signaling (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 (PubMed:12493777, PubMed:15197186, PubMed:17906693, PubMed:7761441). Acts as an ufmylation 'reader' in a kinase-independent manner: specifically recognizes and binds mono-ufmylated histone H4 in response to DNA damage, promoting the recruitment of SUV39H1 to the double-strand breaks, resulting in ATM activation (PubMed:32537488). {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:32537488, ECO:0000269|PubMed:7761441}. |
Q15311 | RALBP1 | T9 | ochoa | RalA-binding protein 1 (RalBP1) (76 kDa Ral-interacting protein) (Dinitrophenyl S-glutathione ATPase) (DNP-SG ATPase) (EC 7.6.2.2, EC 7.6.2.3) (Ral-interacting protein 1) | Multifunctional protein that functions as a downstream effector of RALA and RALB (PubMed:7673236). As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity (PubMed:7673236). As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis (PubMed:10910768, PubMed:12775724). During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle (PubMed:12775724). During mitosis, also controls mitochondrial fission as an effector of RALA (PubMed:21822277). Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (PubMed:21822277). {ECO:0000269|PubMed:10910768, ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:7673236}.; FUNCTION: Could also function as a primary ATP-dependent active transporter for glutathione conjugates of electrophiles. May also actively catalyze the efflux of a wide range of substrates including xenobiotics like doxorubicin (DOX) contributing to cell multidrug resistance. {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11300797, ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:9548755}. |
Q15311 | RALBP1 | S10 | ochoa | RalA-binding protein 1 (RalBP1) (76 kDa Ral-interacting protein) (Dinitrophenyl S-glutathione ATPase) (DNP-SG ATPase) (EC 7.6.2.2, EC 7.6.2.3) (Ral-interacting protein 1) | Multifunctional protein that functions as a downstream effector of RALA and RALB (PubMed:7673236). As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity (PubMed:7673236). As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis (PubMed:10910768, PubMed:12775724). During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle (PubMed:12775724). During mitosis, also controls mitochondrial fission as an effector of RALA (PubMed:21822277). Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (PubMed:21822277). {ECO:0000269|PubMed:10910768, ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:7673236}.; FUNCTION: Could also function as a primary ATP-dependent active transporter for glutathione conjugates of electrophiles. May also actively catalyze the efflux of a wide range of substrates including xenobiotics like doxorubicin (DOX) contributing to cell multidrug resistance. {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11300797, ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:9548755}. |
Q15417 | CNN3 | S9 | ochoa | Calponin-3 (Calponin, acidic isoform) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
Q15464 | SHB | S10 | 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 | S9 | 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}. |
Q15637 | SF1 | T8 | ochoa | Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) | Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}. |
Q15691 | MAPRE1 | T8 | ochoa | Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27225956, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293, ECO:0000269|PubMed:36592928}. |
Q15691 | MAPRE1 | S9 | ochoa | Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1) | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation (PubMed:12388762, PubMed:34608293). Assists chromosome alignment in metaphase by recruiting the SKA complex to the spindle and stabilizing its interactions with microtubule bundles (K-fibers) (PubMed:27225956, PubMed:36592928). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). Functions downstream of Rho GTPases and DIAPH1 in stable microtubule formation (By similarity). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27225956, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293, ECO:0000269|PubMed:36592928}. |
Q15742 | NAB2 | T8 | ochoa | NGFI-A-binding protein 2 (EGR-1-binding protein 2) (Melanoma-associated delayed early response protein) (Protein MADER) | Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). {ECO:0000250}. |
Q15758 | SLC1A5 | S9 | ochoa | Neutral amino acid transporter B(0) (ATB(0)) (Baboon M7 virus receptor) (RD114/simian type D retrovirus receptor) (Sodium-dependent neutral amino acid transporter type 2) (Solute carrier family 1 member 5) | Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (PubMed:17094966, PubMed:23756778, PubMed:26492990, PubMed:29872227, PubMed:34741534, PubMed:8702519). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (PubMed:23756778, PubMed:24953180). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (PubMed:32733894). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (PubMed:17094966). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). {ECO:0000250|UniProtKB:D3ZJ25, ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:17094966, ECO:0000269|PubMed:23492904, ECO:0000269|PubMed:23756778, ECO:0000269|PubMed:24953180, ECO:0000269|PubMed:26492990, ECO:0000269|PubMed:29872227, ECO:0000269|PubMed:32733894, ECO:0000269|PubMed:34741534, ECO:0000269|PubMed:8702519}.; FUNCTION: (Microbial infection) Acts as a cell surface receptor for Feline endogenous virus RD114. {ECO:0000269|PubMed:10051606, ECO:0000269|PubMed:10196349}.; FUNCTION: (Microbial infection) Acts as a cell surface receptor for Baboon M7 endogenous virus. {ECO:0000269|PubMed:10196349}.; FUNCTION: (Microbial infection) Acts as a cell surface receptor for type D simian retroviruses. {ECO:0000269|PubMed:10196349}. |
Q15776 | ZKSCAN8 | S9 | ochoa | Zinc finger protein with KRAB and SCAN domains 8 (LD5-1) (Zinc finger protein 192) | May be involved in transcriptional regulation. |
Q15796 | SMAD2 | T8 | ochoa|psp | Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2) | Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209). {ECO:0000250|UniProtKB:Q62432, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:9892009}. |
Q15822 | CHRNA2 | S10 | ochoa | Neuronal acetylcholine receptor subunit alpha-2 (Nicotinic acetylcholine receptor subunit alpha-2) | Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators (PubMed:18723036). CHRNA2 forms heteropentameric neuronal acetylcholine receptors with CHRNB2 and CHRNB4 and plays a role in nicotine dependence (PubMed:24467848, PubMed:27493220). {ECO:0000269|PubMed:24467848, ECO:0000269|PubMed:27493220, ECO:0000303|PubMed:18723036}. |
Q15836 | VAMP3 | T9 | ochoa | Vesicle-associated membrane protein 3 (VAMP-3) (Cellubrevin) (CEB) (Synaptobrevin-3) | SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}. |
Q15907 | RAB11B | Y8 | ochoa | Ras-related protein Rab-11B (EC 3.6.5.2) (GTP-binding protein YPT3) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970, PubMed:26032412). The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). {ECO:0000269|PubMed:14627637, ECO:0000269|PubMed:19029296, ECO:0000269|PubMed:19244346, ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21248079, ECO:0000269|PubMed:22129970, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26032412, ECO:0000269|PubMed:31204173}. |
Q16186 | ADRM1 | S10 | ochoa | Proteasomal ubiquitin receptor ADRM1 (110 kDa cell membrane glycoprotein) (Gp110) (Adhesion-regulating molecule 1) (ARM-1) (Proteasome regulatory particle non-ATPase 13) (hRpn13) (Rpn13 homolog) | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Within the complex, functions as a proteasomal ubiquitin receptor (PubMed:18497817). Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702870, ECO:0000269|PubMed:25702872}. |
Q16625 | OCLN | S8 | ochoa | Occludin | May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. {ECO:0000269|PubMed:19114660}.; FUNCTION: (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes. {ECO:0000269|PubMed:19182773, ECO:0000269|PubMed:20375010}. |
Q16637 | SMN1 | S8 | ochoa|psp | Survival motor neuron protein (Component of gems 1) (Gemin-1) | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9845364). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (PubMed:17178713, PubMed:21816274, PubMed:22101937). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development (PubMed:23063131). Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:22101937, ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:26700805, ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9845364}. |
Q16667 | CDKN3 | T9 | ochoa | Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase) | May play a role in cell cycle regulation. Dual specificity CC phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues (PubMed:8127873, PubMed:8242750). Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (PubMed:7569954). {ECO:0000269|PubMed:7569954, ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}. |
Q16667 | CDKN3 | S10 | ochoa | Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase) | May play a role in cell cycle regulation. Dual specificity CC phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues (PubMed:8127873, PubMed:8242750). Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (PubMed:7569954). {ECO:0000269|PubMed:7569954, ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}. |
Q3YBR2 | TBRG1 | S9 | ochoa | Transforming growth factor beta regulator 1 (Nuclear interactor of ARF and Mdm2) | Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability. {ECO:0000269|PubMed:17110379}. |
Q3YBR2 | TBRG1 | S10 | ochoa | Transforming growth factor beta regulator 1 (Nuclear interactor of ARF and Mdm2) | Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability. {ECO:0000269|PubMed:17110379}. |
Q3ZCW2 | LGALSL | S8 | ochoa | Galectin-related protein (Galectin-like protein) (Lectin galactoside-binding-like protein) | Does not bind lactose, and may not bind carbohydrates. {ECO:0000269|PubMed:18320588, ECO:0000269|PubMed:18433051}. |
Q4VCS5 | AMOT | S9 | ochoa | Angiomotin | Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions. Repressor of YAP1 and WWTR1/TAZ transcription of target genes, potentially via regulation of Hippo signaling-mediated phosphorylation of YAP1 which results in its recruitment to tight junctions (PubMed:21205866). {ECO:0000269|PubMed:11257124, ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:21205866}. |
Q53QZ3 | ARHGAP15 | T9 | ochoa | Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15) | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction. {ECO:0000269|PubMed:12650940}. |
Q58FF6 | HSP90AB4P | Y9 | ochoa | Putative heat shock protein HSP 90-beta 4 | Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}. |
Q58FF6 | HSP90AB4P | S10 | ochoa | Putative heat shock protein HSP 90-beta 4 | Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. {ECO:0000250}. |
Q5BJD5 | TMEM41B | S10 | ochoa | Transmembrane protein 41B (Protein stasimon) | Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (PubMed:33850023, PubMed:33929485, PubMed:34015269). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (PubMed:33850023, PubMed:33929485, PubMed:34015269). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly (PubMed:30093494, PubMed:30126924, PubMed:30933966, PubMed:33850023, PubMed:33929485, PubMed:34015269, PubMed:34043740). In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (PubMed:33850023). Required for normal motor neuron development (By similarity). {ECO:0000250|UniProtKB:A1A5V7, ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30126924, ECO:0000269|PubMed:30933966, ECO:0000269|PubMed:33850023, ECO:0000269|PubMed:33929485, ECO:0000269|PubMed:34015269, ECO:0000269|PubMed:34043740}.; FUNCTION: (Microbial infection) Critical host factor required for infection by human coronaviruses SARS-CoV-2, HCoV-OC43, HCoV-NL63, and HCoV-229E, as well as all flaviviruses tested such as Zika virus and Yellow fever virus (PubMed:33338421, PubMed:33382968). Required post-entry of the virus to facilitate the ER membrane remodeling necessary to form replication organelles (PubMed:33382968). {ECO:0000269|PubMed:33338421, ECO:0000269|PubMed:33382968, ECO:0000269|PubMed:34043740}. |
Q5BKZ1 | ZNF326 | S10 | ochoa | DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs and DBC1) | Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. {ECO:0000269|PubMed:22446626}. |
Q5JSP0 | FGD3 | S8 | ochoa | FYVE, RhoGEF and PH domain-containing protein 3 (Zinc finger FYVE domain-containing protein 5) | Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}. |
Q5JSP0 | FGD3 | T9 | ochoa | FYVE, RhoGEF and PH domain-containing protein 3 (Zinc finger FYVE domain-containing protein 5) | Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity). {ECO:0000250}. |
Q5SYC1 | CLVS2 | S9 | ochoa | Clavesin-2 (Retinaldehyde-binding protein 1-like 2) (clathrin vesicle-associated Sec14 protein 2) | Required for normal morphology of late endosomes and/or lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). {ECO:0000250, ECO:0000269|PubMed:19651769}. |
Q5T0D9 | TPRG1L | S10 | ochoa | Tumor protein p63-regulated gene 1-like protein (Mossy fiber terminal-associated vertebrate-specific presynaptic protein) (Protein FAM79A) | Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release. {ECO:0000250|UniProtKB:A8WCF8}. |
Q5T0W9 | FAM83B | S8 | ochoa | Protein FAM83B | Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:23912460}. |
Q5T0W9 | FAM83B | S9 | ochoa | Protein FAM83B | Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades. {ECO:0000269|PubMed:22886302, ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:23912460}. |
Q5T4F4 | ZFYVE27 | S9 | ochoa | Protrudin (Spastic paraplegia 33 protein) (Zinc finger FYVE domain-containing protein 27) | Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (PubMed:17082457). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity (By similarity). Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner (PubMed:19289470). Contributes to both the formation and stabilization of the tubular ER network (PubMed:24668814). Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections (PubMed:23969831). Acts as an adapter protein and facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (PubMed:21976701). {ECO:0000250|UniProtKB:Q3TXX3, ECO:0000269|PubMed:17082457, ECO:0000269|PubMed:19289470, ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:23969831, ECO:0000269|PubMed:24668814}. |
Q5VTL8 | PRPF38B | T9 | ochoa | Pre-mRNA-splicing factor 38B (Sarcoma antigen NY-SAR-27) | May be required for pre-mRNA splicing. {ECO:0000305}. |
Q5VV41 | ARHGEF16 | S8 | ochoa | Rho guanine nucleotide exchange factor 16 (Ephexin-4) | Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:20679435}. |
Q5VV41 | ARHGEF16 | S9 | ochoa | Rho guanine nucleotide exchange factor 16 (Ephexin-4) | Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:20679435}. |
Q5XPI4 | RNF123 | S9 | ochoa | E3 ubiquitin-protein ligase RNF123 (EC 2.3.2.27) (Kip1 ubiquitination-promoting complex protein 1) (RING finger protein 123) | Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase (PubMed:15531880, PubMed:16227581, PubMed:25860612). Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin-dependent kinase inhibitor at the G0-G1 transition of the cell cycle (PubMed:15531880, PubMed:16227581). Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B: acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit (PubMed:25860612, PubMed:33168738, PubMed:34873064). Also functions as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity (PubMed:27312109). Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS (PubMed:27312109). {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:16227581, ECO:0000269|PubMed:25860612, ECO:0000269|PubMed:27312109, ECO:0000269|PubMed:33168738, ECO:0000269|PubMed:34873064}. |
Q684P5 | RAP1GAP2 | S9 | ochoa|psp | Rap1 GTPase-activating protein 2 (Rap1GAP2) (GTPase-activating Rap/Ran-GAP domain-like protein 4) | GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:15632203}. |
Q68CQ4 | UTP25 | S8 | ochoa | U3 small nucleolar RNA-associated protein 25 homolog (Digestive organ expansion factor homolog) (UTP25 small subunit processor component) | Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (PubMed:23357851, PubMed:25007945, PubMed:27657329). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329). {ECO:0000250|UniProtKB:Q6PEH4, ECO:0000269|PubMed:23357851, ECO:0000269|PubMed:25007945, ECO:0000269|PubMed:27657329}. |
Q68CQ4 | UTP25 | S10 | ochoa | U3 small nucleolar RNA-associated protein 25 homolog (Digestive organ expansion factor homolog) (UTP25 small subunit processor component) | Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (PubMed:23357851, PubMed:25007945, PubMed:27657329). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329). {ECO:0000250|UniProtKB:Q6PEH4, ECO:0000269|PubMed:23357851, ECO:0000269|PubMed:25007945, ECO:0000269|PubMed:27657329}. |
Q68DQ2 | CRYBG3 | S9 | 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 | S9 | ochoa | HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1) | Amplification-dependent oncogene. |
Q6DD87 | ZNF787 | S9 | ochoa | Zinc finger protein 787 (TTF-I-interacting peptide 20) | May be involved in transcriptional regulation. |
Q6IS14 | EIF5AL1 | T9 | ochoa | Eukaryotic translation initiation factor 5A-1-like (eIF-5A-1-like) (eIF-5A1-like) (Eukaryotic initiation factor 5A isoform 1-like) | Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity). {ECO:0000250|UniProtKB:P23301, ECO:0000250|UniProtKB:P63241}. |
Q6NUQ1 | RINT1 | S10 | ochoa | RAD50-interacting protein 1 (RAD50 interactor 1) (HsRINT-1) (RINT-1) | Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control (PubMed:11096100). Essential for telomere length control (PubMed:16600870). {ECO:0000269|PubMed:11096100, ECO:0000269|PubMed:16600870, ECO:0000305}. |
Q6NXE6 | ARMC6 | S10 | ochoa | Armadillo repeat-containing protein 6 | None |
Q6P0N0 | MIS18BP1 | S9 | ochoa | Mis18-binding protein 1 (Kinetochore-associated protein KNL-2 homolog) (HsKNL-2) (P243) | Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038, ECO:0000269|PubMed:17339379}. |
Q6P1L5 | FAM117B | S10 | ochoa | Protein FAM117B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein) | None |
Q6P597 | KLC3 | S10 | ochoa | Kinesin light chain 3 (KLC2-like) (kinesin light chain 2) | Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Plays a role during spermiogenesis in the development of the sperm tail midpiece and in the normal function of spermatozoa (By similarity). May play a role in the formation of the mitochondrial sheath formation in the developing spermatid midpiece (By similarity). {ECO:0000250|UniProtKB:Q91W40}. |
Q6PJF5 | RHBDF2 | S10 | ochoa | Inactive rhomboid protein 2 (iRhom2) (Rhomboid 5 homolog 2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 5) (Rhomboid veinlet-like protein 6) | Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. {ECO:0000250|UniProtKB:Q80WQ6}. |
Q6SZW1 | SARM1 | S8 | 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}. |
Q6T311 | ARL9 | S9 | ochoa | ADP-ribosylation factor-like protein 9 | None |
Q6UXN9 | WDR82 | S10 | ochoa | WD repeat-containing protein 82 | Regulatory component of the SET1/COMPASS complex implicated in the tethering of this complex to transcriptional start sites of active genes (PubMed:17998332, PubMed:18838538, PubMed:20516061). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332, PubMed:18838538). Component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation (PubMed:39603240, PubMed:39603239). PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). {ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240}. |
Q6ZMZ0 | RNF19B | S9 | ochoa | E3 ubiquitin-protein ligase RNF19B (EC 2.3.2.31) (IBR domain-containing protein 3) (Natural killer lytic-associated molecule) (RING finger protein 19B) | E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1 (PubMed:16709802, PubMed:27485036). Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells (PubMed:10438909). Protects against staurosporin-induced cell death (PubMed:27485036). {ECO:0000269|PubMed:10438909, ECO:0000269|PubMed:16709802, ECO:0000269|PubMed:27485036}. |
Q6ZRV2 | FAM83H | S8 | ochoa | Protein FAM83H | May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:23902688}. |
Q6ZRV2 | FAM83H | S9 | ochoa | Protein FAM83H | May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). {ECO:0000269|PubMed:18252228, ECO:0000269|PubMed:23902688}. |
Q6ZU35 | CRACD | S10 | ochoa | Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics) | Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin. {ECO:0000269|PubMed:30361697}. |
Q6ZW76 | ANKS3 | S9 | ochoa | Ankyrin repeat and SAM domain-containing protein 3 | May be involved in vasopressin signaling in the kidney. {ECO:0000250|UniProtKB:Q9CZK6}. |
Q6ZWE6 | PLEKHM3 | S10 | ochoa | Pleckstrin homology domain-containing family M member 3 (PH domain-containing family M member 3) (Differentiation associated protein) | Involved in skeletal muscle differentiation. May act as a scaffold protein for AKT1 during muscle differentiation. {ECO:0000250|UniProtKB:Q8BM47}. |
Q6ZWJ1 | STXBP4 | S10 | ochoa | Syntaxin-binding protein 4 (Syntaxin 4-interacting protein) (STX4-interacting protein) (Synip) | Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity). {ECO:0000250}. |
Q70Z53 | FRA10AC1 | S9 | ochoa | Protein FRA10AC1 | May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:34694367}. |
Q719H9 | KCTD1 | S9 | ochoa | BTB/POZ domain-containing protein KCTD1 (Potassium channel tetramerization domain-containing protein 1) | May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent. {ECO:0000269|PubMed:18358072, ECO:0000269|PubMed:19115315}. |
Q7KZF4 | SND1 | S10 | ochoa | Staphylococcal nuclease domain-containing protein 1 (EC 3.1.31.1) (100 kDa coactivator) (EBNA2 coactivator p100) (Tudor domain-containing protein 11) (p100 co-activator) | Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:18453631, PubMed:28546213). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity). {ECO:0000250|UniProtKB:Q78PY7, ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213, ECO:0000269|PubMed:9809063}.; FUNCTION: (Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269|PubMed:7651391}.; FUNCTION: (Microbial infection) Promotes SARS-CoV-2 RNA synthesis by binding to negative-sense RNA and the viral protein nsp9. {ECO:0000269|PubMed:37794589}. |
Q7L2H7 | EIF3M | S10 | ochoa | Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Fetal lung protein B5) (hFL-B5) (PCI domain-containing protein 1) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17403899, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17403899). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03012, ECO:0000269|PubMed:17403899, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). {ECO:0000269|PubMed:15919898}. |
Q7L7X3 | TAOK1 | S9 | ochoa | Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Kinase from chicken homolog B) (hKFC-B) (MARK Kinase) (MARKK) (Prostate-derived sterile 20-like kinase 2) (PSK-2) (PSK2) (Prostate-derived STE20-like kinase 2) (Thousand and one amino acid protein kinase 1) (TAOK1) (hTAOK1) | Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. Plays an essential role in the regulation of neuronal development in the central nervous system (PubMed:33565190). Also plays a role in the regulation of neuronal migration to the cortical plate (By similarity). {ECO:0000250|UniProtKB:Q5F2E8, ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16407310, ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:17900936, ECO:0000269|PubMed:33565190}. |
Q7L9L4 | MOB1B | S9 | ochoa | MOB kinase activator 1B (Mob1 homolog 1A) (Mob1A) (Mob1B) (Mps one binder kinase activator-like 1A) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 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. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L. {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}. |
Q7L9L4 | MOB1B | S10 | ochoa | MOB kinase activator 1B (Mob1 homolog 1A) (Mob1A) (Mob1B) (Mps one binder kinase activator-like 1A) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 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. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L. {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}. |
Q7LFL8 | CXXC5 | S8 | ochoa | CXXC-type zinc finger protein 5 (CF5) (Putative MAPK-activating protein PM08) (Putative NF-kappa-B-activating protein 102) (Retinoid-inducible nuclear factor) (RINF) | May indirectly participate in activation of the NF-kappa-B and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of canonical Wnt signaling activity in neural stem cells (By similarity). Required for DNA damage-induced ATM phosphorylation, p53 activation and cell cycle arrest. Involved in myelopoiesis. Transcription factor. Binds to the oxygen responsive element of COX4I2 and represses its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen) (PubMed:23303788). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ (PubMed:23303788). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (PubMed:29276034). {ECO:0000250|UniProtKB:Q5XIQ3, ECO:0000269|PubMed:19182210, ECO:0000269|PubMed:19557330, ECO:0000269|PubMed:23303788, ECO:0000269|PubMed:29276034}. |
Q7Z2W7 | TRPM8 | S9 | psp | Transient receptor potential cation channel subfamily M member 8 (Long transient receptor potential channel 6) (LTrpC-6) (LTrpC6) (Transient receptor potential p8) (Trp-p8) | Non-selective ion channel permeable to monovalent and divalent cations, including Na(+), K(+), and Ca(2+), with higher permeability for Ca(2+). Activated by multiple factors, such as temperature, voltage, pressure, and changes in osmolality. Activated by cool temperatures (<23-28 degrees Celsius) and by chemical ligands evoking a sensation of coolness, such as menthol and icilin therefore plays a central role in the detection of environmental cold temperatures (PubMed:15306801, PubMed:15852009, PubMed:16174775, PubMed:25559186, PubMed:37857704). TRPM8 is a voltage-dependent channel; its activation by cold or chemical ligands shifts its voltage thresholds towards physiological membrane potentials, leading to the opening of the channel (PubMed:15306801). In addition to its critical role in temperature sensing, regulates basal tear secretion by sensing evaporation-induced cooling and changes in osmolality (By similarity). May plays a role in prostate cancer cell migration (PubMed:16174775, PubMed:25559186). {ECO:0000250|UniProtKB:Q8R4D5, ECO:0000269|PubMed:15306801, ECO:0000269|PubMed:15852009, ECO:0000269|PubMed:16174775, ECO:0000269|PubMed:25559186, ECO:0000269|PubMed:37857704}.; FUNCTION: [Isoform 2]: Negatively regulates menthol- and cold-induced channel activity by stabilizing the closed state of the channel. {ECO:0000269|PubMed:22128173}.; FUNCTION: [Isoform 3]: Negatively regulates menthol- and cold-induced channel activity by stabilizing the closed state of the channel. {ECO:0000269|PubMed:22128173}. |
Q7Z2X7 | PAGE2 | S9 | ochoa | P antigen family member 2 (PAGE-2) (G antigen family C 2) (Prostate-associated gene 2 protein) | None |
Q7Z3C6 | ATG9A | Y8 | psp | Autophagy-related protein 9A (APG9-like 1) (mATG9) | Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:22456507, PubMed:27510922, PubMed:29437695, PubMed:32513819, PubMed:32610138, PubMed:33106659, PubMed:33468622, PubMed:33850023). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:16940348, PubMed:22456507, PubMed:33106659). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106659). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (PubMed:30917996). In addition to autophagy, also plays a role in necrotic cell death (By similarity). {ECO:0000250|UniProtKB:Q68FE2, ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:27510922, ECO:0000269|PubMed:29437695, ECO:0000269|PubMed:30917996, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0000269|PubMed:33468622, ECO:0000269|PubMed:33850023}. |
Q7Z434 | MAVS | Y9 | psp | Mitochondrial antiviral-signaling protein (MAVS) (CARD adapter inducing interferon beta) (Cardif) (Interferon beta promoter stimulator protein 1) (IPS-1) (Putative NF-kappa-B-activating protein 031N) (Virus-induced-signaling adapter) (VISA) | Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325). {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20451243, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:23087404, ECO:0000269|PubMed:23582325, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27736772, ECO:0000269|PubMed:27992402, ECO:0000269|PubMed:33110251, ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:37582970}. |
Q7Z4H3 | HDDC2 | S10 | ochoa | 5'-deoxynucleotidase HDDC2 (EC 3.1.3.89) (HD domain-containing protein 2) (Hepatitis C virus NS5A-transactivated protein 2) (HCV NS5A-transactivated protein 2) | Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP). {ECO:0000250|UniProtKB:P53144}. |
Q7Z4S6 | KIF21A | S8 | ochoa | Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62) | Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250|UniProtKB:Q9QXL2, ECO:0000269|PubMed:24120883}. |
Q7Z4S6 | KIF21A | S9 | ochoa | Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62) | Processive microtubule plus-end directed motor protein involved in neuronal axon guidance. Is recruited by KANK1 to cortical microtubule stabilizing complexes (CMSCs) at focal adhesions (FAs) rims where it promotes microtubule capture and stability. Controls microtubule polymerization rate at axonal growth cones and suppresses microtubule growth without inducing microtubule disassembly once it reaches the cell cortex. {ECO:0000250|UniProtKB:Q9QXL2, ECO:0000269|PubMed:24120883}. |
Q7Z5U6 | WDR53 | S10 | ochoa | WD repeat-containing protein 53 | None |
Q7Z614 | SNX20 | S9 | ochoa | Sorting nexin-20 (Selectin ligand-interactor cytoplasmic 1) (SLIC-1) | May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, or on SELPLG-mediated cell-cell adhesion. {ECO:0000305|PubMed:18196517}. |
Q7Z7L9 | ZSCAN2 | T10 | ochoa | Zinc finger and SCAN domain-containing protein 2 (Zinc finger protein 29 homolog) (Zfp-29) (Zinc finger protein 854) | May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis. {ECO:0000250}. |
Q86SE8 | NPM2 | S8 | ochoa | Nucleoplasmin-2 | Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. {ECO:0000269|PubMed:21863821}. |
Q86SQ7 | SDCCAG8 | S8 | ochoa | Serologically defined colon cancer antigen 8 (Antigen NY-CO-8) (Centrosomal colon cancer autoantigen protein) (hCCCAP) | Plays a role in the establishment of cell polarity and epithelial lumen formation (By similarity). Also plays an essential role in ciliogenesis and subsequent Hedgehog signaling pathway that requires the presence of intact primary cilia for pathway activation. Mechanistically, interacts with and mediates RABEP2 centrosomal localization which is critical for ciliogenesis (PubMed:27224062). {ECO:0000250|UniProtKB:Q80UF4, ECO:0000269|PubMed:27224062}. |
Q86SQ7 | SDCCAG8 | T9 | ochoa | Serologically defined colon cancer antigen 8 (Antigen NY-CO-8) (Centrosomal colon cancer autoantigen protein) (hCCCAP) | Plays a role in the establishment of cell polarity and epithelial lumen formation (By similarity). Also plays an essential role in ciliogenesis and subsequent Hedgehog signaling pathway that requires the presence of intact primary cilia for pathway activation. Mechanistically, interacts with and mediates RABEP2 centrosomal localization which is critical for ciliogenesis (PubMed:27224062). {ECO:0000250|UniProtKB:Q80UF4, ECO:0000269|PubMed:27224062}. |
Q86TI2 | DPP9 | T8 | ochoa | Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 2) (DPRP-2) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9) | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929, PubMed:36112693). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36112693, PubMed:36357533). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:33731929, PubMed:33731932, PubMed:34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (PubMed:33731929). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:31525884, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36112693, ECO:0000269|PubMed:36357533}. |
Q86U86 | PBRM1 | T9 | ochoa | Protein polybromo-1 (hPB1) (BRG1-associated factor 180) (BAF180) (Polybromo-1D) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
Q86U86 | PBRM1 | S10 | ochoa | Protein polybromo-1 (hPB1) (BRG1-associated factor 180) (BAF180) (Polybromo-1D) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
Q86UX6 | STK32C | S10 | ochoa | Serine/threonine-protein kinase 32C (EC 2.7.11.1) (PKE) (Yet another novel kinase 3) | None |
Q86UX7 | FERMT3 | S8 | ochoa | Fermitin family homolog 3 (Kindlin-3) (MIG2-like protein) (Unc-112-related protein 2) | Plays a central role in cell adhesion in hematopoietic cells (PubMed:19234463, PubMed:26359933). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234460). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity). {ECO:0000250|UniProtKB:Q8K1B8, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463, ECO:0000269|PubMed:26359933}.; FUNCTION: Isoform 2 may act as a repressor of NF-kappa-B and apoptosis. {ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463}. |
Q86V81 | ALYREF | S8 | ochoa | THO complex subunit 4 (Tho4) (Ally of AML-1 and LEF-1) (Aly/REF export factor) (Transcriptional coactivator Aly/REF) (bZIP-enhancing factor BEF) | Functions as an mRNA export adapter; component of the transcription/export (TREX) complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B (PubMed:17984224). Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex (PubMed:37020021). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:37020021). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224, PubMed:37020021). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway) (PubMed:11675789, PubMed:11707413, PubMed:11979277, PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim (PubMed:19165146). Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (PubMed:28418038). Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation (PubMed:10488337). Involved in transcription elongation and genome stability (PubMed:12438613). {ECO:0000269|PubMed:10488337, ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:11707413, ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:37020021}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. {ECO:0000269|PubMed:12438613, ECO:0000269|PubMed:18974867}. |
Q86V86 | PIM3 | S8 | ochoa | Serine/threonine-protein kinase pim-3 (EC 2.7.11.1) | Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth. {ECO:0000269|PubMed:15540201, ECO:0000269|PubMed:16818649, ECO:0000269|PubMed:17270021, ECO:0000269|PubMed:17876606, ECO:0000269|PubMed:18593906}. |
Q86VP6 | CAND1 | S9 | ochoa | Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (TBP-interacting protein of 120 kDa A) (TBP-interacting protein 120A) (p120 CAND1) | Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes. {ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}. |
Q86VQ6 | TXNRD3 | S8 | ochoa | Thioredoxin reductase 3 (EC 1.8.1.9) (Thioredoxin and glutathione reductase) (Thioredoxin reductase 3 intronic transcript 1) (Thioredoxin reductase 3 neighbor gene) (Thioredoxin reductase TR2) | Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity). {ECO:0000250|UniProtKB:Q99MD6}. |
Q86VR2 | RETREG3 | T9 | ochoa | Reticulophagy regulator 3 | 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). Promotes ER membrane curvature and ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes (PubMed:33826365). Required for collagen quality control in a LIR motif-dependent manner (By similarity). Mediates NRF1-enhanced neurite outgrowth (PubMed:26040720). {ECO:0000250|UniProtKB:Q9CQV4, ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:33826365, ECO:0000269|PubMed:34338405}. |
Q86WJ1 | CHD1L | S8 | ochoa | Chromodomain-helicase-DNA-binding protein 1-like (EC 3.6.4.-) (Amplified in liver cancer protein 1) | ATP-dependent chromatin remodeler that mediates chromatin-remodeling following DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:33357431, PubMed:34210977, PubMed:34486521, PubMed:34874266). Recruited to DNA damage sites through interaction with poly-ADP-ribose: specifically recognizes and binds histones that are poly-ADP-ribosylated on serine residues in response to DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Poly-ADP-ribose-binding activates the ATP-dependent chromatin remodeler activity, thereby regulating chromatin during DNA repair (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Catalyzes nucleosome sliding away from DNA breaks in an ATP-dependent manner (PubMed:19661379, PubMed:29220652, PubMed:29220653). Chromatin remodeling activity promotes PARP2 removal from chromatin (PubMed:33275888). {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:33275888, ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34210977, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. |
Q86WR7 | PROSER2 | S8 | ochoa | Proline and serine-rich protein 2 | None |
Q86XR8 | CEP57 | S10 | ochoa | Centrosomal protein of 57 kDa (Cep57) (FGF2-interacting protein) (Testis-specific protein 57) (Translokin) | Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring-like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2, but that of FGF1. {ECO:0000269|PubMed:22321063}. |
Q86Y82 | STX12 | Y9 | ochoa | Syntaxin-12 | SNARE promoting fusion of transport vesicles with target membranes. Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. {ECO:0000250|UniProtKB:G3V7P1}. |
Q86YV0 | RASAL3 | T9 | ochoa | RAS protein activator like-3 | Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}. |
Q86YV0 | RASAL3 | S10 | ochoa | RAS protein activator like-3 | Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}. |
Q86Z02 | HIPK1 | S9 | ochoa | Homeodomain-interacting protein kinase 1 (EC 2.7.11.1) (Nuclear body-associated kinase 2) | Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (PubMed:24559171). {ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:19646965, ECO:0000269|PubMed:24559171}. |
Q8IU68 | TMC8 | S8 | ochoa | Transmembrane channel-like protein 8 (Epidermodysplasia verruciformis protein 2) | Acts as a regulatory protein involved in the regulation of numerous cellular processes (PubMed:18158319, PubMed:23429285, PubMed:30068544, PubMed:32917726). Together with its homolog TMC6/EVER1, forms a complex with calcium-binding protein CIB1 in lymphocytes and keratynocytes where TMC6 and TMC8 stabilize CIB1 levels and reciprocally (PubMed:30068544, PubMed:32917726). Together with TMC6, also forms a complex with and activates zinc transporter ZNT1 at the ER membrane of keratynocytes, thereby facilitating zinc uptake into the ER (PubMed:18158319). Also inhibits receptor-mediated calcium release from ER stores and calcium activated and volume regulated chloride channels (PubMed:25220380). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also sequesters TRADD which impairs the recruitment of TRAF2 and RIPK1 in the pro-survival complex I and promotes proapoptotic complex II formation, and may therefore be involved in TNF-induced cell death/survival decisions (PubMed:23429285). {ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:23429285, ECO:0000269|PubMed:25220380, ECO:0000269|PubMed:30068544, ECO:0000269|PubMed:32917726}. |
Q8IU68 | TMC8 | S9 | ochoa | Transmembrane channel-like protein 8 (Epidermodysplasia verruciformis protein 2) | Acts as a regulatory protein involved in the regulation of numerous cellular processes (PubMed:18158319, PubMed:23429285, PubMed:30068544, PubMed:32917726). Together with its homolog TMC6/EVER1, forms a complex with calcium-binding protein CIB1 in lymphocytes and keratynocytes where TMC6 and TMC8 stabilize CIB1 levels and reciprocally (PubMed:30068544, PubMed:32917726). Together with TMC6, also forms a complex with and activates zinc transporter ZNT1 at the ER membrane of keratynocytes, thereby facilitating zinc uptake into the ER (PubMed:18158319). Also inhibits receptor-mediated calcium release from ER stores and calcium activated and volume regulated chloride channels (PubMed:25220380). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also sequesters TRADD which impairs the recruitment of TRAF2 and RIPK1 in the pro-survival complex I and promotes proapoptotic complex II formation, and may therefore be involved in TNF-induced cell death/survival decisions (PubMed:23429285). {ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:23429285, ECO:0000269|PubMed:25220380, ECO:0000269|PubMed:30068544, ECO:0000269|PubMed:32917726}. |
Q8IUH3 | RBM45 | S9 | ochoa | RNA-binding protein 45 (Developmentally-regulated RNA-binding protein 1) (RB-1) (RNA-binding motif protein 45) | RNA-binding protein with binding specificity for poly(C). May play an important role in neural development. {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000269|PubMed:12220514}. |
Q8IUH4 | ZDHHC13 | S8 | psp | Palmitoyltransferase ZDHHC13 (EC 2.3.1.225) (Huntingtin-interacting protein 14-related protein) (HIP14-related protein) (Huntingtin-interacting protein HIP3RP) (Putative MAPK-activating protein PM03) (Putative NF-kappa-B-activating protein 209) (Zinc finger DHHC domain-containing protein 13) (DHHC-13) | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (By similarity). Palmitoyltransferase for HTT and GAD2. May play a role in Mg(2+) transport. {ECO:0000250|UniProtKB:Q9CWU2}. |
Q8IV56 | PRR15 | S9 | ochoa | Proline-rich protein 15 | May have a role in proliferation and/or differentiation. {ECO:0000250}. |
Q8IV56 | PRR15 | S10 | ochoa | Proline-rich protein 15 | May have a role in proliferation and/or differentiation. {ECO:0000250}. |
Q8IWA5 | SLC44A2 | Y8 | ochoa | Choline transporter-like protein 2 (Solute carrier family 44 member 2) | [Isoform 1]: Choline/H+ antiporter, mainly in mitochodria (PubMed:10677542, PubMed:20665236, PubMed:23651124, PubMed:33789160). Also acts as a low-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy pathway (PubMed:33789160). {ECO:0000269|PubMed:10677542, ECO:0000269|PubMed:20665236, ECO:0000269|PubMed:23651124, ECO:0000269|PubMed:33789160}.; FUNCTION: [Isoform 3]: Does not exhibit choline transporter activity. {ECO:0000269|PubMed:10677542, ECO:0000269|PubMed:20665236}. |
Q8IXW5 | RPAP2 | S8 | ochoa | Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 (EC 3.1.3.16) (RNA polymerase II-associated protein 2) | Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes (PubMed:17643375, PubMed:22137580, PubMed:24997600). Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic reticulum unfolded protein response (UPR), to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:22137580, ECO:0000269|PubMed:24997600, ECO:0000269|PubMed:30118681}. |
Q8IXW5 | RPAP2 | S9 | ochoa | Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 (EC 3.1.3.16) (RNA polymerase II-associated protein 2) | Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes (PubMed:17643375, PubMed:22137580, PubMed:24997600). Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic reticulum unfolded protein response (UPR), to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:22137580, ECO:0000269|PubMed:24997600, ECO:0000269|PubMed:30118681}. |
Q8IY18 | SMC5 | S9 | ochoa | Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (hSMC5) | Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:26983541}. |
Q8IY67 | RAVER1 | T8 | ochoa | Ribonucleoprotein PTB-binding 1 (Protein raver-1) | Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}. |
Q8IYB3 | SRRM1 | T9 | 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 | S10 | 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}. |
Q8IYE0 | CCDC146 | T8 | ochoa | Coiled-coil domain-containing protein 146 | Essential for sperm flagellum biogenesis and male fertility. {ECO:0000250|UniProtKB:E9Q9F7}. |
Q8IYJ3 | SYTL1 | S8 | psp | Synaptotagmin-like protein 1 (Exophilin-7) (Protein JFC1) | May play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes (By similarity). {ECO:0000250, ECO:0000269|PubMed:11278853, ECO:0000269|PubMed:18266782}. |
Q8IZL8 | PELP1 | S10 | ochoa | Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) (Transcription factor HMX3) | Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors (PubMed:14963108). Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates pre-60S association of the critical remodeling factor MDN1 (PubMed:21326211). May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K. {ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108, ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770, ECO:0000269|PubMed:15579769, ECO:0000269|PubMed:15994929, ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611, ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:21326211, ECO:0000269|PubMed:22872859}. |
Q8N0S6 | CENPL | S9 | ochoa | Centromere protein L (CENP-L) (Interphase centromere complex protein 33) | Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16716197}. |
Q8N111 | CEND1 | S9 | ochoa | Cell cycle exit and neuronal differentiation protein 1 (BM88 antigen) | Involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9JKC6}. |
Q8N111 | CEND1 | S10 | ochoa | Cell cycle exit and neuronal differentiation protein 1 (BM88 antigen) | Involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9JKC6}. |
Q8N122 | RPTOR | S8 | 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}. |
Q8N3J5 | PPM1K | T8 | ochoa | Protein phosphatase Mn(2+)-dependent 1K (EC 3.1.3.16) (Branched-chain alpha-ketoacid dehydrogenase phosphatase) (BCKDH) (BDP) (EC 3.1.3.52) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C family member) (Protein phosphatase 2C isoform kappa) (PP2C-kappa) ([3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase, mitochondrial) | Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715). {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715, ECO:0000269|PubMed:19411760, ECO:0000269|PubMed:22291014, ECO:0000269|PubMed:22589535, ECO:0000269|PubMed:23086801, ECO:0000269|PubMed:29779826}. |
Q8N3U4 | STAG2 | T9 | 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}. |
Q8N4L2 | PIP4P2 | S10 | ochoa | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (Type 2 PtdIns-4,5-P2 4-Ptase) (EC 3.1.3.78) (PtdIns-4,5-P2 4-Ptase II) (Transmembrane protein 55A) | Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (PubMed:16365287). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (PubMed:16365287). Negatively regulates the phagocytosis of large particles by reducing phagosomal phosphatidylinositol 4,5-bisphosphate accumulation during cup formation (By similarity). {ECO:0000250|UniProtKB:Q9CZX7, ECO:0000269|PubMed:16365287}. |
Q8N594 | MPND | S8 | ochoa | MPN domain-containing protein (EC 3.4.-.-) | Probable protease (By similarity). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its degradation (PubMed:30982744). Binds only double strand DNA (dsDNA) in a sequence-independent manner (By similarity). {ECO:0000250|UniProtKB:Q3TV65, ECO:0000250|UniProtKB:Q5VVJ2, ECO:0000269|PubMed:30982744}. |
Q8N5F7 | NKAP | S9 | ochoa | NF-kappa-B-activating protein | Acts as a transcriptional repressor (PubMed:14550261, PubMed:19409814, PubMed:31587868). Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development (PubMed:19409814). Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter. {ECO:0000269|PubMed:14550261, ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:31587868}. |
Q8N5I9 | NOPCHAP1 | S10 | ochoa | NOP protein chaperone 1 | Client-loading PAQosome/R2TP complex cofactor that selects NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP) assembly. Acts as a bridge between NOP58 and the R2TP complex via RUVBL1:RUVBL2. {ECO:0000269|PubMed:33367824}. |
Q8N6S5 | ARL6IP6 | S10 | ochoa | ADP-ribosylation factor-like protein 6-interacting protein 6 (ARL-6-interacting protein 6) (Aip-6) (Phosphonoformate immuno-associated protein 1) | None |
Q8N6T7 | SIRT6 | S10 | ochoa|psp | NAD-dependent protein deacylase sirtuin-6 (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-6) (EC 2.3.1.286) (Protein mono-ADP-ribosyltransferase sirtuin-6) (EC 2.4.2.-) (Regulatory protein SIR2 homolog 6) (hSIRT6) (SIR2-like protein 6) | NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (PubMed:18337721, PubMed:19135889, PubMed:19625767, PubMed:21362626, PubMed:21680843, PubMed:23217706, PubMed:23552949, PubMed:23653361, PubMed:24052263, PubMed:27180906, PubMed:27322069, PubMed:29555651, PubMed:30374165). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (PubMed:23552949, PubMed:24052263, PubMed:27322069). Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B (PubMed:19625767, PubMed:21362626, PubMed:23892288, PubMed:23911928, PubMed:24012758, PubMed:26456828, PubMed:26898756, PubMed:27043296, PubMed:27180906, PubMed:30374165, PubMed:33067423). Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing (By similarity). Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac (PubMed:23911928, PubMed:31995034, PubMed:32538779). SIRT6 participation to DSB repair is probably involved in extension of life span (By similarity). Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (PubMed:29474172, PubMed:32789493). Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (PubMed:27043296). Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage (PubMed:18337721, PubMed:19625767, PubMed:21847107). Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac (PubMed:25915124, PubMed:29555651). Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism (PubMed:24012758, PubMed:26787900). Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes (By similarity). Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect (PubMed:23217706). Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (PubMed:26787900). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 (PubMed:23142079, PubMed:25009184). Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA (By similarity). Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 (By similarity). Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 (By similarity). The defatty-acylase activity is specifically involved in regulation of protein secretion (PubMed:23552949, PubMed:24052263, PubMed:27322069, PubMed:28406396). Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (PubMed:23552949, PubMed:28406396). Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 (PubMed:21680843, PubMed:22753495, PubMed:27322069, PubMed:27568560). Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription (PubMed:21680843, PubMed:22753495, PubMed:27568560). {ECO:0000250|UniProtKB:P59941, ECO:0000269|PubMed:18337721, ECO:0000269|PubMed:19135889, ECO:0000269|PubMed:19625767, ECO:0000269|PubMed:21362626, ECO:0000269|PubMed:21680843, ECO:0000269|PubMed:21847107, ECO:0000269|PubMed:22753495, ECO:0000269|PubMed:23142079, ECO:0000269|PubMed:23217706, ECO:0000269|PubMed:23552949, ECO:0000269|PubMed:23653361, ECO:0000269|PubMed:23892288, ECO:0000269|PubMed:23911928, ECO:0000269|PubMed:24012758, ECO:0000269|PubMed:24052263, ECO:0000269|PubMed:25009184, ECO:0000269|PubMed:25915124, ECO:0000269|PubMed:26456828, ECO:0000269|PubMed:26787900, ECO:0000269|PubMed:26898756, ECO:0000269|PubMed:27043296, ECO:0000269|PubMed:27180906, ECO:0000269|PubMed:27322069, ECO:0000269|PubMed:27568560, ECO:0000269|PubMed:28406396, ECO:0000269|PubMed:29474172, ECO:0000269|PubMed:29555651, ECO:0000269|PubMed:30374165, ECO:0000269|PubMed:31995034, ECO:0000269|PubMed:32538779, ECO:0000269|PubMed:32789493, ECO:0000269|PubMed:33067423}. |
Q8N726 | CDKN2A | T8 | psp | Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF) | Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (By similarity). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development. {ECO:0000250|UniProtKB:Q64364, ECO:0000269|PubMed:11314011, ECO:0000269|PubMed:11314038, ECO:0000269|PubMed:12660818, ECO:0000269|PubMed:14636574, ECO:0000269|PubMed:15361825, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15876874, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:16713577, ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:22094112, ECO:0000269|PubMed:9724636}.; FUNCTION: [Isoform smARF]: May be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform is stabilized by C1QBP. {ECO:0000269|PubMed:16713577}. |
Q8N7R7 | CCNYL1 | S10 | ochoa | Cyclin-Y-like protein 1 | Key regulator of Wnt signaling implicated in various biological processes including male fertility, embryonic neurogenesis and cortex development. Activates the cyclin-dependent kinase CDK16, and promotes sperm maturation. {ECO:0000250|UniProtKB:D3YUJ3}. |
Q8N8F7 | LSMEM1 | T8 | ochoa | Leucine-rich single-pass membrane protein 1 | None |
Q8N8F7 | LSMEM1 | S10 | ochoa | Leucine-rich single-pass membrane protein 1 | None |
Q8N9Q2 | SREK1IP1 | S10 | ochoa | Protein SREK1IP1 (SFRS12-interacting protein 1) (SREK1-interacting protein 1) (Splicing regulatory protein of 18 kDa) (p18SRP) | Possible splicing regulator involved in the control of cellular survival. |
Q8NBF2 | NHLRC2 | S10 | ochoa | NHL repeat-containing protein 2 | Required for normal embryonic development. {ECO:0000250|UniProtKB:Q8BZW8}. |
Q8NCA9 | ZNF784 | S10 | ochoa | Zinc finger protein 784 | May be involved in transcriptional regulation. |
Q8NCY6 | MSANTD4 | S10 | ochoa | Myb/SANT-like DNA-binding domain-containing protein 4 (Myb/SANT-like DNA-binding domain containing 4 with coiled-coils) | None |
Q8NDT2 | RBM15B | S10 | ochoa | Putative RNA-binding protein 15B (One-twenty two protein 3) (HsOTT3) (HuOTT3) (RNA-binding motif protein 15B) | RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:27602518). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA splicing (PubMed:21044963). Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1 (PubMed:19586903). {ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:21044963, ECO:0000269|PubMed:27602518, ECO:0000305|PubMed:16129689}. |
Q8NEL9 | DDHD1 | S8 | ochoa|psp | Phospholipase DDHD1 (EC 3.1.1.111) (EC 3.1.1.32) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1) (EC 3.1.1.118) (Phospholipid sn-1 acylhydrolase) | Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (Probable) (PubMed:20359546, PubMed:22922100). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (Probable) (PubMed:20359546). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology (PubMed:24599962). These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (PubMed:24599962). May play a regulatory role in spermatogenesis or sperm function (PubMed:24599962). {ECO:0000250|UniProtKB:Q80YA3, ECO:0000269|PubMed:20359546, ECO:0000269|PubMed:22922100, ECO:0000269|PubMed:24599962, ECO:0000303|PubMed:24599962, ECO:0000305|PubMed:37189713}. |
Q8NEZ2 | VPS37A | S10 | ochoa | Vacuolar protein sorting-associated protein 37A (hVps37A) (ESCRT-I complex subunit VPS37A) (Hepatocellular carcinoma-related protein 1) | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15240819}. |
Q8NFT2 | STEAP2 | S9 | ochoa | Metalloreductase STEAP2 (EC 1.16.1.-) (Prostate cancer-associated protein 1) (Protein up-regulated in metastatic prostate cancer) (PUMPCn) (Six-transmembrane epithelial antigen of prostate 2) (SixTransMembrane protein of prostate 1) | Integral membrane protein that functions as a NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane (By similarity). Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By similarity). Can also reduce Cu(2+) to Cu(1+) (By similarity). {ECO:0000250|UniProtKB:Q687X5, ECO:0000250|UniProtKB:Q8BWB6}. |
Q8NFU3 | TSTD1 | S8 | ochoa | Thiosulfate:glutathione sulfurtransferase (TST) (EC 2.8.1.3) | Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism (PubMed:24981631). Provides the link between the first step in mammalian H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate (PubMed:24981631). The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor (PubMed:24981631). GSS(-) spontaneously reacts with glutathione to form glutathione disulfide (Probable). {ECO:0000269|PubMed:24981631, ECO:0000305}. |
Q8NFY9 | KBTBD8 | S10 | ochoa | Kelch repeat and BTB domain-containing protein 8 (T-cell activation kelch repeat protein) (TA-KRP) | Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification (PubMed:26399832). The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the formation of a NOLC1-TCOF1 complex that 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:26399832}. |
Q8NG97 | OR2Z1 | S10 | ochoa | Olfactory receptor 2Z1 (Olfactory receptor 2Z2) (Olfactory receptor OR19-4) | Odorant receptor. {ECO:0000305}. |
Q8TAA9 | VANGL1 | S8 | ochoa | Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) | None |
Q8TAC2 | JOSD2 | S10 | ochoa | Josephin-2 (EC 3.4.19.12) (Josephin domain-containing protein 2) | Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme. {ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:21118805, ECO:0000269|PubMed:23625928}. |
Q8TBC5 | ZSCAN18 | S10 | ochoa | Zinc finger and SCAN domain-containing protein 18 (Zinc finger protein 447) | May be involved in transcriptional regulation. |
Q8TBE0 | BAHD1 | S8 | ochoa | Bromo adjacent homology domain-containing 1 protein (BAH domain-containing protein 1) | Heterochromatin protein that acts as a transcription repressor and has the ability to promote the formation of large heterochromatic domains. May act by recruiting heterochromatin proteins such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by binding to its CpG-rich P3 promoter and recruiting heterochromatin proteins. At specific stages of Listeria infection, in complex with TRIM28, corepresses interferon-stimulated genes, including IFNL1, IFNL2 and IFNL3. {ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:21252314}. |
Q8TDB6 | DTX3L | S9 | ochoa | E3 ubiquitin-protein ligase DTX3L (EC 2.3.2.27) (B-lymphoma- and BAL-associated protein) (Protein deltex-3-like) (RING-type E3 ubiquitin transferase DTX3L) (Rhysin-2) (Rhysin2) | E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses (PubMed:12670957, PubMed:19818714, PubMed:23230272, PubMed:26479788). Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4 (PubMed:28525742). In response to DNA damage, mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1) (PubMed:19818714). The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me) (PubMed:19818714). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). By monoubiquitinating histone H2B H2BC9/H2BJ and thereby promoting chromatin remodeling, positively regulates STAT1-dependent interferon-stimulated gene transcription and thus STAT1-mediated control of viral replication (PubMed:26479788). Independently of its catalytic activity, promotes the sorting of chemokine receptor CXCR4 from early endosome to lysosome following CXCL12 stimulation by reducing E3 ligase ITCH activity and thus ITCH-mediated ubiquitination of endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (PubMed:24790097). In addition, required for the recruitment of HGS and STAM to early endosomes (PubMed:24790097). In association with PARP9, plays a role in antiviral responses by mediating 'Lys-48'-linked ubiquitination of encephalomyocarditis virus (EMCV) and human rhinovirus (HRV) C3 proteases and thus promoting their proteasomal-mediated degradation (PubMed:26479788). {ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:19818714, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:24790097, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742}. |
Q8TDH9 | BLOC1S5 | T8 | ochoa | Biogenesis of lysosome-related organelles complex 1 subunit 5 (BLOC-1 subunit 5) (Protein Muted homolog) | Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes (PubMed:32565547). In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:32565547}. |
Q8TE77 | SSH3 | S9 | ochoa | Protein phosphatase Slingshot homolog 3 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 3) (SSH-3L) (hSSH-3L) | Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). {ECO:0000250}. |
Q8TEB1 | DCAF11 | S8 | ochoa | DDB1- and CUL4-associated factor 11 (WD repeat-containing protein 23) | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}. |
Q8TF42 | UBASH3B | S8 | ochoa | Ubiquitin-associated and SH3 domain-containing protein B (EC 3.1.3.48) (Cbl-interacting protein p70) (Suppressor of T-cell receptor signaling 1) (STS-1) (T-cell ubiquitin ligand 2) (TULA-2) (Tyrosine-protein phosphatase STS1/TULA2) | Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination. {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17880946}. |
Q8TF76 | HASPIN | S10 | psp | Serine/threonine-protein kinase haspin (EC 2.7.11.1) (Germ cell-specific gene 2 protein) (H-haspin) (Haploid germ cell-specific nuclear protein kinase) | Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle. {ECO:0000269|PubMed:11228240, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:17084365, ECO:0000269|PubMed:20705812, ECO:0000269|PubMed:20929775}. |
Q8WV19 | SFT2D1 | S9 | ochoa | Vesicle transport protein SFT2A (SFT2 domain-containing protein 1) (pRGR1) | May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}. |
Q8WVC0 | LEO1 | S10 | ochoa | RNA polymerase-associated protein LEO1 (Replicative senescence down-regulated leo1-like protein) | Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling. {ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15791002, ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}. |
Q8WVE0 | EEF1AKMT1 | T9 | ochoa | EEF1A lysine methyltransferase 1 (EC 2.1.1.-) (N(6)-adenine-specific DNA methyltransferase 2) (Protein-lysine N-methyltransferase N6AMT2) (eEF1A-KMT) | Protein N-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'. {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000269|PubMed:26545399, ECO:0000269|PubMed:28663172}. |
Q8WWH5 | TRUB1 | S10 | ochoa | Pseudouridylate synthase TRUB1 (EC 5.4.99.-) (TruB pseudouridine synthase homolog 1) (tRNA pseudouridine 55 synthase TRUB1) (Psi55 synthase TRUB1) (EC 5.4.99.25) | Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs (PubMed:28073919, PubMed:31477916, PubMed:32926445). Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure (PubMed:28073919, PubMed:31477916). Constitutes the major pseudouridine synthase acting on mRNAs (PubMed:28073919). Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs (PubMed:32926445, PubMed:33023933). Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity (PubMed:32926445). Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28-binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation (PubMed:32926445). {ECO:0000269|PubMed:28073919, ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:32926445, ECO:0000269|PubMed:33023933}. |
Q8WWP7 | GIMAP1 | T8 | ochoa | GTPase IMAP family member 1 (Immunity-associated protein 1) (hIMAP1) | May regulate lymphocyte survival. Required for normal levels of mature T-lymphocytes and mature B-cells (By similarity). {ECO:0000250}. |
Q8WXF7 | ATL1 | S10 | ochoa | Atlastin-1 (ATL-1) (EC 3.6.5.-) (Brain-specific GTP-binding protein) (GTP-binding protein 3) (GBP-3) (hGBP3) (Guanine nucleotide-binding protein 3) (Spastic paraplegia 3 protein A) | Atlastin-1 (ATL1) 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:14506257, PubMed:18270207, PubMed:19665976, PubMed:27619977, PubMed:34817557, PubMed:38509071). Two atlastin-1 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 (PubMed:14506257, PubMed:21220294, PubMed:21368113, PubMed:23334294, PubMed:38509071). May also regulate more or less directly Golgi biogenesis (PubMed:17321752). Indirectly regulates axonal development (By similarity). {ECO:0000250|UniProtKB:Q6PST4, ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:21368113, ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:34817557, ECO:0000269|PubMed:38509071}. |
Q8WYL5 | SSH1 | S9 | ochoa | Protein phosphatase Slingshot homolog 1 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 1) (SSH-1L) (hSSH-1L) | Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:14645219, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460}. |
Q8WYQ5 | DGCR8 | S8 | 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}. |
Q92599 | SEPTIN8 | S10 | ochoa | Septin-8 | Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (PubMed:15116257). Seems to participate in the process of SNARE complex formation in synaptic vesicles (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:B0BNF1, ECO:0000269|PubMed:15116257}.; FUNCTION: [Isoform 4]: Stabilizes BACE1 protein levels and promotes the sorting and accumulation of BACE1 to the recycling or endosomal compartments, modulating the beta-amyloidogenic processing of APP. {ECO:0000269|PubMed:27084579}. |
Q92609 | TBC1D5 | T8 | ochoa | TBC1 domain family member 5 | May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583, ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}. |
Q92613 | JADE3 | S8 | ochoa | Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16) | Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. {ECO:0000269|PubMed:16387653}. |
Q92613 | JADE3 | S9 | ochoa | Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16) | Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. {ECO:0000269|PubMed:16387653}. |
Q92613 | JADE3 | S10 | ochoa | Protein Jade-3 (Jade family PHD finger protein 3) (PHD finger protein 16) | Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. {ECO:0000269|PubMed:16387653}. |
Q92734 | TFG | S8 | ochoa | Protein TFG (TRK-fused gene protein) | Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858). {ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:23479643, ECO:0000269|PubMed:27813252}. |
Q92826 | HOXB13 | T8 | psp | Homeobox protein Hox-B13 | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds preferentially to methylated DNA (PubMed:28473536). {ECO:0000269|PubMed:28473536}. |
Q92888 | ARHGEF1 | S10 | ochoa | Rho guanine nucleotide exchange factor 1 (115 kDa guanine nucleotide exchange factor) (p115-RhoGEF) (p115RhoGEF) (Sub1.5) | Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits (PubMed:9641915, PubMed:9641916). Acts as a GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase (PubMed:30521495, PubMed:8810315, PubMed:9641915, PubMed:9641916). Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain (PubMed:9641916). This GEF activity is inhibited by binding to activated GNA12 (PubMed:9641916). Mediates angiotensin-2-induced RhoA activation (PubMed:20098430). In lymphoid follicles, may trigger activation of GNA13 as part of S1PR2-dependent signaling pathway that leads to inhibition of germinal center (GC) B cell growth and migration outside the GC niche. {ECO:0000250|UniProtKB:Q61210, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:30521495, ECO:0000269|PubMed:8810315, ECO:0000269|PubMed:9641915, ECO:0000269|PubMed:9641916}. |
Q92900 | UPF1 | S9 | 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}. |
Q92900 | UPF1 | S10 | 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}. |
Q92963 | RIT1 | S10 | ochoa | GTP-binding protein Rit1 (EC 3.6.5.2) (Ras-like protein expressed in many tissues) (Ras-like without CAAX protein 1) | Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation. {ECO:0000269|PubMed:15632082, ECO:0000269|PubMed:23791108}. |
Q93015 | NAA80 | S8 | ochoa | N-alpha-acetyltransferase 80 (HsNAAA80) (EC 2.3.1.-) (N-acetyltransferase 6) (Protein fusion-2) (Protein fus-2) | N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively) (PubMed:29581253, PubMed:30028079). N-terminal acetylation of processed beta- and gamma-actin regulates actin filament depolymerization and elongation (PubMed:29581253). In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu (PubMed:29581253, PubMed:30028079). In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp (PubMed:10644992, PubMed:29581307). May act as a tumor suppressor (PubMed:10644992). {ECO:0000269|PubMed:10644992, ECO:0000269|PubMed:29581253, ECO:0000269|PubMed:29581307, ECO:0000269|PubMed:30028079}. |
Q969F1 | GTF3C6 | S9 | ochoa | General transcription factor 3C polypeptide 6 (Transcription factor IIIC 35 kDa subunit) (TFIIIC 35 kDa subunit) (TFIIIC35) (Transcription factor IIIC subunit 6) | Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters. {ECO:0000269|PubMed:17409385}. |
Q969H0 | FBXW7 | S10 | psp | F-box/WD repeat-containing protein 7 (Archipelago homolog) (hAgo) (F-box and WD-40 domain-containing protein 7) (F-box protein FBX30) (SEL-10) (hCdc4) | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:17434132, PubMed:22748924, PubMed:26976582, PubMed:28727686, PubMed:34741373, PubMed:35395208). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination (PubMed:17434132, PubMed:22748924, PubMed:26774286, PubMed:26976582, PubMed:28727686, PubMed:34741373). Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NFE2L1, NOTCH2, MCL1, MLST8, RICTOR, and probably PSEN1 (PubMed:11565034, PubMed:11585921, PubMed:12354302, PubMed:14739463, PubMed:15103331, PubMed:17558397, PubMed:17873522, PubMed:22608923, PubMed:22748924, PubMed:25775507, PubMed:25897075, PubMed:26976582, PubMed:28007894, PubMed:28727686, PubMed:29149593, PubMed:34102342). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (PubMed:14739463). Involved in bone homeostasis and negative regulation of osteoclast differentiation (PubMed:29149593). Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination (PubMed:27238018). Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage (PubMed:26774286). The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining (PubMed:26774286). {ECO:0000269|PubMed:11565034, ECO:0000269|PubMed:11585921, ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:22608923, ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:26774286, ECO:0000269|PubMed:26976582, ECO:0000269|PubMed:27238018, ECO:0000269|PubMed:28007894, ECO:0000269|PubMed:28727686, ECO:0000269|PubMed:29149593, ECO:0000269|PubMed:34102342, ECO:0000269|PubMed:34741373, ECO:0000269|PubMed:35395208, ECO:0000305|PubMed:12354302}. |
Q969T4 | UBE2E3 | S8 | ochoa | Ubiquitin-conjugating enzyme E2 E3 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme E3) (UbcH9) (Ubiquitin carrier protein E3) (Ubiquitin-conjugating enzyme E2-23 kDa) (Ubiquitin-protein ligase E3) | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. {ECO:0000269|PubMed:10343118, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27237050}. |
Q96AY2 | EME1 | S9 | ochoa | Structure-specific endonuclease subunit EME1 (Crossover junction endonuclease EME1) (Essential meiotic structure-specific endonuclease 1) (MMS4 homolog) (hMMS4) | Non-catalytic subunit of the structure-specific, heterodimeric DNA endonuclease MUS81-EME1 which is involved in the maintenance of genome stability. In the complex, EME1 is required for DNA cleavage, participating in DNA recognition and bending (PubMed:12686547, PubMed:12721304, PubMed:14617801, PubMed:17289582, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). MUS81-EME1 cleaves 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24733841, PubMed:35290797). Active during prometaphase, MUS81-EME1 resolves mitotic recombination intermediates, including Holliday junctions, which form during homologous recombination (PubMed:14617801, PubMed:24813886). {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582, ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:24813886, ECO:0000269|PubMed:35290797, ECO:0000269|PubMed:39015284}. |
Q96AZ1 | EEF1AKMT3 | S10 | ochoa | EEF1A lysine methyltransferase 3 (EC 2.1.1.-) (Hepatocellular carcinoma-associated antigen 557a) (Methyltransferase-like protein 21B) (Protein-lysine methyltransferase METTL21B) (eEF1A-KMT3) | Protein-lysine methyltransferase that selectively mono-, di- and trimethylates 'Lys-165' of the translation elongation factors EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner. EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. {ECO:0000269|PubMed:28108655, ECO:0000269|PubMed:28663172}. |
Q96B18 | DACT3 | S10 | ochoa | Dapper homolog 3 (Antagonist of beta-catenin Dapper homolog 3) (Arginine-rich region 1 protein) (Dapper antagonist of catenin 3) | May be involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. {ECO:0000269|PubMed:18538736}. |
Q96B49 | TOMM6 | S9 | ochoa | Mitochondrial import receptor subunit TOM6 homolog (Overexpressed breast tumor protein) (Translocase of outer membrane 6 kDa subunit homolog) | None |
Q96BT3 | CENPT | S8 | ochoa | Centromere protein T (CENP-T) (Interphase centromere complex protein 22) | Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:21529714, ECO:0000269|PubMed:21695110}. |
Q96BT3 | CENPT | S10 | ochoa | Centromere protein T (CENP-T) (Interphase centromere complex protein 22) | Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:21529714, ECO:0000269|PubMed:21695110}. |
Q96C19 | EFHD2 | T8 | ochoa | EF-hand domain-containing protein D2 (Swiprosin-1) | May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000250}. |
Q96CC6 | RHBDF1 | S8 | ochoa | Inactive rhomboid protein 1 (iRhom1) (Epidermal growth factor receptor-related protein) (Rhomboid 5 homolog 1) (Rhomboid family member 1) (p100hRho) | Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:18524845, ECO:0000269|PubMed:18832597, ECO:0000269|PubMed:21439629}. |
Q96CC6 | RHBDF1 | S10 | ochoa | Inactive rhomboid protein 1 (iRhom1) (Epidermal growth factor receptor-related protein) (Rhomboid 5 homolog 1) (Rhomboid family member 1) (p100hRho) | Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:18524845, ECO:0000269|PubMed:18832597, ECO:0000269|PubMed:21439629}. |
Q96CG3 | TIFA | T9 | psp | TRAF-interacting protein with FHA domain-containing protein A (Putative MAPK-activating protein PM14) (Putative NF-kappa-B-activating protein 20) (TRAF2-binding protein) | Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (PubMed:12566447, PubMed:15492226, PubMed:26068852, PubMed:28222186, PubMed:28877472, PubMed:30111836). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (PubMed:15492226, PubMed:26068852). TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of pro-inflammatory NF-kappa-B signaling (PubMed:30111836). {ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:15492226, ECO:0000269|PubMed:26068852, ECO:0000269|PubMed:28222186, ECO:0000269|PubMed:28877472, ECO:0000269|PubMed:30111836}. |
Q96CP6 | GRAMD1A | S8 | 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}. |
Q96D31 | ORAI1 | S10 | ochoa | Calcium release-activated calcium channel protein 1 (Protein orai-1) (Transmembrane protein 142A) | Pore-forming subunit of 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 (Probable) (PubMed:16645049, PubMed:16733527, PubMed:16807233, PubMed:16921383, PubMed:19249086, PubMed:19706554, PubMed:23307288, PubMed:26956484, PubMed:28219928). Assembles with ORAI2 and ORAI3 to form hexameric CRAC channels that mediate Ca(2+) influx upon depletion of endoplasmic reticulum Ca(2+) store and channel activation by Ca(2+) sensor STIM1, a process known as store-operated Ca(2+) entry (SOCE). Various pore subunit combinations may account for distinct CRAC channel spatiotemporal and cell-type specific dynamics. ORAI1 mainly contributes to the generation of Ca(2+) plateaus involved in sustained Ca(2+) entry and is dispensable for cytosolic Ca(2+) oscillations, whereas ORAI2 and ORAI3 generate oscillatory patterns. CRAC channels assemble in Ca(2+) signaling microdomains where Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT transcription factors recruited to ORAI1 via AKAP5. Activates NFATC2/NFAT1 and NFATC3/NFAT4-mediated transcriptional responses. CRAC channels are the main pathway for Ca(2+) influx in T cells and promote the immune response to pathogens by activating NFAT-dependent cytokine and chemokine transcription (PubMed:16582901, PubMed:17442569, PubMed:19182790, PubMed:20354224, PubMed:22641696, PubMed:26221052, PubMed:32415068, PubMed:33941685). Assembles with ORAI3 to form channels that mediate store-independent Ca(2+) influx in response to inflammatory metabolites arachidonate or its derivative leukotriene C4, termed ARC and LRC channels respectively (PubMed:19622606, PubMed:32415068). Plays a prominent role in Ca(2+) influx at the basolateral membrane of mammary epithelial cells independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May mediate transepithelial transport of large quantities of Ca(2+) for milk secretion (By similarity) (PubMed:20887894). {ECO:0000250|UniProtKB:Q8BWG9, ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:16921383, ECO:0000269|PubMed:17442569, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19622606, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:20354224, ECO:0000269|PubMed:20887894, ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:26221052, ECO:0000269|PubMed:26956484, ECO:0000269|PubMed:28219928, ECO:0000269|PubMed:32415068, ECO:0000269|PubMed:33941685, ECO:0000305|PubMed:16766533}.; FUNCTION: [Isoform alpha]: Pore-forming subunit of both CRAC and ARC channels. Couples Ca(2+) influx to NFAT-mediated transcriptional responses. {ECO:0000269|PubMed:16921383, ECO:0000269|PubMed:17442569, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19622606, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:26221052, ECO:0000269|PubMed:33941685}.; FUNCTION: [Isoform beta]: Pore-forming subunit of CRAC channels exclusively. {ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:26221052, ECO:0000269|PubMed:33941685}. |
Q96D46 | NMD3 | T8 | ochoa | 60S ribosomal export protein NMD3 (hNMD3) | Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}. |
Q96DE5 | ANAPC16 | S8 | ochoa | Anaphase-promoting complex subunit 16 (APC16) (Cyclosome subunit 16) | 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:20360068). 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:20360068). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:29033132}. |
Q96DE5 | ANAPC16 | S9 | ochoa | Anaphase-promoting complex subunit 16 (APC16) (Cyclosome subunit 16) | 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:20360068). 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:20360068). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:29033132}. |
Q96DF8 | ESS2 | S10 | ochoa | Splicing factor ESS-2 homolog (DiGeorge syndrome critical region 13) (DiGeorge syndrome critical region 14) (DiGeorge syndrome protein H) (DGS-H) (Protein ES2) | May be involved in pre-mRNA splicing. {ECO:0000250|UniProtKB:P34420}. |
Q96DU7 | ITPKC | S9 | ochoa | Inositol-trisphosphate 3-kinase C (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase C) (IP3 3-kinase C) (IP3K C) (InsP 3-kinase C) | 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 (PubMed:11085927, PubMed:12747803). Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate (By similarity). {ECO:0000250|UniProtKB:Q80ZG2, ECO:0000269|PubMed:11085927, ECO:0000269|PubMed:12747803}. |
Q96E14 | RMI2 | S9 | ochoa | RecQ-mediated genome instability protein 2 (hRMI2) (BLM-associated protein of 18 kDa) (BLAP18) | Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates. It is required to regulate sister chromatid segregation and to limit DNA crossover. Essential for the stability, localization, and function of BLM, TOP3A, and complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM. {ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083, ECO:0000269|PubMed:27977684}. |
Q96EP1 | CHFR | S10 | ochoa | E3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING finger protein 196) (RING-type E3 ubiquitin transferase CHFR) | E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress. {ECO:0000269|PubMed:10935642, ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:14694445, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19182791}. |
Q96EV2 | RBM33 | S8 | 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}. |
Q96EW2 | HSPBAP1 | T8 | ochoa | HSPB1-associated protein 1 (27 kDa heat shock protein-associated protein 1) (Protein associated with small stress protein 1) | May play a role in cellular stress response. {ECO:0000250}. |
Q96EW2 | HSPBAP1 | T9 | ochoa | HSPB1-associated protein 1 (27 kDa heat shock protein-associated protein 1) (Protein associated with small stress protein 1) | May play a role in cellular stress response. {ECO:0000250}. |
Q96HB5 | CCDC120 | S9 | ochoa | Coiled-coil domain-containing protein 120 | Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth. {ECO:0000269|PubMed:25326380}. |
Q96HB5 | CCDC120 | S10 | ochoa | Coiled-coil domain-containing protein 120 | Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth. {ECO:0000269|PubMed:25326380}. |
Q96HR3 | MED30 | S9 | ochoa | Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25) | 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. {ECO:0000269|PubMed:11909976, ECO:0000269|PubMed:16595664}. |
Q96IZ0 | PAWR | T8 | ochoa | PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) | Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Also seems to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}. |
Q96IZ0 | PAWR | S9 | ochoa | PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) | Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Also seems to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}. |
Q96IZ0 | PAWR | S10 | ochoa | PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) | Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Also seems to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}. |
Q96K58 | ZNF668 | S10 | ochoa | Zinc finger protein 668 | May be involved in transcriptional regulation. May play a role in DNA repair process. {ECO:0000269|PubMed:34313816}. |
Q96KB5 | PBK | T9 | ochoa|psp | Lymphokine-activated killer T-cell-originated protein kinase (EC 2.7.12.2) (Cancer/testis antigen 84) (CT84) (MAPKK-like protein kinase) (Nori-3) (PDZ-binding kinase) (Spermatogenesis-related protein kinase) (SPK) (T-LAK cell-originated protein kinase) | Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. {ECO:0000269|PubMed:10781613, ECO:0000269|PubMed:17482142}. |
Q96LT7 | C9orf72 | S9 | ochoa | Guanine nucleotide exchange factor C9orf72 | Acts as a guanine-nucleotide releasing factor (GEF) for Rab GTPases by promoting the conversion of inactive RAB-GDP to the active form RAB-GTP (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531, PubMed:37821429). Acts as a GEF for RAB39A which enables HOPS-mediated autophagosome-lysosome membrane tethering and fusion in mammalian autophagy (PubMed:37821429). Component of the C9orf72-SMCR8 complex where both subunits display GEF activity and that regulates autophagy (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531). As part of the C9orf72-SMCR8-WDR41 (CSW) complex, functions as GEF for RAB8A and RAB39B, thereby promoting autophagosome maturation (PubMed:27103069). As part of the C9orf72-SMCR8 complex, also functions as GTPase activating protein (GAP) for RAB8A and RAB11A in vitro (PubMed:32303654). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and modulating its protein kinase activity (PubMed:27617292). Promotes initiation of autophagy by regulating the RAB1A-dependent trafficking of the ULK1/ATG1 kinase complex to the phagophore which leads to autophagosome formation (PubMed:27334615). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131). Plays a role in endosomal trafficking (PubMed:24549040). May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Promotes the lysosomal localization and lysosome-mediated degradation of CARM1 which leads to inhibition of starvation-induced lipid metabolism (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to CFL1/cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Required for SMCR8 protein expression and localization at pre- and post-synaptic compartments in the forebrain, also regulates protein abundance of RAB3A and GRIA1/GLUR1 in post-synaptic compartments in the forebrain and hippocampus (By similarity). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:27559131, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:28195531, ECO:0000269|PubMed:32303654, ECO:0000269|PubMed:37821429}.; FUNCTION: [Isoform 1]: Regulates stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}.; FUNCTION: [Isoform 2]: Does not play a role in regulation of stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}. |
Q96MF7 | NSMCE2 | S9 | ochoa | E3 SUMO-protein ligase NSE2 (EC 2.3.2.-) (E3 SUMO-protein transferase NSE2) (MMS21 homolog) (hMMS21) (Non-structural maintenance of chromosomes element 2 homolog) (Non-SMC element 2 homolog) | E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination (PubMed:16055714, PubMed:16810316). Is not be required for the stability of the complex (PubMed:16055714, PubMed:16810316). The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (PubMed:16055714, PubMed:16810316). The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) (PubMed:17589526). Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2 (PubMed:16055714, PubMed:16810316, PubMed:17589526, PubMed:31400850). Required for recruitment of telomeres to PML nuclear bodies (PubMed:17589526). SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines (PubMed:17589526). Required for sister chromatid cohesion during prometaphase and mitotic progression (PubMed:19502785). {ECO:0000269|PubMed:16055714, ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:31400850}. |
Q96MY1 | NOL4L | S8 | ochoa | Nucleolar protein 4-like | None |
Q96NB3 | ZNF830 | T9 | ochoa | Zinc finger protein 830 (Coiled-coil domain-containing protein 16) | May play a role in pre-mRNA splicing as component of the spliceosome (PubMed:25599396). Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription (By similarity). {ECO:0000250|UniProtKB:Q8R1N0, ECO:0000305|PubMed:25599396}. |
Q96QD8 | SLC38A2 | S10 | 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}. |
Q96QR8 | PURB | S8 | ochoa | Transcriptional regulator protein Pur-beta (Purine-rich element-binding protein B) | Transcriptional regulator which can act as an activator or a repressor. Represses the transcription of ACTA2 in fibroblasts and smooth muscle cells via its ability to interact with the purine-rich strand of a MCAT- containing element in the 5' flanking region of the gene. Represses the transcription of MYOCD, capable of repressing all isoforms of MYOCD but the magnitude of the repressive effects is most notable for the SMC- specific isoforms. Promotes hepatic glucose production by activating the transcription of ADCY6, leading to cAMP accumulation, increased PKA activity, CREB activation, and increased transcription of PCK1 and G6PC genes (By similarity). Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene (PubMed:1448097). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250|UniProtKB:O35295, ECO:0000250|UniProtKB:Q68A21, ECO:0000269|PubMed:1448097}. |
Q96R06 | SPAG5 | S8 | ochoa | Sperm-associated antigen 5 (Astrin) (Deepest) (Mitotic spindle-associated protein p126) (MAP126) | Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase (PubMed:11724960, PubMed:12356910, PubMed:27462074). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331, PubMed:27462074). In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457). {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074, ECO:0000305|PubMed:11724960}. |
Q96R06 | SPAG5 | S10 | ochoa | Sperm-associated antigen 5 (Astrin) (Deepest) (Mitotic spindle-associated protein p126) (MAP126) | Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase (PubMed:11724960, PubMed:12356910, PubMed:27462074). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331, PubMed:27462074). In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457). {ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:18361916, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:27462074, ECO:0000305|PubMed:11724960}. |
Q96S44 | TP53RK | T8 | ochoa | EKC/KEOPS complex subunit TP53RK (EC 3.6.-.-) (Atypical serine/threonine protein kinase TP53RK) (Nori-2) (TP53-regulating kinase) (EC 2.7.11.1) (p53-related protein kinase) | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (PubMed:22912744, PubMed:27903914). The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37 (PubMed:22912744, PubMed:27903914). TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation (PubMed:11546806). {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9, ECO:0000269|PubMed:11546806, ECO:0000305|PubMed:22912744, ECO:0000305|PubMed:27903914}. |
Q96S53 | TESK2 | S8 | ochoa | Dual specificity testis-specific protein kinase 2 (EC 2.7.12.1) (Testicular protein kinase 2) | Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis. |
Q96S97 | MYADM | T8 | ochoa | Myeloid-associated differentiation marker (Protein SB135) | None |
Q96S97 | MYADM | T9 | ochoa | Myeloid-associated differentiation marker (Protein SB135) | None |
Q96SB8 | SMC6 | S10 | ochoa | Structural maintenance of chromosomes protein 6 (SMC protein 6) (SMC-6) (hSMC6) | Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:26983541}. |
Q96ST3 | SIN3A | S10 | ochoa | Paired amphipathic helix protein Sin3a (Histone deacetylase complex subunit Sin3a) (Transcriptional corepressor Sin3a) | Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (By similarity). Required for cortical neuron differentiation and callosal axon elongation (By similarity). {ECO:0000250|UniProtKB:Q60520, ECO:0000269|PubMed:12150998}. |
Q99471 | PFDN5 | T8 | ochoa | Prefoldin subunit 5 (Myc modulator 1) (c-Myc-binding protein Mm-1) | Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. {ECO:0000269|PubMed:9630229}. |
Q99594 | TEAD3 | S9 | ochoa | Transcriptional enhancer factor TEF-5 (DTEF-1) (TEA domain family member 3) (TEAD-3) | Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, 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. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to multiple functional elements of the human chorionic somatomammotropin-B gene enhancer. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. |
Q99594 | TEAD3 | S10 | ochoa | Transcriptional enhancer factor TEF-5 (DTEF-1) (TEA domain family member 3) (TEAD-3) | Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, 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. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to multiple functional elements of the human chorionic somatomammotropin-B gene enhancer. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. |
Q99613 | EIF3C | S9 | ochoa | Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110) | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
Q99708 | RBBP8 | S10 | ochoa | DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) | Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117). {ECO:0000250|UniProtKB:Q80YR6, ECO:0000269|PubMed:15485915, ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462, ECO:0000269|PubMed:23273981, ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:30601117, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:33836577}. |
Q99767 | APBA2 | S8 | ochoa | Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2) | Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. |
Q9BPY3 | FAM118B | S9 | ochoa | Protein FAM118B | May play a role in Cajal bodies formation. {ECO:0000269|PubMed:24569877}. |
Q9BPZ3 | PAIP2 | S10 | ochoa | Polyadenylate-binding protein-interacting protein 2 (PABP-interacting protein 2) (PAIP-2) (Poly(A)-binding protein-interacting protein 2) | Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization. {ECO:0000269|PubMed:11172725}. |
Q9BR01 | SULT4A1 | T8 | psp | Sulfotransferase 4A1 (ST4A1) (EC 2.8.2.-) (Brain sulfotransferase-like protein) (hBR-STL) (hBR-STL-1) (Nervous system sulfotransferase) (NST) | Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS. {ECO:0000269|PubMed:17425406}. |
Q9BR77 | CCDC77 | T8 | ochoa | Coiled-coil domain-containing protein 77 | None |
Q9BRA2 | TXNDC17 | S8 | ochoa | Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein) (TRP14) (Protein 42-9-9) (Thioredoxin-like protein 5) | Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide. {ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}. |
Q9BRR8 | GPATCH1 | S8 | ochoa | G patch domain-containing protein 1 (Evolutionarily conserved G-patch domain-containing protein) | None |
Q9BRZ2 | TRIM56 | S9 | ochoa | E3 ubiquitin-protein ligase TRIM56 (EC 2.3.2.27) (RING finger protein 109) (Tripartite motif-containing protein 56) | E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 (PubMed:21289118, PubMed:29426904). In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (By similarity). Also mediate monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904). Promotes also TNFalpha-induced NF-kappa-B signaling by mediating 'Lys-63'-linked ubiquitination TAK1, leading to enhanced interaction between TAK1 and CHUK/IKKalpha (PubMed:35952808). Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (PubMed:22948160). Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus (PubMed:22948160). Acts as a restriction factor of Zika virus through direct interaction with the viral RNA via its C-terminal region (PubMed:31251739). {ECO:0000250|UniProtKB:Q80VI1, ECO:0000269|PubMed:21289118, ECO:0000269|PubMed:22948160, ECO:0000269|PubMed:29426904, ECO:0000269|PubMed:31251739, ECO:0000269|PubMed:35952808}. |
Q9BSJ8 | ESYT1 | S10 | ochoa | Extended synaptotagmin-1 (E-Syt1) (Membrane-bound C2 domain-containing protein) | Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels (PubMed:23791178, PubMed:24183667). Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane (PubMed:24183667). Acts as an inhibitor of ADGRD1 G-protein-coupled receptor activity in absence of cytosolic calcium (PubMed:38758649). Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). {ECO:0000250|UniProtKB:A0FGR8, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24183667, ECO:0000269|PubMed:38758649}. |
Q9BTE7 | DCUN1D5 | S9 | ochoa | DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) | Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs) (PubMed:19617556, PubMed:23201271, PubMed:26906416). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (PubMed:23098533, PubMed:24192928). {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23098533, ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:26906416}. |
Q9BTU6 | PI4K2A | S9 | ochoa|psp | Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-alpha) | Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678, ECO:0000305}. |
Q9BTV4 | TMEM43 | T8 | ochoa | Transmembrane protein 43 (Protein LUMA) | May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination (PubMed:34050020). {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34050020}. |
Q9BTV4 | TMEM43 | S9 | ochoa | Transmembrane protein 43 (Protein LUMA) | May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination (PubMed:34050020). {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34050020}. |
Q9BUL5 | PHF23 | S9 | 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}. |
Q9BUP3 | HTATIP2 | S8 | ochoa | Protein HTATIP2 (30 kDa HIV-1 TAT-interacting protein) (HIV-1 TAT-interactive protein 2) | Represses translation by preventing reactivation of elongation factor eEF1A (By similarity). May also inhibit nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors (PubMed:15282309). Has additionally been proposed to act as a redox sensor involved in cellular oxidative stress surveillance (PubMed:18519672). {ECO:0000250|UniProtKB:B0BNF8, ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:18519672}. |
Q9BVC4 | MLST8 | S10 | ochoa | Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Gable) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8) | Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073, PubMed:28489822). mTORC1 is activated in response to growth factors or amino acids (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In response to nutrients, 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:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). 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:24403073). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:24403073). Within mTORC1, MLST8 interacts directly with MTOR and enhances its kinase activity (PubMed:12718876). In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity (PubMed:12718876). As part of the mTORC2 complex, transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15467718, PubMed:35926713). mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive (PubMed:15467718, 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:15467718, PubMed:35926713). mTORC2 functions 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). 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:15467718). mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:15467718). mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657' (PubMed:15467718). Within mTORC2, MLST8 acts as a bridge between MAPKAP1/SIN1 and MTOR (PubMed:31085701). {ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:24403073, ECO:0000269|PubMed:28489822, ECO:0000269|PubMed:31085701, ECO:0000269|PubMed:35926713}. |
Q9BVJ6 | UTP14A | S9 | ochoa | U3 small nucleolar RNA-associated protein 14 homolog A (Antigen NY-CO-16) (Serologically defined colon cancer antigen 16) | May be required for ribosome biogenesis. {ECO:0000250}. |
Q9BW27 | NUP85 | T9 | ochoa | Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (FROUNT) (Nucleoporin Nup75) (Nucleoporin Nup85) (Pericentrin-1) | Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (PubMed:12718872). As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus (PubMed:12718872). The Nup107-160 complex seems to be required for spindle assembly during mitosis (PubMed:16807356). NUP85 is required for membrane clustering of CCL2-activated CCR2 (PubMed:15995708). Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade (PubMed:15995708). Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356, ECO:0000269|PubMed:30179222}. |
Q9BWH2 | FUNDC2 | S10 | ochoa | FUN14 domain-containing protein 2 (Cervical cancer proto-oncogene 3 protein) (HCC-3) (Hepatitis C virus core-binding protein 6) | Binds directly and specifically 1,2-Diacyl-sn-glycero-3-phospho-(1'-myo-inositol-3',4',5'-bisphosphate) (PIP3) leading to the recruitment of PIP3 to mitochondria and may play a role in the regulation of the platelet activation via AKT/GSK3B/cGMP signaling pathways (PubMed:29786068). May act as transcription factor that regulates SREBP1 (isoform SREBP-1C) expression in order to modulate triglyceride (TG) homeostasis in hepatocytes (PubMed:25855506, PubMed:29187281). {ECO:0000269|PubMed:25855506, ECO:0000269|PubMed:29187281, ECO:0000269|PubMed:29786068}. |
Q9BWJ5 | SF3B5 | S9 | ochoa | Splicing factor 3B subunit 5 (SF3b5) (Pre-mRNA-splicing factor SF3b 10 kDa subunit) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:28781166, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B4 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34822310}. |
Q9BWN1 | PRR14 | S8 | ochoa | Proline-rich protein 14 | Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (PubMed:24209742). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (PubMed:24209742). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (PubMed:27041574). {ECO:0000269|PubMed:24209742, ECO:0000269|PubMed:25906157, ECO:0000269|PubMed:27041574}. |
Q9BWQ6 | YIPF2 | T8 | ochoa | Protein YIPF2 (YIP1 family member 2) | None |
Q9BXH1 | BBC3 | S10 | psp | Bcl-2-binding component 3, isoforms 1/2 (JFY-1) (p53 up-regulated modulator of apoptosis) | Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (PubMed:11463391, PubMed:23340338). Promotes partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53, releasing the bound p53/TP53 to induce apoptosis (PubMed:23340338). Regulates ER stress-induced neuronal apoptosis (By similarity). {ECO:0000250|UniProtKB:Q99ML1, ECO:0000269|PubMed:11463391, ECO:0000269|PubMed:23340338}. |
Q9BXR0 | QTRT1 | S9 | ochoa | Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC 2.4.2.64) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) | Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023, PubMed:20354154, PubMed:34009357, PubMed:34241577). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity). Modification of cytoplasmic tRNAs with queuosine controls the elongation speed of cognate codons, thereby ensuring the correct folding of nascent proteins to maintain proteome integrity (PubMed:30093495). {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:11255023, ECO:0000269|PubMed:20354154, ECO:0000269|PubMed:30093495, ECO:0000269|PubMed:34009357, ECO:0000269|PubMed:34241577}. |
Q9BXW9 | FANCD2 | S8 | psp | Fanconi anemia group D2 protein (Protein FACD2) | Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching. {ECO:0000250|UniProtKB:Q68Y81, ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12239151, ECO:0000269|PubMed:14517836, ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15377654, ECO:0000269|PubMed:15454491, ECO:0000269|PubMed:15650050, ECO:0000269|PubMed:15661754, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:19465921, ECO:0000269|PubMed:30335751, ECO:0000269|PubMed:36385258}. |
Q9BZ29 | DOCK9 | S10 | ochoa | Dedicator of cytokinesis protein 9 (Cdc42 guanine nucleotide exchange factor zizimin-1) (Zizimin-1) | Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. {ECO:0000269|PubMed:12172552, ECO:0000269|PubMed:19745154}. |
Q9BZX2 | UCK2 | T8 | ochoa | Uridine-cytidine kinase 2 (UCK 2) (EC 2.7.1.48) (Cytidine monophosphokinase 2) (Testis-specific protein TSA903) (Uridine monophosphokinase 2) | Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate (PubMed:11306702, PubMed:11494055). Does not phosphorylate deoxyribonucleosides or purine ribonucleosides (PubMed:11306702). Can use ATP or GTP as a phosphate donor (PubMed:11306702). Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine (PubMed:11306702). {ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055}. |
Q9C004 | SPRY4 | S8 | ochoa | Protein sprouty homolog 4 (Spry-4) | Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras (PubMed:12027893). Probably impairs the formation of GTP-Ras (PubMed:12027893). Inhibits Ras-independent, but not Ras-dependent, activation of RAF1 (PubMed:12717443). Represses integrin-mediated cell spreading via inhibition of TESK1-mediated phosphorylation of cofilin (PubMed:15584898). {ECO:0000269|PubMed:12027893, ECO:0000269|PubMed:12717443, ECO:0000269|PubMed:15584898}. |
Q9C040 | TRIM2 | S10 | ochoa | Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING finger protein 86) (RING-type E3 ubiquitin transferase TRIM2) | UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. Plays a role in antiviral immunity and limits New World arenavirus infection independently of its ubiquitin ligase activity (PubMed:24068738). {ECO:0000250|UniProtKB:Q9ESN6, ECO:0000269|PubMed:24068738}. |
Q9C086 | INO80B | S9 | ochoa | INO80 complex subunit B (High mobility group AT-hook 1-like 4) (IES2 homolog) (hIes2) (PAP-1-associated protein 1) (PAPA-1) (Zinc finger HIT domain-containing protein 4) | Induces growth and cell cycle arrests at the G1 phase of the cell cycle. {ECO:0000269|PubMed:15556297}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000269|PubMed:15556297}. |
Q9C0C2 | TNKS1BP1 | S10 | ochoa | 182 kDa tankyrase-1-binding protein | None |
Q9GZP1 | NRSN2 | S10 | ochoa | Neurensin-2 | May play a role in maintenance and/or transport of vesicles. |
Q9GZU1 | MCOLN1 | S10 | ochoa | Mucolipin-1 (ML1) (MG-2) (Mucolipidin) (Transient receptor potential channel mucolipin 1) (TRPML1) | Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis (PubMed:11013137, PubMed:12459486, PubMed:14749347, PubMed:15336987, PubMed:18794901, PubMed:25720963, PubMed:27623384, PubMed:29019983). Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (PubMed:25720963, PubMed:29019983). Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy (PubMed:11013137, PubMed:12459486, PubMed:14749347, PubMed:15336987, PubMed:25720963, PubMed:27623384, PubMed:29019983). Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion (By similarity). Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events (PubMed:16978393). By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels (PubMed:25720963, PubMed:25733853, PubMed:27787197). Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy (PubMed:27357649). Also functions as a Fe(2+) permeable channel in late endosomes and lysosomes (PubMed:18794901). Also permeable to Mg(2+), Na(+). K(+) and Cs(+) (By similarity). Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 (PubMed:25130899) In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (By similarity). {ECO:0000250|UniProtKB:Q99J21, ECO:0000269|PubMed:12459486, ECO:0000269|PubMed:14749347, ECO:0000269|PubMed:15336987, ECO:0000269|PubMed:16978393, ECO:0000269|PubMed:18794901, ECO:0000269|PubMed:25130899, ECO:0000269|PubMed:25720963, ECO:0000269|PubMed:25733853, ECO:0000269|PubMed:27357649, ECO:0000269|PubMed:27623384, ECO:0000269|PubMed:27787197, ECO:0000269|PubMed:29019983, ECO:0000305|PubMed:11013137}.; FUNCTION: May contribute to cellular lipase activity within the late endosomal pathway or at the cell surface which may be involved in processes of membrane reshaping and vesiculation, especially the growth of tubular structures. However, it is not known, whether it conveys the enzymatic activity directly, or merely facilitates the activity of an associated phospholipase. {ECO:0000305|PubMed:21256127}. |
Q9H0S4 | DDX47 | S9 | ochoa | Probable ATP-dependent RNA helicase DDX47 (EC 3.6.4.13) (DEAD box protein 47) | Required for efficient ribosome biogenesis (By similarity). May have a role in mRNA splicing (PubMed:16963496). Involved in apoptosis (PubMed:15977068). {ECO:0000250|UniProtKB:Q9VIF6, ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}. |
Q9H2D1 | SLC25A32 | S9 | ochoa | Solute carrier family 25 member 32 (Mitochondrial FAD transporter) | Facilitates flavin adenine dinucleotide (FAD) translocation across the mitochondrial inner membrane into the mitochondrial matrix where it acts as a redox cofactor to assist flavoenzyme activities in fundamental metabolic processes including fatty acid beta-oxidation, amino acid and choline metabolism as well as mitochondrial electron transportation. In particular, provides FAD to DLD dehydrogenase of the glycine cleavage system, part of mitochondrial one-carbon metabolic pathway involved in neural tube closure in early embryogenesis. {ECO:0000269|PubMed:16165386, ECO:0000269|PubMed:29666258, ECO:0000269|PubMed:35727412}. |
Q9H3M7 | TXNIP | S9 | ochoa | Thioredoxin-interacting protein (Thioredoxin-binding protein 2) (Vitamin D3 up-regulated protein 1) | May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability (PubMed:17603038). Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm (By similarity). Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest (PubMed:12821938). Required for the maturation of natural killer cells (By similarity). Acts as a suppressor of tumor cell growth (PubMed:18541147). Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1) (PubMed:21460850). {ECO:0000250|UniProtKB:Q8BG60, ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:21460850}. |
Q9H3Q1 | CDC42EP4 | S10 | ochoa | Cdc42 effector protein 4 (Binder of Rho GTPases 4) | Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts. |
Q9H3R0 | KDM4C | S8 | ochoa | Lysine-specific demethylase 4C (EC 1.14.11.66) (Gene amplified in squamous cell carcinoma 1 protein) (GASC-1 protein) (JmjC domain-containing histone demethylation protein 3C) (Jumonji domain-containing protein 2C) ([histone H3]-trimethyl-L-lysine(9) demethylase 4C) | Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:28262558}. |
Q9H3U1 | UNC45A | T8 | ochoa | Protein unc-45 homolog A (Unc-45A) (GCUNC-45) (Smooth muscle cell-associated protein 1) (SMAP-1) | Acts as a co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000269|PubMed:12119110, ECO:0000269|PubMed:16478993, ECO:0000305}. |
Q9H3Y8 | PPDPF | S9 | ochoa | Pancreatic progenitor cell differentiation and proliferation factor (Exocrine differentiation and proliferation factor) | Probable regulator of exocrine pancreas development. {ECO:0000250}. |
Q9H3Z4 | DNAJC5 | S8 | ochoa | DnaJ homolog subfamily C member 5 (Ceroid-lipofuscinosis neuronal protein 4) (Cysteine string protein) (CSP) | Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250|UniProtKB:P60904, ECO:0000250|UniProtKB:Q29455}. |
Q9H3Z4 | DNAJC5 | S10 | ochoa|psp | DnaJ homolog subfamily C member 5 (Ceroid-lipofuscinosis neuronal protein 4) (Cysteine string protein) (CSP) | Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250|UniProtKB:P60904, ECO:0000250|UniProtKB:Q29455}. |
Q9H4A3 | WNK1 | S10 | 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}. |
Q9H4A4 | RNPEP | S10 | 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}. |
Q9H4A6 | GOLPH3 | S8 | ochoa | Golgi phosphoprotein 3 (Coat protein GPP34) (Mitochondrial DNA absence factor) (MIDAS) | Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may 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. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis. {ECO:0000269|PubMed:16263763, ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:22745132, ECO:0000269|PubMed:23027862, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23500462}. |
Q9H4A6 | GOLPH3 | S9 | ochoa | Golgi phosphoprotein 3 (Coat protein GPP34) (Mitochondrial DNA absence factor) (MIDAS) | Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may 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. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis. {ECO:0000269|PubMed:16263763, ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:22745132, ECO:0000269|PubMed:23027862, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23500462}. |
Q9H4I2 | ZHX3 | T8 | ochoa | Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) | Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}. |
Q9H4M7 | PLEKHA4 | S8 | ochoa | Pleckstrin homology domain-containing family A member 4 (PH domain-containing family A member 4) (Phosphoinositol 3-phosphate-binding protein 1) (PEPP-1) | Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides. {ECO:0000269|PubMed:11001876}. |
Q9H4M7 | PLEKHA4 | S9 | ochoa | Pleckstrin homology domain-containing family A member 4 (PH domain-containing family A member 4) (Phosphoinositol 3-phosphate-binding protein 1) (PEPP-1) | Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides. {ECO:0000269|PubMed:11001876}. |
Q9H4Z3 | PCIF1 | S8 | ochoa | mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase (EC 2.1.1.62) (Cap-specific adenosine methyltransferase) (CAPAM) (hCAPAM) (Phosphorylated CTD-interacting factor 1) (hPCIF1) (Protein phosphatase 1 regulatory subunit 121) | Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178, PubMed:30487554, PubMed:31279658, PubMed:31279659, PubMed:33428944). Recruited to the early elongation complex of RNA polymerase II (RNAPII) via interaction with POLR2A and mediates formation of m6A(m) co-transcriptionally (PubMed:30467178). {ECO:0000269|PubMed:30467178, ECO:0000269|PubMed:30487554, ECO:0000269|PubMed:31279658, ECO:0000269|PubMed:31279659, ECO:0000269|PubMed:33428944}. |
Q9H6D7 | HAUS4 | S8 | ochoa | HAUS augmin-like complex subunit 4 | Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. |
Q9H6Q3 | SLA2 | S10 | ochoa | Src-like-adapter 2 (Modulator of antigen receptor signaling) (MARS) (Src-like adapter protein 2) (SLAP-2) | Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. {ECO:0000269|PubMed:11696592}. |
Q9H6S0 | YTHDC2 | S8 | ochoa | 3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (YTH domain-containing protein 2) (hYTHDC2) | 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity). {ECO:0000250|UniProtKB:B2RR83, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29970596}. |
Q9H6S3 | EPS8L2 | S8 | 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}. |
Q9H813 | PACC1 | T8 | ochoa | Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206) | Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925, ECO:0000269|PubMed:31318332}. |
Q9H813 | PACC1 | S9 | ochoa | Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206) | Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925, ECO:0000269|PubMed:31318332}. |
Q9H8E8 | KAT14 | S8 | ochoa | Cysteine-rich protein 2-binding protein (CSRP2-binding protein) (ADA2A-containing complex subunit 2) (ATAC2) (CRP2-binding partner) (CRP2BP) (Lysine acetyltransferase 14) | Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle. {ECO:0000269|PubMed:19103755}. |
Q9H8E8 | KAT14 | S9 | ochoa | Cysteine-rich protein 2-binding protein (CSRP2-binding protein) (ADA2A-containing complex subunit 2) (ATAC2) (CRP2-binding partner) (CRP2BP) (Lysine acetyltransferase 14) | Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle. {ECO:0000269|PubMed:19103755}. |
Q9H8S9 | MOB1A | S9 | ochoa|psp | MOB kinase activator 1A (Mob1 alpha) (Mob1A) (Mob1 homolog 1B) (Mps one binder kinase activator-like 1B) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 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. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}. |
Q9H8S9 | MOB1A | S10 | ochoa | MOB kinase activator 1A (Mob1 alpha) (Mob1A) (Mob1 homolog 1B) (Mps one binder kinase activator-like 1B) | Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 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. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38. {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}. |
Q9H8V3 | ECT2 | S9 | 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}. |
Q9HAJ7 | SAP30L | S10 | ochoa | Histone deacetylase complex subunit SAP30L (HCV non-structural protein 4A-transactivated protein 2) (Sin3 corepressor complex subunit SAP30L) (Sin3-associated protein p30-like) | [Isoform 1]: Functions as a transcription repressor, probably via its interaction with histone deacetylase complexes (PubMed:16820529, PubMed:18070604). Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus (PubMed:16820529). Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import (PubMed:19015240, PubMed:26609676). {ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:18070604, ECO:0000269|PubMed:19015240, ECO:0000269|PubMed:26609676}.; FUNCTION: [Isoform 2]: Functions as a transcription repressor; isoform 2 has lower transcription repressor activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:18070604}.; FUNCTION: [Isoform 3]: Functions as a transcription repressor; its activity is marginally lower than that of isoform 1. {ECO:0000269|PubMed:18070604}. |
Q9HAP2 | MLXIP | S9 | ochoa | MLX-interacting protein (Class E basic helix-loop-helix protein 36) (bHLHe36) (Transcriptional activator MondoA) | Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000250|UniProtKB:Q2VPU4, ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}. |
Q9HAS0 | C17orf75 | S8 | ochoa | Protein Njmu-R1 | As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1 (PubMed:29426865). May have a role in spermatogenesis. {ECO:0000269|PubMed:29426865}. |
Q9HCD5 | NCOA5 | S9 | ochoa | Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA) | Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). {ECO:0000269|PubMed:15073177}. |
Q9HCS7 | XAB2 | S8 | ochoa | Pre-mRNA-splicing factor SYF1 (Protein HCNP) (XPA-binding protein 2) | Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770). Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing (PubMed:10944529, PubMed:17981804). {ECO:0000269|PubMed:10944529, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17981804, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. |
Q9NQC1 | JADE2 | S9 | ochoa | E3 ubiquitin-protein ligase Jade-2 (EC 2.3.2.27) (Jade family PHD finger protein 2) (PHD finger protein 15) | Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity (PubMed:16387653). Acts as an E3 ubiquitin-protein ligase mediating the ubiquitination and subsequent proteasomal degradation of target protein histone demethylase KDM1A (PubMed:25018020). Also acts as a ubiquitin ligase E3 toward itself. Positive regulator of neurogenesis (By similarity). {ECO:0000250|UniProtKB:Q6ZQF7, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:25018020}. |
Q9NR19 | ACSS2 | S10 | ochoa | Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acetyl-CoA synthetase 1) (AceCS1) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme) (Propionate--CoA ligase) (EC 6.2.1.17) | Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:10843999, PubMed:28003429, PubMed:28552616). Acetate is the preferred substrate (PubMed:10843999, PubMed:28003429). Can also utilize propionate with a much lower affinity (By similarity). Nuclear ACSS2 promotes glucose deprivation-induced lysosomal biogenesis and autophagy, tumor cell survival and brain tumorigenesis (PubMed:28552616). Glucose deprivation results in AMPK-mediated phosphorylation of ACSS2 leading to its translocation to the nucleus where it binds to TFEB and locally produces acetyl-CoA for histone acetylation in the promoter regions of TFEB target genes thereby activating their transcription (PubMed:28552616). The regulation of genes associated with autophagy and lysosomal activity through ACSS2 is important for brain tumorigenesis and tumor survival (PubMed:28552616). Acts as a chromatin-bound transcriptional coactivator that up-regulates histone acetylation and expression of neuronal genes (By similarity). Can be recruited to the loci of memory-related neuronal genes to maintain a local acetyl-CoA pool, providing the substrate for histone acetylation and promoting the expression of specific genes, which is essential for maintaining long-term spatial memory (By similarity). {ECO:0000250|UniProtKB:Q9QXG4, ECO:0000269|PubMed:10843999, ECO:0000269|PubMed:28003429, ECO:0000269|PubMed:28552616}. |
Q9NR28 | DIABLO | S9 | psp | Diablo IAP-binding mitochondrial protein (Diablo homolog, mitochondrial) (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspases) (SMAC) [Cleaved into: Diablo IAP-binding mitochondrial protein, cleaved form] | Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/BRUCE by inhibiting its binding to caspases (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106). {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758105, ECO:0000269|PubMed:36758106}.; FUNCTION: [Isoform 3]: Attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. {ECO:0000269|PubMed:14523016}.; FUNCTION: [Isoform 1]: Defective in the capacity to down-regulate the XIAP/BIRC4 abundance. {ECO:0000269|PubMed:14523016}. |
Q9NR33 | POLE4 | S9 | ochoa | DNA polymerase epsilon subunit 4 (DNA polymerase II subunit 4) (DNA polymerase epsilon subunit p12) | Accessory component of the DNA polymerase epsilon complex (PubMed:10801849). Participates in DNA repair and in chromosomal DNA replication (By similarity). {ECO:0000250|UniProtKB:P27344, ECO:0000269|PubMed:10801849}. |
Q9NR46 | SH3GLB2 | S10 | ochoa | Endophilin-B2 (SH3 domain-containing GRB2-like protein B2) | None |
Q9NRA8 | EIF4ENIF1 | T9 | 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}. |
Q9NRY5 | FAM114A2 | T9 | ochoa | Protein FAM114A2 | None |
Q9NS56 | TOPORS | S9 | ochoa | E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3) | Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage-induced cell death through IKBKE sumoylation. {ECO:0000269|PubMed:15247280, ECO:0000269|PubMed:15735665, ECO:0000269|PubMed:16122737, ECO:0000269|PubMed:17803295, ECO:0000269|PubMed:18077445, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:20188669}. |
Q9NSA3 | CTNNBIP1 | S10 | ochoa | Beta-catenin-interacting protein 1 (Inhibitor of beta-catenin and Tcf-4) | Prevents the interaction between CTNNB1 and TCF family members, and acts as a negative regulator of the Wnt signaling pathway. {ECO:0000269|PubMed:12408824}. |
Q9NSY1 | BMP2K | S10 | ochoa | BMP-2-inducible protein kinase (BIKe) (EC 2.7.11.1) | May be involved in osteoblast differentiation. {ECO:0000250|UniProtKB:Q91Z96}. |
Q9NUJ3 | TCP11L1 | S8 | ochoa | T-complex protein 11-like protein 1 | None |
Q9NVA2 | SEPTIN11 | S9 | ochoa | Septin-11 | Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy. {ECO:0000250, ECO:0000269|PubMed:15196925, ECO:0000269|PubMed:19234302, ECO:0000305}. |
Q9NVC6 | MED17 | S10 | ochoa | Mediator of RNA polymerase II transcription subunit 17 (Activator-recruited cofactor 77 kDa component) (ARC77) (Cofactor required for Sp1 transcriptional activation subunit 6) (CRSP complex subunit 6) (Mediator complex subunit 17) (Thyroid hormone receptor-associated protein complex 80 kDa component) (Trap80) (Transcriptional coactivator CRSP77) (Vitamin D3 receptor-interacting protein complex 80 kDa component) (DRIP80) | 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. {ECO:0000269|PubMed:16595664}. |
Q9NVD7 | PARVA | S8 | ochoa|psp | Alpha-parvin (Actopaxin) (CH-ILKBP) (Calponin-like integrin-linked kinase-binding protein) (Matrix-remodeling-associated protein 2) | Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration. Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration (PubMed:30367047). {ECO:0000250, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:30367047}. |
Q9NVD7 | PARVA | S10 | ochoa | Alpha-parvin (Actopaxin) (CH-ILKBP) (Calponin-like integrin-linked kinase-binding protein) (Matrix-remodeling-associated protein 2) | Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration. Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration (PubMed:30367047). {ECO:0000250, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:30367047}. |
Q9NVT9 | ARMC1 | S9 | ochoa | Armadillo repeat-containing protein 1 | In association with mitochondrial contact site and cristae organizing system (MICOS) complex components and mitochondrial outer membrane sorting assembly machinery (SAM) complex components may regulate mitochondrial dynamics playing a role in determining mitochondrial length, distribution and motility. {ECO:0000269|PubMed:31644573}. |
Q9NWQ4 | GPATCH2L | S10 | ochoa | G patch domain-containing protein 2-like | None |
Q9NWV8 | BABAM1 | S8 | ochoa | BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) | Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}. |
Q9NWZ3 | IRAK4 | S8 | psp | Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64) | Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. {ECO:0000269|PubMed:11960013, ECO:0000269|PubMed:12538665, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:17217339, ECO:0000269|PubMed:17337443, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509, ECO:0000269|PubMed:24316379}. |
Q9NX09 | DDIT4 | S10 | ochoa | DNA damage-inducible transcript 4 protein (HIF-1 responsive protein RTP801) (Protein regulated in development and DNA damage response 1) (REDD-1) | Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes (By similarity). Required for mTORC1-mediated defense against viral protein synthesis and virus replication (By similarity). Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. {ECO:0000250, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15632201, ECO:0000269|PubMed:15988001, ECO:0000269|PubMed:17005863, ECO:0000269|PubMed:17379067, ECO:0000269|PubMed:19557001, ECO:0000269|PubMed:20166753, ECO:0000269|PubMed:21460850}. |
Q9NX76 | CMTM6 | S8 | ochoa | CKLF-like MARVEL transmembrane domain-containing protein 6 (Chemokine-like factor superfamily member 6) | Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its STUB1-mediated ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. {ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417}. |
Q9NXG0 | CNTLN | S8 | ochoa | Centlein (Centrosomal protein) | Required for centrosome cohesion and recruitment of CEP68 to centrosomes. {ECO:0000269|PubMed:24554434}. |
Q9NXH3 | PPP1R14D | S8 | ochoa | Protein phosphatase 1 regulatory subunit 14D (Gastrointestinal and brain-specific PP1-inhibitory protein 1) (GBPI-1) | Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000269|PubMed:12974676}. |
Q9NXR1 | NDE1 | S9 | 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}. |
Q9NXR1 | NDE1 | S10 | 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}. |
Q9NXV2 | KCTD5 | S10 | ochoa | BTB/POZ domain-containing protein KCTD5 | Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex (PubMed:18573101). Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4 (PubMed:19361449). {ECO:0000269|PubMed:18573101, ECO:0000269|PubMed:19361449}. |
Q9NXW9 | ALKBH4 | T8 | ochoa | Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (Alkylated DNA repair protein alkB homolog 4) (DNA N6-methyl adenine demethylase ALKBH4) (EC 1.14.11.51) (Lysine-specific demethylase ALKBH4) (EC 1.14.11.-) | Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes (PubMed:23673617). Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617). In addition to proteins, also demethylates DNA: specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing (By similarity). {ECO:0000250|UniProtKB:Q9D8F1, ECO:0000269|PubMed:23673617}. |
Q9NYA4 | MTMR4 | S8 | ochoa | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4 (EC 3.1.3.95) (FYVE domain-containing dual specificity protein phosphatase 2) (FYVE-DSP2) (Myotubularin-related protein 4) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Zinc finger FYVE domain-containing protein 11) | Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:11302699, PubMed:16787938, PubMed:20736309, PubMed:27625994, PubMed:29962048, PubMed:30944173). Decreases the levels of phosphatidylinositol 3-phosphate, a phospholipid found in cell membranes where it acts as key regulator of both cell signaling and intracellular membrane traffic, in a subset of endosomal membranes to negatively regulate both endocytic recycling and trafficking and/or maturation of endosomes toward lysosomes (PubMed:16787938, PubMed:20736309, PubMed:29962048). Through phosphatidylinositol 3-phosphate turnover in phagosome membranes regulates phagocytosis and phagosome maturation (PubMed:31543504). By decreasing phosphatidylinositol 3-monophosphate (PI3P) levels in immune cells it can also regulate the innate immune response (PubMed:30944173). Beside its lipid phosphatase activity, can also function as a molecular adapter to regulate midbody abscission during mitotic cytokinesis (PubMed:25659891). Can also negatively regulate TGF-beta and BMP signaling through Smad proteins dephosphorylation and retention in endosomes (PubMed:20061380, PubMed:23150675). {ECO:0000269|PubMed:11302699, ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:20061380, ECO:0000269|PubMed:20736309, ECO:0000269|PubMed:23150675, ECO:0000269|PubMed:25659891, ECO:0000269|PubMed:27625994, ECO:0000269|PubMed:29962048, ECO:0000269|PubMed:30944173, ECO:0000269|PubMed:31543504}. |
Q9NYD6 | HOXC10 | T8 | ochoa | Homeobox protein Hox-C10 (Homeobox protein Hox-3I) | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9NYM9 | BET1L | S9 | ochoa | BET1-like protein (Golgi SNARE with a size of 15 kDa) (GOS-15) (GS15) (Vesicle transport protein GOS15) | Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}. |
Q9NYP3 | DONSON | S9 | ochoa | Protein downstream neighbor of Son (B17) | Replisome component that maintains genome stability by protecting stalled or damaged replication forks. After the induction of replication stress, required for the stabilization of stalled replication forks, the efficient activation of the intra-S-phase and G/2M cell-cycle checkpoints and the maintenance of genome stability. {ECO:0000269|PubMed:28191891}. |
Q9NZL9 | MAT2B | S9 | ochoa | Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta) (MAT II beta) (Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase) | Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine (PubMed:10644686, PubMed:23189196, PubMed:25075345). Can bind NADP (in vitro) (PubMed:23189196, PubMed:23425511). {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:23189196, ECO:0000269|PubMed:23425511, ECO:0000269|PubMed:25075345}. |
Q9NZT2 | OGFR | S8 | ochoa | Opioid growth factor receptor (OGFr) (Protein 7-60) (Zeta-type opioid receptor) | Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation. |
Q9NZT2 | OGFR | T9 | ochoa | Opioid growth factor receptor (OGFr) (Protein 7-60) (Zeta-type opioid receptor) | Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation. |
Q9P0K8 | FOXJ2 | S8 | ochoa | Forkhead box protein J2 (Fork head homologous X) | [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation (PubMed:10777590, PubMed:10966786). Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity). {ECO:0000250|UniProtKB:Q9ES18, ECO:0000269|PubMed:10777590, ECO:0000269|PubMed:10966786}.; FUNCTION: [Isoform FOXJ2.S]: Transcriptional activator. {ECO:0000269|PubMed:10966786}. |
Q9P1Q0 | VPS54 | S8 | ochoa | Vacuolar protein sorting-associated protein 54 (Hepatocellular carcinoma protein 8) (Tumor antigen HOM-HCC-8) (Tumor antigen SLP-8p) | 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 the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:18367545). Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling (PubMed:25799061). {ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}. |
Q9P1V8 | SAMD15 | S10 | ochoa | Sterile alpha motif domain-containing protein 15 (SAM domain-containing protein 15) | None |
Q9P253 | VPS18 | Y8 | ochoa | Vacuolar protein sorting-associated protein 18 homolog (hVPS18) | Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in dendrite development of Pukinje cells (By similarity). {ECO:0000250|UniProtKB:Q8R307, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25783203}. |
Q9P265 | DIP2B | S9 | ochoa | Disco-interacting protein 2 homolog B (DIP2 homolog B) | Negatively regulates axonal outgrowth and is essential for normal synaptic transmission. Not required for regulation of axon polarity. Promotes acetylation of alpha-tubulin. {ECO:0000250|UniProtKB:Q3UH60}. |
Q9P273 | TENM3 | Y9 | ochoa | Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3) | Involved in neural development by regulating the establishment of proper connectivity within the nervous system. Acts in both pre- and postsynaptic neurons in the hippocampus to control the assembly of a precise topographic projection: required in both CA1 and subicular neurons for the precise targeting of proximal CA1 axons to distal subiculum, probably by promoting homophilic cell adhesion. Required for proper dendrite morphogenesis and axon targeting in the vertebrate visual system, thereby playing a key role in the development of the visual pathway. Regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC). May also be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes. {ECO:0000250|UniProtKB:Q9WTS6}. |
Q9P2D7 | DNAH1 | Y9 | ochoa | Dynein axonemal heavy chain 1 (Axonemal beta dynein heavy chain 1) (Ciliary dynein heavy chain 1) (Heat shock regulated protein 1) (HSRF-1) (hDHC7) | Force generating protein of cilia required for sperm flagellum motility. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (PubMed:24360805). {ECO:0000250|UniProtKB:Q91XQ0, ECO:0000269|PubMed:24360805}. |
Q9P2Y4 | ZNF219 | S10 | ochoa | Zinc finger protein 219 | Transcriptional regulator (PubMed:14621294, PubMed:19549071). Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' (PubMed:14621294). Binds to the HMGN1 promoter and may repress HMGN1 expression (PubMed:14621294). Regulates SNCA expression in primary cortical neurons (PubMed:19549071). Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with SOX9 (By similarity). Plays a role in chondrocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q6IQX8, ECO:0000269|PubMed:14621294, ECO:0000269|PubMed:19549071}. |
Q9UBI6 | GNG12 | T8 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
Q9UBU7 | DBF4 | S10 | ochoa | Protein DBF4 homolog A (Activator of S phase kinase) (Chiffon homolog A) (DBF4-type zinc finger-containing protein 1) | Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle. {ECO:0000269|PubMed:10373557, ECO:0000269|PubMed:10523313, ECO:0000269|PubMed:17062569}. |
Q9UBU9 | NXF1 | S9 | ochoa | Nuclear RNA export factor 1 (Tip-associated protein) (Tip-associating protein) (mRNA export factor TAP) | Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}. |
Q9UEE5 | STK17A | S9 | ochoa | Serine/threonine-protein kinase 17A (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 1) | Acts as a positive regulator of apoptosis. Also acts as a regulator of cellular reactive oxygen species. {ECO:0000269|PubMed:21489989, ECO:0000269|PubMed:9786912}. |
Q9UH99 | SUN2 | T9 | ochoa | SUN domain-containing protein 2 (Protein unc-84 homolog B) (Rab5-interacting protein) (Rab5IP) (Sad1/unc-84 protein-like 2) | As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000250|UniProtKB:Q8BJS4, ECO:0000269|PubMed:18396275, ECO:0000305}. |
Q9UHG0 | DCDC2 | S8 | ochoa | Doublecortin domain-containing protein 2 (Protein RU2S) | Protein that plays a role in the inhibition of canonical Wnt signaling pathway (PubMed:25557784). May be involved in neuronal migration during development of the cerebral neocortex (By similarity). Involved in the control of ciliogenesis and ciliary length (PubMed:25601850, PubMed:27319779). {ECO:0000250|UniProtKB:D3ZR10, ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25601850, ECO:0000269|PubMed:27319779}. |
Q9UHG0 | DCDC2 | S9 | ochoa | Doublecortin domain-containing protein 2 (Protein RU2S) | Protein that plays a role in the inhibition of canonical Wnt signaling pathway (PubMed:25557784). May be involved in neuronal migration during development of the cerebral neocortex (By similarity). Involved in the control of ciliogenesis and ciliary length (PubMed:25601850, PubMed:27319779). {ECO:0000250|UniProtKB:D3ZR10, ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25601850, ECO:0000269|PubMed:27319779}. |
Q9UHN6 | CEMIP2 | S10 | ochoa | Cell surface hyaluronidase CEMIP2 (EC 3.2.1.35) (Cell migration-inducing hyaluronidase 2) (Transmembrane protein 2) | Cell surface hyaluronidase that mediates the initial cleavage of extracellular high-molecular-weight hyaluronan into intermediate-size hyaluronan of approximately 10-5 kDa fragments (PubMed:37527776). Very specific to hyaluronan; not able to cleave chondroitin sulfate or dermatan sulfate. Has an essential function in systemic hyaluronan catabolism and turnover and regulates cell adhesion and migration via hyaluronan degradation at focal adhesion sites (By similarity). Acts as a regulator of angiogenesis and heart morphogenesis by mediating degradation of extracellular hyaluronan, thereby regulating VEGF signaling (By similarity). {ECO:0000250|UniProtKB:A3KPQ7, ECO:0000250|UniProtKB:Q5FWI3, ECO:0000269|PubMed:37527776}. |
Q9UHR5 | SAP30BP | S9 | ochoa | SAP30-binding protein (Transcriptional regulator protein HCNGP) | Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3 (PubMed:21221920). May be involved in the regulation of beta-2-microglobulin genes (By similarity). {ECO:0000250|UniProtKB:Q02614, ECO:0000269|PubMed:21221920}.; FUNCTION: (Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC. {ECO:0000269|PubMed:21221920}. |
Q9UHR5 | SAP30BP | S10 | ochoa | SAP30-binding protein (Transcriptional regulator protein HCNGP) | Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3 (PubMed:21221920). May be involved in the regulation of beta-2-microglobulin genes (By similarity). {ECO:0000250|UniProtKB:Q02614, ECO:0000269|PubMed:21221920}.; FUNCTION: (Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC. {ECO:0000269|PubMed:21221920}. |
Q9UHY1 | NRBP1 | T8 | ochoa | Nuclear receptor-binding protein | Required for embryonic development (By similarity). Plays a role in intestinal epithelial cell fate and proliferation, thereby involved in the architectural development of the intestine potentially via the regulation of Wnt-responsive genes (By similarity). May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication (PubMed:15084397). {ECO:0000250|UniProtKB:Q99J45, ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397}. |
Q9UIC8 | LCMT1 | S8 | ochoa | Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein-leucine O-methyltransferase) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1) | Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. {ECO:0000269|PubMed:10600115}. |
Q9UIC8 | LCMT1 | S9 | ochoa | Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (Protein-leucine O-methyltransferase) ([Phosphatase 2A protein]-leucine-carboxy methyltransferase 1) | Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. {ECO:0000269|PubMed:10600115}. |
Q9UID3 | VPS51 | S10 | 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}. |
Q9UK41 | VPS28 | T8 | ochoa | Vacuolar protein sorting-associated protein 28 homolog (H-Vps28) (ESCRT-I complex subunit VPS28) | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. {ECO:0000269|PubMed:11916981}. |
Q9UKK9 | NUDT5 | S9 | ochoa | ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H) | Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:17052728, PubMed:19699693, PubMed:21389046). Can also hydrolyze other nucleotide sugars with low activity (PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:Q9JKX6, ECO:0000269|PubMed:10567213, ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046, ECO:0000269|PubMed:27257257}. |
Q9UKK9 | NUDT5 | S10 | ochoa | ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H) | Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:17052728, PubMed:19699693, PubMed:21389046). Can also hydrolyze other nucleotide sugars with low activity (PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity). {ECO:0000250|UniProtKB:Q9JKX6, ECO:0000269|PubMed:10567213, ECO:0000269|PubMed:10722730, ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046, ECO:0000269|PubMed:27257257}. |
Q9UKT5 | FBXO4 | S8 | ochoa | F-box only protein 4 | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10531035, PubMed:18598945, PubMed:20181953, PubMed:29142209). Promotes ubiquitination of cyclin-D1 (CCND1) and its subsequent proteasomal degradation (PubMed:18598945). However, it does not act as a major regulator of CCND1 stability during the G1/S transition (By similarity). Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 (PubMed:16275645, PubMed:20159592). Promotes ubiquitination of FXR1 following phosphorylation of FXR1 by GSK3B, leading to FXR1 degradation by the proteasome (PubMed:29142209). {ECO:0000250|UniProtKB:Q8CHQ0, ECO:0000269|PubMed:10531035, ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:29142209}. |
Q9UKY7 | CDV3 | S8 | ochoa | Protein CDV3 homolog | None |
Q9UL46 | PSME2 | S10 | ochoa | Proteasome activator complex subunit 2 (11S regulator complex subunit beta) (REG-beta) (Activator of multicatalytic protease subunit 2) (Proteasome activator 28 subunit beta) (PA28b) (PA28beta) | Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. |
Q9UL54 | TAOK2 | S9 | ochoa | Serine/threonine-protein kinase TAO2 (EC 2.7.11.1) (Kinase from chicken homolog C) (hKFC-C) (Prostate-derived sterile 20-like kinase 1) (PSK-1) (PSK1) (Prostate-derived STE20-like kinase 1) (Thousand and one amino acid protein kinase 2) | Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation. {ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:11279118, ECO:0000269|PubMed:12639963, ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:17158878, ECO:0000269|PubMed:17396146}. |
Q9ULJ1 | ODF2L | S9 | ochoa | Protein BCAP (Basal body centriole-associated protein) (Outer dense fiber protein 2-like) (ODF2-like protein) | Acts as a suppressor of ciliogenesis, specifically, the initiation of ciliogenesis. {ECO:0000269|PubMed:28775150}. |
Q9ULR5 | PAIP2B | S10 | ochoa | Polyadenylate-binding protein-interacting protein 2B (PABP-interacting protein 2B) (PAIP-2B) (Poly(A)-binding protein-interacting protein 2B) | Inhibits translation of capped and polyadenylated mRNAs by displacing PABPC1 from the poly(A) tail. {ECO:0000269|PubMed:16804161}. |
Q9UMX3 | BOK | S8 | ochoa | Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9) | [Isoform 1]: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:15102863, PubMed:20673843, PubMed:27076518). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:15102863, PubMed:27076518). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:27076518). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (By similarity). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression (PubMed:19942931). May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (PubMed:24113155). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155, ECO:0000269|PubMed:27076518}.; FUNCTION: [Isoform 2]: Pro-apoptotic molecule exerting its function through the mitochondrial pathway. {ECO:0000269|PubMed:15775999}. |
Q9UNX3 | RPL26L1 | S9 | ochoa | Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) | None |
Q9UPY5 | SLC7A11 | T9 | ochoa | Cystine/glutamate transporter (Amino acid transport system xc-) (Calcium channel blocker resistance protein CCBR1) (Solute carrier family 7 member 11) (xCT) | Heterodimer with SLC3A2, that functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:11133847, PubMed:11417227, PubMed:14722095, PubMed:15151999, PubMed:34880232, PubMed:35245456, PubMed:35352032). Provides L-cystine for the maintenance of the redox balance between extracellular L-cystine and L-cysteine and for the maintenance of the intracellular levels of glutathione that is essential for cells protection from oxidative stress (By similarity). The transport is sodium-independent, electroneutral with a stoichiometry of 1:1, and is drove by the high intracellular concentration of L-glutamate and the intracellular reduction of L-cystine (PubMed:11133847, PubMed:11417227). In addition, mediates the import of L-kynurenine leading to anti-ferroptotic signaling propagation required to maintain L-cystine and glutathione homeostasis (PubMed:35245456). Moreover, mediates N-acetyl-L-cysteine uptake into the placenta leading to subsequently down-regulation of pathways associated with oxidative stress, inflammation and apoptosis (PubMed:34120018). In vitro can also transport L-aspartate (PubMed:11417227). May participate in astrocyte and meningeal cell proliferation during development and can provide neuroprotection by promoting glutathione synthesis and delivery from non-neuronal cells such as astrocytes and meningeal cells to immature neurons (By similarity). Controls the production of pheomelanin pigment directly (By similarity). {ECO:0000250|UniProtKB:Q9WTR6, ECO:0000269|PubMed:11133847, ECO:0000269|PubMed:11417227, ECO:0000269|PubMed:14722095, ECO:0000269|PubMed:15151999, ECO:0000269|PubMed:34120018, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:35245456, ECO:0000269|PubMed:35352032}. |
Q9UQ35 | SRRM2 | T9 | 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}. |
Q9UQQ2 | SH2B3 | S9 | ochoa | SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk) | Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}. |
Q9UQQ2 | SH2B3 | S10 | ochoa | SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk) | Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}. |
Q9UQR0 | SCML2 | S9 | 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}. |
Q9Y241 | HIGD1A | S8 | ochoa | HIG1 domain family member 1A, mitochondrial (Hypoxia-inducible gene 1 protein) (RCF1 homolog A) (RCF1a) | Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}. |
Q9Y287 | ITM2B | S8 | ochoa | Integral membrane protein 2B (Immature BRI2) (imBRI2) (Protein E25B) (Transmembrane protein BRI) (Bri) [Cleaved into: BRI2, membrane form (Mature BRI2) (mBRI2); BRI2 intracellular domain (BRI2 ICD); BRI2C, soluble form; Bri23 peptide (Bri2-23) (ABri23) (C-terminal peptide) (P23 peptide)] | Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.; FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the amyloid-beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42.; FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers. |
Q9Y2I7 | PIKFYVE | S8 | ochoa | 1-phosphatidylinositol 3-phosphate 5-kinase (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (FYVE finger-containing phosphoinositide kinase) (PIKfyve) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (Serine-protein kinase PIKFYVE) (EC 2.7.11.1) | Dual specificity kinase implicated in myriad essential cellular processes such as maintenance of endomembrane homeostasis, and endocytic-vacuolar pathway, lysosomal trafficking, nuclear transport, stress- or hormone-induced signaling and cell cycle progression (PubMed:23086417). The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Sole enzyme to catalyze the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form (PtdIns(3,5)P2) (PubMed:17556371). Also catalyzes the phosphorylation of phosphatidylinositol on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 5-phosphate (PtdIns(5)P) (PubMed:22621786). Has serine-protein kinase activity and is able to autophosphorylate and transphosphorylate. Autophosphorylation inhibits its own phosphatidylinositol 3-phosphate 5-kinase activity, stimulates FIG4 lipid phosphatase activity and down-regulates lipid product formation (PubMed:33098764). Involved in key endosome operations such as fission and fusion in the course of endosomal cargo transport (PubMed:22621786). Required for the maturation of early into late endosomes, phagosomes and lysosomes (PubMed:30612035). Regulates vacuole maturation and nutrient recovery following engulfment of macromolecules, initiates the redistribution of accumulated lysosomal contents back into the endosome network (PubMed:27623384). Critical regulator of the morphology, degradative activity, and protein turnover of the endolysosomal system in macrophages and platelets (By similarity). In neutrophils, critical to perform chemotaxis, generate ROS, and undertake phagosome fusion with lysosomes (PubMed:28779020). Plays a key role in the processing and presentation of antigens by major histocompatibility complex class II (MHC class II) mediated by CTSS (PubMed:30612035). Regulates melanosome biogenesis by controlling the delivery of proteins from the endosomal compartment to the melanosome (PubMed:29584722). Essential for systemic glucose homeostasis, mediates insulin-induced signals for endosome/actin remodeling in the course of GLUT4 translocation/glucose uptake activation (By similarity). Supports microtubule-based endosome-to-trans-Golgi network cargo transport, through association with SPAG9 and RABEPK (By similarity). Mediates EGFR trafficking to the nucleus (PubMed:17909029). {ECO:0000250|UniProtKB:Q9Z1T6, ECO:0000269|PubMed:17556371, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:22621786, ECO:0000269|PubMed:27623384, ECO:0000269|PubMed:28779020, ECO:0000269|PubMed:29584722, ECO:0000269|PubMed:30612035, ECO:0000269|PubMed:33098764, ECO:0000303|PubMed:23086417}.; FUNCTION: (Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC) by endocytosis. {ECO:0000269|PubMed:32221306}. |
Q9Y2J2 | EPB41L3 | S9 | ochoa | Band 4.1-like protein 3 (4.1B) (Differentially expressed in adenocarcinoma of the lung protein 1) (DAL-1) (Erythrocyte membrane protein band 4.1-like 3) [Cleaved into: Band 4.1-like protein 3, N-terminally processed] | Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5. {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}. |
Q9Y2Q0 | ATP8A1 | S9 | ochoa | Phospholipid-transporting ATPase IA (EC 7.6.2.1) (ATPase class I type 8A member 1) (Chromaffin granule ATPase II) (P4-ATPase flippase complex alpha subunit ATP8A1) | Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the cell membrane (By similarity). Acts as aminophospholipid translocase at the cell membrane in neuronal cells (By similarity). {ECO:0000250|UniProtKB:P70704, ECO:0000269|PubMed:31416931}. |
Q9Y2Z0 | SUGT1 | T8 | ochoa | Protein SGT1 homolog (Protein 40-6-3) (Sgt1) (Suppressor of G2 allele of SKP1 homolog) | May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. |
Q9Y342 | PLLP | S9 | ochoa | Plasmolipin (Plasma membrane proteolipid) | Main component of the myelin sheath that plays an important role in myelin membrane biogenesis and myelination (PubMed:26002055). Plays an essential function in apical endocytosis. Regulates epithelial development through the regulation of apical endocytosis (By similarity). Part of the intracellular machinery that mediates basolateral-to-apical transport of ICAM-1, an essential adhesion receptor in epithelial cells, from the subapical compartment in hepatic epithelial cells (PubMed:34999972). {ECO:0000250|UniProtKB:A3KQ86, ECO:0000269|PubMed:26002055, ECO:0000269|PubMed:34999972}. |
Q9Y365 | STARD10 | T8 | ochoa | START domain-containing protein 10 (StARD10) (Antigen NY-CO-28) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28) (StAR-related lipid transfer protein 10) | May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. {ECO:0000250, ECO:0000269|PubMed:15911624}. |
Q9Y385 | UBE2J1 | S9 | ochoa | Ubiquitin-conjugating enzyme E2 J1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme J1) (Non-canonical ubiquitin-conjugating enzyme 1) (NCUBE-1) (Yeast ubiquitin-conjugating enzyme UBC6 homolog E) (HsUBC6e) | Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) and is essential for cells to recover from ER stress (PubMed:28321712). Plays a role in MAPKAPK2-dependent translational control of TNF-alpha synthesis (PubMed:24020373). Also acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the E3 ubiquitin-protein ligase RNF26 (PubMed:33472082). Plays a role in male fecundity through the interaction with the E3 ubiquitin-protein ligase RNF133 (PubMed:35831855). {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12082160, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:24020373, ECO:0000269|PubMed:28321712, ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:35831855}.; FUNCTION: (Microbial infection) Promotes Dengue virus RNA replication by negatively regulating IFN-beta signaling and mediating 'Lys-48'-linked ubiquitination on IRF3 (PubMed:30157886). {ECO:0000269|PubMed:30157886}. |
Q9Y3B9 | RRP15 | S8 | ochoa | RRP15-like protein (Ribosomal RNA-processing protein 15) | None |
Q9Y3C5 | RNF11 | S10 | ochoa | RING finger protein 11 | Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. {ECO:0000269|PubMed:14755250}. |
Q9Y3M2 | CBY1 | S9 | ochoa | Protein chibby homolog 1 (ARPP-binding protein) (Cytosolic leucine-rich protein) (PIGEA-14) (PKD2 interactor, Golgi and endoplasmic reticulum-associated 1) | Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors (PubMed:12712206, PubMed:19435523). Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins (PubMed:15194699). Promotes adipocyte and cardiomyocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q9D1C2, ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699, ECO:0000269|PubMed:19435523}. |
Q9Y483 | MTF2 | S10 | ochoa | Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (hPCl2) | Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (PubMed:23142980, PubMed:23228662, PubMed:31959557). Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation (By similarity). Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells (By similarity). Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex (By similarity). In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally (By similarity). Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity). {ECO:0000250|UniProtKB:Q02395, ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23228662, ECO:0000269|PubMed:31959557}. |
Q9Y4P1 | ATG4B | Y8 | ochoa | Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 1) (Autophagin-1) (Autophagy-related protein 4 homolog B) (HsAPG4B) (hAPG4B) | Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004, PubMed:26378241, PubMed:27527864, PubMed:28633005, PubMed:28821708, PubMed:29232556, PubMed:30076329, PubMed:30443548, PubMed:30661429). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:20818167, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28287329, PubMed:28633005, PubMed:29458288, PubMed:30661429). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:19322194, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:19322194, PubMed:29458288, PubMed:32686895, PubMed:33909989). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106). {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:22302004, ECO:0000269|PubMed:26378241, ECO:0000269|PubMed:27527864, ECO:0000269|PubMed:28287329, ECO:0000269|PubMed:28633005, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:29232556, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30076329, ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:32686895, ECO:0000269|PubMed:33773106, ECO:0000269|PubMed:33909989}. |
Q9Y5J7 | TIMM9 | S8 | ochoa | Mitochondrial import inner membrane translocase subunit Tim9 | Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}. |
Q9Y6D9 | MAD1L1 | T8 | psp | Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181) | Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:36322655}.; FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. {ECO:0000269|PubMed:19010891}. |
Q9Y6G9 | DYNC1LI1 | S9 | ochoa | Cytoplasmic dynein 1 light intermediate chain 1 (LIC1) (Dynein light chain A) (DLC-A) (Dynein light intermediate chain 1, cytosolic) (DLIC-1) | Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. Forms a functional Rab11/RAB11FIP3/dynein complex onto endosomal membrane that regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endosomal recycling compartment (ERC) (PubMed:20026645). {ECO:0000269|PubMed:19229290, ECO:0000269|PubMed:20026645}. |
Q9Y6J0 | CABIN1 | S10 | ochoa | Calcineurin-binding protein cabin-1 (Calcineurin inhibitor) (CAIN) | May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:9655484}. |
Q9Y6K9 | IKBKG | S8 | psp | NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) | Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:14695475, PubMed:20724660, PubMed:21518757, PubMed:9751060). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308, PubMed:33567255). Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308). Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3 (PubMed:19854139). Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (PubMed:20724660). {ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:19033441, ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660, ECO:0000269|PubMed:21518757, ECO:0000269|PubMed:21606507, ECO:0000269|PubMed:27777308, ECO:0000269|PubMed:33567255, ECO:0000269|PubMed:9751060}.; FUNCTION: (Microbial infection) Also considered to be a mediator for HTLV-1 Tax oncoprotein activation of NF-kappa-B. {ECO:0000269|PubMed:10364167, ECO:0000269|PubMed:11064457}. |
P08758 | ANXA5 | T8 | Sugiyama | Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CPB-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. |
Q86TG7 | PEG10 | S10 | Sugiyama | Retrotransposon-derived protein PEG10 (Embryonal carcinoma differentiation-regulated protein) (Mammalian retrotransposon-derived protein 2) (Myelin expression factor 3-like protein 1) (MEF3-like protein 1) (Paternally expressed gene 10 protein) (Retrotransposon gag domain-containing protein 3) (Retrotransposon-derived gag-like polyprotein) (Ty3/Gypsy-like protein) | Retrotransposon-derived protein that binds its own mRNA and self-assembles into virion-like capsids (PubMed:34413232). Forms virion-like extracellular vesicles that encapsulate their own mRNA and are released from cells, enabling intercellular transfer of PEG10 mRNA (PubMed:34413232). Binds its own mRNA in the 5'-UTR region, in the region near the boundary between the nucleocapsid (NC) and protease (PRO) coding sequences and in the beginning of the 3'-UTR region (PubMed:34413232). Involved in placenta formation: required for trophoblast stem cells differentiation (By similarity). Involved at the immediate early stage of adipocyte differentiation (By similarity). Overexpressed in many cancers and enhances tumor progression: promotes cell proliferation by driving cell cycle progression from G0/G1 (PubMed:12810624, PubMed:16423995, PubMed:26235627, PubMed:28193232). Enhances cancer progression by inhibiting the TGF-beta signaling, possibly via interaction with the TGF-beta receptor ACVRL1 (PubMed:15611116, PubMed:26235627, PubMed:30094509). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter; additional evidences are however required to confirm this result (By similarity). {ECO:0000250|UniProtKB:Q7TN75, ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15611116, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:26235627, ECO:0000269|PubMed:28193232, ECO:0000269|PubMed:30094509, ECO:0000269|PubMed:34413232}. |
P62906 | RPL10A | T9 | Sugiyama | Large ribosomal subunit protein uL1 (60S ribosomal protein L10a) (CSA-19) (Neural precursor cell expressed developmentally down-regulated protein 6) (NEDD-6) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
P61254 | RPL26 | T8 | Sugiyama | Large ribosomal subunit protein uL24 (60S ribosomal protein L26) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:26100019}. |
Q9UNX3 | RPL26L1 | T8 | Sugiyama | Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) | None |
P13798 | APEH | S8 | Sugiyama | Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Acyl-peptide hydrolase) (APH) (Acylaminoacyl-peptidase) (Oxidized protein hydrolase) (OPH) | This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus (PubMed:10719179, PubMed:1740429, PubMed:2006156). It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Also, involved in the degradation of oxidized and glycated proteins (PubMed:10719179). {ECO:0000250|UniProtKB:P13676, ECO:0000269|PubMed:10719179, ECO:0000269|PubMed:1740429, ECO:0000269|PubMed:2006156}. |
P46109 | CRKL | S8 | Sugiyama | Crk-like protein | May mediate the transduction of intracellular signals. |
P46109 | CRKL | S9 | Sugiyama | Crk-like protein | May mediate the transduction of intracellular signals. |
Q13148 | TARDBP | T8 | SIGNOR | 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}. |
O14965 | AURKA | S10 | GPS6|ELM|EPSD|PSP | Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Breast tumor-amplified kinase) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A) | Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013). Phosphorylates MCRS1 which is required for MCRS1-mediated kinetochore fiber assembly and mitotic progression (PubMed:27192185). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735). {ECO:0000250|UniProtKB:A0A8I3S724, ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27192185, ECO:0000269|PubMed:27335426, ECO:0000269|PubMed:28218735}. |
P61024 | CKS1B | S9 | Sugiyama | Cyclin-dependent kinases regulatory subunit 1 (CKS-1) | Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. |
A1L429 | GAGE12B; | Y9 | Sugiyama | G antigen 12B/C/D/E (GAGE-12B) (GAGE-12C) (GAGE-12D) (GAGE-12E) | None |
A6NDE8 | GAGE12H | Y9 | Sugiyama | G antigen 12H (GAGE-12H) | None |
A6NER3 | GAGE12J | Y9 | Sugiyama | G antigen 12J (GAGE-12J) | None |
O76087 | GAGE7 | Y9 | Sugiyama | G antigen 7 (GAGE-7) (AL4) (Cancer/testis antigen 4.7) (CT4.7) (GAGE-12I) (GAGE-7B) (GAGE-8) | None |
P0CL80 | GAGE12F | Y9 | Sugiyama | G antigen 12F (GAGE-12F) | None |
P0DSO3 | GAGE4 | Y9 | Sugiyama | G antigen 4 (Cancer/testis antigen 4.4) (CT4.4) | Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes. {ECO:0000269|PubMed:7544395}. |
Q13069 | GAGE5 | Y9 | Sugiyama | G antigen 5 (GAGE-5) (Cancer/testis antigen 4.5) (CT4.5) | None |
Q13070 | GAGE6 | Y9 | Sugiyama | G antigen 6 (GAGE-6) (Cancer/testis antigen 4.6) (CT4.6) | None |
Q14232 | EIF2B1 | Y9 | Sugiyama | Translation initiation factor eIF2B subunit alpha (eIF2B GDP-GTP exchange factor subunit alpha) | Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on eukaryotic initiation factor 2 (eIF2) gamma subunit (PubMed:25858979, PubMed:27023709, PubMed:31048492). Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed (PubMed:25858979, PubMed:31048492). {ECO:0000269|PubMed:25858979, ECO:0000269|PubMed:27023709, ECO:0000269|PubMed:31048492}. |
P61024 | CKS1B | Y8 | Sugiyama | Cyclin-dependent kinases regulatory subunit 1 (CKS-1) | Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. |
Q15369 | ELOC | Y8 | Sugiyama | Elongin-C (EloC) (Elongin 15 kDa subunit) (RNA polymerase II transcription factor SIII subunit C) (SIII p15) (Transcription elongation factor B polypeptide 1) | SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P83940, ECO:0000269|PubMed:7821821}.; FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:21199876, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:30166453, PubMed:33268465, PubMed:38326650, PubMed:35512830). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). Component the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C 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:26138980, PubMed:29775578, PubMed:29779948, PubMed:36805027, PubMed:38177675). The ECS(ASB9) complex mediates ubiquitination and degradation of CKB (PubMed:33268465). As part of a multisubunit ubiquitin ligase complex, polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). {ECO:0000250|UniProtKB:P83940, ECO:0000269|PubMed:10205047, ECO:0000269|PubMed:12004076, ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:21199876, ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:35512830, ECO:0000269|PubMed:36805027, ECO:0000269|PubMed:38177675, ECO:0000269|PubMed:38326650}.; FUNCTION: (Microbial infection) Following infection by HIV-1 virus, component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G (PubMed:18562529, PubMed:20532212, PubMed:22190037, PubMed:24225024, PubMed:24402281, PubMed:36754086). The complex can also ubiquitinate APOBEC3H to some extent (PubMed:37640699). {ECO:0000269|PubMed:18562529, ECO:0000269|PubMed:20532212, ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:24225024, ECO:0000269|PubMed:24402281, ECO:0000269|PubMed:36754086, ECO:0000269|PubMed:37640699}. |
Q9NZB2 | FAM120A | Y9 | Sugiyama | 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}. |
O75874 | IDH1 | S9 | Sugiyama | Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) | Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity). {ECO:0000250|UniProtKB:Q9XSG3, ECO:0000269|PubMed:10521434, ECO:0000269|PubMed:19935646, ECO:0000303|PubMed:10521434}. |
P61925 | PKIA | Y8 | GPS6|SIGNOR|ELM|iPTMNet|EPSD | cAMP-dependent protein kinase inhibitor alpha (PKI-alpha) (cAMP-dependent protein kinase inhibitor, muscle/brain isoform) | Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. |
P31689 | DNAJA1 | Y8 | Sugiyama | DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2) | Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as a co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}. |
P21108 | PRPS1L1 | S8 | Sugiyama | Ribose-phosphate pyrophosphokinase 3 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 1-like 1) (PRPS1-like 1) (Phosphoribosyl pyrophosphate synthase III) (PRS-III) | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. |
P60891 | PRPS1 | S8 | Sugiyama | Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (PPRibP) (Phosphoribosyl pyrophosphate synthase I) (PRS-I) | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. {ECO:0000269|PubMed:16939420, ECO:0000269|PubMed:17701900, ECO:0000269|PubMed:7593598}. |
Q92777 | SYN2 | S10 | ELM|iPTMNet|EPSD | Synapsin-2 (Synapsin II) | Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons (By similarity). {ECO:0000250}. |
P25789 | PSMA4 | T9 | Sugiyama | Proteasome subunit alpha type-4 (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) (Proteasome subunit alpha-3) (alpha-3) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
Q08211 | DHX9 | Y9 | Sugiyama | ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (DExH-box helicase 9) (Leukophysin) (LKP) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) | Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing (PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:24990949, PubMed:25062910, PubMed:28221134, PubMed:9111062, PubMed:37467750). Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:10198287, PubMed:9111062). Also binds to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1 (PubMed:11038348, PubMed:11149922, PubMed:11416126, PubMed:15355351, PubMed:28221134, PubMed:9323138, PubMed:9662397). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). Also acts as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA (PubMed:10924507, PubMed:11402034, PubMed:9162007). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process (PubMed:17531811). Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (PubMed:11687588). {ECO:0000250|UniProtKB:O70133, ECO:0000269|PubMed:10198287, ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11038348, ECO:0000269|PubMed:11149922, ECO:0000269|PubMed:11402034, ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:12711669, ECO:0000269|PubMed:15355351, ECO:0000269|PubMed:1537828, ECO:0000269|PubMed:16680162, ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20669935, ECO:0000269|PubMed:21247876, ECO:0000269|PubMed:21561811, ECO:0000269|PubMed:22190748, ECO:0000269|PubMed:24049074, ECO:0000269|PubMed:24990949, ECO:0000269|PubMed:25062910, ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:28355180, ECO:0000269|PubMed:28636595, ECO:0000269|PubMed:37467750, ECO:0000269|PubMed:9111062, ECO:0000269|PubMed:9162007, ECO:0000269|PubMed:9323138, ECO:0000269|PubMed:9662397}.; FUNCTION: (Microbial infection) Plays a role in HIV-1 replication and virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by facilitating the binding of RNA polymerase II holoenzyme to the proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation response element (TAR)-containing mRNAs (PubMed:11096080, PubMed:9892698). Involved also in HIV-1 mRNA splicing and transport (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-1 double-stranded RNA region of the primer binding site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 incorporation into virions and virion infectivity (PubMed:27107641). Also plays a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in plasmacytoid dendritic cells (pDCs), and hence induce antiviral innate immune responses (PubMed:20696886, PubMed:21957149). Binds (via the OB-fold region) to viral single-stranded DNA unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886). {ECO:0000269|PubMed:11096080, ECO:0000269|PubMed:16680162, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:21957149, ECO:0000269|PubMed:25149208, ECO:0000269|PubMed:27107641, ECO:0000269|PubMed:9892698}. |
P37840 | SNCA | S9 | iPTMNet|EPSD | Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP) | Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Also acts as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590). {ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:26442590, ECO:0000269|PubMed:28288128, ECO:0000269|PubMed:30404828}. |
O60829 | PAGE4 | S9 | EPSD|PSP | P antigen family member 4 (PAGE-4) (G antigen family C member 1) (PAGE-1) | Intrinsically disordered protein that potentiates the transcriptional activator activity of JUN (PubMed:24263171, PubMed:28289210). Protects cells from stress-induced apoptosis by inhibiting reactive oxygen species (ROS) production and via regulation of the MAPK signaling pathway (PubMed:21357425, PubMed:25374899, PubMed:30658679). {ECO:0000269|PubMed:21357425, ECO:0000269|PubMed:24263171, ECO:0000269|PubMed:25374899, ECO:0000269|PubMed:28289210, ECO:0000269|PubMed:30658679}. |
P54840 | GYS2 | S8 | SIGNOR | Glycogen [starch] synthase, liver (EC 2.4.1.11) (Glycogen synthase 2) | 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:1731614, ECO:0000269|PubMed:9691087}. |
P21108 | PRPS1L1 | S10 | Sugiyama | Ribose-phosphate pyrophosphokinase 3 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 1-like 1) (PRPS1-like 1) (Phosphoribosyl pyrophosphate synthase III) (PRS-III) | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. |
P60891 | PRPS1 | S10 | Sugiyama | Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (PPRibP) (Phosphoribosyl pyrophosphate synthase I) (PRS-I) | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. {ECO:0000269|PubMed:16939420, ECO:0000269|PubMed:17701900, ECO:0000269|PubMed:7593598}. |
P05787 | KRT8 | S9 | GPS6 | Keratin, type II cytoskeletal 8 (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8) | Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. |
P41091 | EIF2S3 | T9 | Sugiyama | Eukaryotic translation initiation factor 2 subunit 3 (EC 3.6.5.3) (Eukaryotic translation initiation factor 2 subunit gamma X) (eIF2-gamma X) (eIF2gX) | Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC) (By similarity). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (By similarity). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). {ECO:0000250|UniProtKB:P05198, ECO:0000269|PubMed:31836389}. |
Q2VIR3 | EIF2S3B | T9 | Sugiyama | Eukaryotic translation initiation factor 2 subunit 3B (EC 3.6.5.3) (Eukaryotic translation initiation factor 2 subunit gamma A) (eIF-2-gamma A) (eIF-2gA) | Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). {ECO:0000250|UniProtKB:P05198}. |
O76070 | SNCG | S9 | Sugiyama | Gamma-synuclein (Breast cancer-specific gene 1 protein) (Persyn) (Synoretin) (SR) | Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}. |
O95292 | VAPB | S9 | Sugiyama | 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}. |
P13693 | TPT1 | S9 | Sugiyama | Translationally-controlled tumor protein (TCTP) (Fortilin) (Histamine-releasing factor) (HRF) (p23) | Involved in calcium binding and microtubule stabilization (PubMed:12167714, PubMed:15162379, PubMed:15958728). Acts as a negative regulator of TSC22D1-mediated apoptosis, via interaction with and destabilization of TSC22D1 protein (PubMed:18325344). {ECO:0000269|PubMed:12167714, ECO:0000269|PubMed:15162379, ECO:0000269|PubMed:15958728, ECO:0000269|PubMed:18325344}. |
P41238 | APOBEC1 | S8 | Sugiyama | C->U-editing enzyme APOBEC-1 (EC 3.5.4.-) (Apolipoprotein B mRNA-editing enzyme catalytic subunit 1) (APO1) (APOBEC-1) (Apolipoprotein B mRNA-editing enzyme 1) (EC 3.5.4.36) (HEPR) (mRNA(cytosine(6666)) deaminase 1) | Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs (PubMed:30844405). Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA (PubMed:24916387). Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (PubMed:11727199). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity). {ECO:0000250|UniProtKB:P51908, ECO:0000269|PubMed:11727199, ECO:0000269|PubMed:24916387, ECO:0000269|PubMed:30844405}. |
Q16654 | PDK4 | S10 | Sugiyama | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4) | Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. {ECO:0000269|PubMed:15955060, ECO:0000269|PubMed:18658136, ECO:0000269|PubMed:21816445, ECO:0000269|PubMed:21852536}. |
Q16816 | PHKG1 | S10 | Sugiyama | Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (PHK-gamma-M) (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1, EC 2.7.11.26) | Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). {ECO:0000250}. |
Q6P2M8 | PNCK | T8 | Sugiyama | Calcium/calmodulin-dependent protein kinase type 1B (EC 2.7.11.17) (CaM kinase I beta) (CaM kinase IB) (CaM-KI beta) (CaMKI-beta) (Pregnancy up-regulated non-ubiquitously-expressed CaM kinase) | Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By similarity). {ECO:0000250}. |
Q15785 | TOMM34 | S8 | Sugiyama | Mitochondrial import receptor subunit TOM34 (hTom34) (Translocase of outer membrane 34 kDa subunit) | Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state. {ECO:0000269|PubMed:10101285, ECO:0000269|PubMed:11913975, ECO:0000269|PubMed:9324309}. |
O14818 | PSMA7 | T8 | Sugiyama | Proteasome subunit alpha type-7 (Proteasome subunit RC6-1) (Proteasome subunit XAPC7) (Proteasome subunit alpha-4) (alpha-4) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
Q96GD4 | AURKB | Y8 | Sugiyama | Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B) | Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:29449677). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:26829474). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (PubMed:15249581). Required for central/midzone spindle assembly and cleavage furrow formation (PubMed:12458200, PubMed:12686604). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (PubMed:11516652, PubMed:12925766, PubMed:14610074). Phosphorylation of INCENP leads to increased AURKB activity (PubMed:11516652, PubMed:12925766, PubMed:14610074). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (PubMed:11756469, PubMed:11784863, PubMed:11856369, PubMed:12689593, PubMed:14602875, PubMed:16103226, PubMed:21658950). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (PubMed:21658950). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (PubMed:11784863, PubMed:11856369). AURKB is also required for kinetochore localization of BUB1 and SGO1 (PubMed:15020684, PubMed:17617734). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (PubMed:20959462). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (PubMed:33542149). Phosphorylates KRT5 during anaphase and telophase (By similarity). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (PubMed:25666058). {ECO:0000250|UniProtKB:O70126, ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515, ECO:0000269|PubMed:25666058, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29449677, ECO:0000269|PubMed:33542149}. |
P22061 | PCMT1 | S9 | Sugiyama | Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) | Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (PubMed:3167043, PubMed:6469980). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity). {ECO:0000250|UniProtKB:P23506, ECO:0000269|PubMed:3167043, ECO:0000269|PubMed:6469980}. |
Q9UKG9 | CROT | S8 | Sugiyama | Peroxisomal carnitine O-octanoyltransferase (COT) (EC 2.3.1.137) | Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. {ECO:0000269|PubMed:10486279}. |
Q9UKG9 | CROT | T9 | Sugiyama | Peroxisomal carnitine O-octanoyltransferase (COT) (EC 2.3.1.137) | Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. {ECO:0000269|PubMed:10486279}. |
B2RUZ4 | SMIM1 | Y10 | ochoa | Small integral membrane protein 1 (Vel blood group antigen) | Regulator of red blood cell formation. {ECO:0000250|UniProtKB:B3DHH5}. |
J3KQ70 | INO80B-WBP1 | T10 | ochoa | HCG2039827, isoform CRA_e (INO80B-WBP1 readthrough (NMD candidate)) | None |
K7EPI3 | None | Y10 | ochoa | Dilute domain-containing protein | None |
O15440 | ABCC5 | Y10 | ochoa | ATP-binding cassette sub-family C member 5 (EC 7.6.2.-) (EC 7.6.2.2) (Multi-specific organic anion transporter C) (MOAT-C) (Multidrug resistance-associated protein 5) (SMRP) (pABC11) | ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of endogenous metabolites such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro) (PubMed:10893247, PubMed:12637526, PubMed:12695538, PubMed:15899835, PubMed:17229149, PubMed:25964343). Also acts as a general glutamate conjugate and analog transporter that can limit the brain levels of endogenous metabolites, drugs, and toxins (PubMed:26515061). Confers resistance to the antiviral agent PMEA (PubMed:12695538). Able to transport several anticancer drugs including methotrexate, and nucleotide analogs in vitro, however it does with low affinity, thus the exact role of ABCC5 in mediating resistance still needs to be elucidated (PubMed:10840050, PubMed:12435799, PubMed:12695538, PubMed:15899835). Acts as a heme transporter required for the translocation of cytosolic heme to the secretory pathway (PubMed:24836561). May play a role in energy metabolism by regulating the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine cells (By similarity). {ECO:0000250|UniProtKB:Q9R1X5, ECO:0000269|PubMed:10840050, ECO:0000269|PubMed:10893247, ECO:0000269|PubMed:12435799, ECO:0000269|PubMed:12637526, ECO:0000269|PubMed:12695538, ECO:0000269|PubMed:15899835, ECO:0000269|PubMed:17229149, ECO:0000269|PubMed:24836561, ECO:0000269|PubMed:25964343, ECO:0000269|PubMed:26515061}. |
O60869 | EDF1 | T10 | ochoa | Endothelial differentiation-related factor 1 (EDF-1) (Multiprotein-bridging factor 1) (MBF1) | Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism. {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021, ECO:0000269|PubMed:15112053, ECO:0000269|PubMed:9813014}. |
O75170 | PPP6R2 | T10 | ochoa|psp | Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2) | Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. {ECO:0000269|PubMed:16769727}. |
P00338 | LDHA | Y10 | ochoa|psp | L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59) | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:11276087}. |
P02545 | LMNA | T10 | ochoa|psp | Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}. |
P05023 | ATP1A1 | Y10 | ochoa | Sodium/potassium-transporting ATPase subunit alpha-1 (Na(+)/K(+) ATPase alpha-1 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-1) | This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:29499166, PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404}. |
P07476 | IVL | T10 | ochoa | Involucrin | Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. |
P11413 | G6PD | T10 | ochoa | Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:35122041, ECO:0000269|PubMed:38066190, ECO:0000269|PubMed:743300}. |
P12956 | XRCC6 | T10 | ochoa | X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6) | Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Required for double-strand break repair and V(D)J recombination (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Also has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). It works in the 3'-5' direction (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Binding to DNA may be mediated by XRCC6 (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks (PubMed:20383123). 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:12145306). 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). Negatively regulates apoptosis by interacting with BAX and sequestering it from the mitochondria (PubMed:15023334). Might have deubiquitination activity, acting on BAX (PubMed:18362350). {ECO:0000269|PubMed:11493912, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:15023334, ECO:0000269|PubMed:18362350, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}. |
P14618 | PKM | T10 | ochoa | Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (p58) | Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263). {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723, ECO:0000269|PubMed:20847263}.; FUNCTION: [Isoform M2]: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100). {ECO:0000250|UniProtKB:P52480, ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263, ECO:0000269|PubMed:21620138, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900}.; FUNCTION: [Isoform M1]: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed:18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed:20847263). {ECO:0000269|PubMed:18337823, ECO:0000269|PubMed:20847263}. |
P16402 | H1-3 | T10 | ochoa | Histone H1.3 (Histone H1c) (Histone H1s-2) | Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}. |
P16989 | YBX3 | T10 | ochoa | Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB) | Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. |
P18850 | ATF6 | T10 | ochoa | Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha] | [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464). {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11779464}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR (PubMed:10564271, PubMed:11158310, PubMed:11163209, PubMed:11779464). Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3') (PubMed:10564271, PubMed:11158310, PubMed:11779464). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor (PubMed:10564271, PubMed:11158310, PubMed:11779464). May play a role in foveal development and cone function in the retina (PubMed:26029869). {ECO:0000269|PubMed:10564271, ECO:0000269|PubMed:11158310, ECO:0000269|PubMed:11163209, ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:26029869}. |
P20648 | ATP4A | Y10 | psp | Potassium-transporting ATPase alpha chain 1 (EC 7.2.2.19) (Gastric H(+)/K(+) ATPase subunit alpha) (Proton pump) | The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (By similarity). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (By similarity). {ECO:0000250|UniProtKB:P09626, ECO:0000250|UniProtKB:P19156, ECO:0000250|UniProtKB:Q64436}. |
P22736 | NR4A1 | T10 | ochoa | Nuclear receptor subfamily 4immunitygroup A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3) | Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' (PubMed:18690216, PubMed:8121493, PubMed:9315652). Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain (PubMed:18690216). Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation (PubMed:22983157). Regulates the inflammatory response in macrophages by regulating metabolic adaptations during inflammation, including repressing the transcription of genes involved in the citric acid cycle (TCA) (By similarity). Inhibits NF-kappa-B signaling by binding to low-affinity NF-kappa-B binding sites, such as at the IL2 promoter (PubMed:15466594). May act concomitantly with NR4A2 in regulating the expression of delayed-early genes during liver regeneration (By similarity). Plays a role in the vascular response to injury (By similarity). {ECO:0000250|UniProtKB:P12813, ECO:0000250|UniProtKB:P22829, ECO:0000269|PubMed:15466594, ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:8121493, ECO:0000269|PubMed:9315652}.; FUNCTION: In the cytosol, upon its detection of both bacterial lipopolysaccharide (LPS) and NBRE-containing mitochondrial DNA released by GSDMD pores during pyroptosis, it promotes non-canonical NLRP3 inflammasome activation by stimulating association of NLRP3 and NEK7. {ECO:0000250|UniProtKB:P12813}. |
P24844 | MYL9 | T10 | psp | Myosin regulatory light polypeptide 9 (20 kDa myosin light chain) (LC20) (MLC-2C) (Myosin RLC) (Myosin regulatory light chain 2, smooth muscle isoform) (Myosin regulatory light chain 9) (Myosin regulatory light chain MRLC1) | Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (PubMed:11942626, PubMed:2526655). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity). {ECO:0000250|UniProtKB:Q9CQ19, ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:2526655}. |
P28289 | TMOD1 | Y10 | ochoa | Tropomodulin-1 (Erythrocyte tropomodulin) (E-Tmod) | Blocks the elongation and depolymerization of the actin filaments at the pointed end (PubMed:38168645). The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus. {ECO:0000269|PubMed:38168645, ECO:0000269|PubMed:8002995}. |
P31949 | S100A11 | T10 | psp | Protein S100-A11 (Calgizzarin) (Metastatic lymph node gene 70 protein) (MLN 70) (Protein S100-C) (S100 calcium-binding protein A11) [Cleaved into: Protein S100-A11, N-terminally processed] | Facilitates the differentiation and the cornification of keratinocytes. {ECO:0000269|PubMed:18618420}. |
P34947 | GRK5 | T10 | psp | G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5) | Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro). {ECO:0000269|PubMed:19661922, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20038610, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:21728385}. |
P38435 | GGCX | T10 | ochoa | Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase) | Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide (PubMed:17073445). Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP) (PubMed:17073445). {ECO:0000269|PubMed:17073445}. |
P42566 | EPS15 | T10 | 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}. |
P49356 | FNTB | Y10 | ochoa | Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) | Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}. |
P50402 | EMD | T10 | 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}. |
P51965 | UBE2E1 | T10 | ochoa | Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1) | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. Catalyzes monoubiquitination of other proteins in both an E3-dependent and E3-independent manner (PubMed:27237050). {ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:27237050}. |
P53567 | CEBPG | T10 | ochoa | CCAAT/enhancer-binding protein gamma (C/EBP gamma) | Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. {ECO:0000250|UniProtKB:P26801, ECO:0000250|UniProtKB:P53568, ECO:0000269|PubMed:7665092}. |
P61247 | RPS3A | T10 | psp | Small ribosomal subunit protein eS1 (40S ribosomal protein S3a) (v-fos transformation effector protein) (Fte-1) | Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. |
P62310 | LSM3 | T10 | ochoa | U6 snRNA-associated Sm-like protein LSm3 | Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:28781166}. |
P62491 | RAB11A | Y10 | ochoa | Ras-related protein Rab-11A (Rab-11) (EC 3.6.5.2) (YL8) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:15601896, PubMed:15689490, PubMed:17462998, PubMed:19542231, PubMed:20026645, PubMed:20890297, PubMed:21282656, PubMed:26032412). The small Rab GTPase RAB11A regulates endocytic recycling (PubMed:20026645). Forms a functional Rab11/RAB11FIP3/dynein complex 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). Acts as a major regulator of membrane delivery during cytokinesis (PubMed:15601896). Together with MYO5B and RAB8A participates in epithelial cell polarization (PubMed:21282656). Together with Rabin8/RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells (PubMed:17462998). Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane (PubMed:19542231). Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane (PubMed:15689490). Regulates the recycling of FCGRT (receptor of Fc region of monomeric IgG) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes (By similarity). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879, PubMed:31204173). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-endososomal dependent export route via interaction with WDR44 (PubMed:32344433). {ECO:0000250|UniProtKB:P62490, ECO:0000250|UniProtKB:P62492, ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:15689490, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26032412, ECO:0000269|PubMed:31204173, ECO:0000269|PubMed:32344433}. |
P62753 | RPS6 | T10 | ochoa | Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (Phosphoprotein NP33) | Component of the 40S small ribosomal subunit (PubMed:23636399, PubMed:8706699). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (PubMed:17220279). 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:17220279, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:8706699}. |
P63165 | SUMO1 | T10 | ochoa | Small ubiquitin-related modifier 1 (SUMO-1) (GAP-modifying protein 1) (GMP1) (SMT3 homolog 3) (Sentrin) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (Ubiquitin-like protein UBL1) | Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}. |
P63215 | GNG3 | T10 | ochoa | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. |
P63244 | RACK1 | T10 | ochoa | Small ribosomal subunit protein RACK1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Receptor of activated protein C kinase 1) [Cleaved into: Small ribosomal subunit protein RACK1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed) (Receptor of activated protein C kinase 1, N-terminally processed)] | Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity). {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:9584165}.; FUNCTION: (Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. {ECO:0000269|PubMed:21347310}.; FUNCTION: (Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs. {ECO:0000269|PubMed:11312657}.; FUNCTION: (Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs. {ECO:0000269|PubMed:28636603}.; FUNCTION: (Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses. {ECO:0000269|PubMed:25416947}. |
Q08495 | DMTN | T10 | ochoa | Dematin (Dematin actin-binding protein) (Erythrocyte membrane protein band 4.9) | Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:10565303, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471}. |
Q12891 | HYAL2 | T10 | ochoa | Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2) (Lung carcinoma protein 2) (LuCa-2) | Catalyzes hyaluronan degradation into small fragments that are endocytosed and degraded in lysosomes by HYAL1 and exoglycosidases (PubMed:9712871). Essential for the breakdown of extracellular matrix hyaluronan (PubMed:28081210). {ECO:0000269|PubMed:28081210, ECO:0000269|PubMed:9712871}. |
Q13541 | EIF4EBP1 | T10 | ochoa | Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) | Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:7935836}. |
Q13568 | IRF5 | T10 | psp | Interferon regulatory factor 5 (IRF-5) | Transcription factor that plays a critical role in innate immunity by activating expression of type I interferon (IFN) IFNA and INFB and inflammatory cytokines downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9 (PubMed:11303025, PubMed:15695821, PubMed:22412986, PubMed:25326418, PubMed:32433612). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (By similarity). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction downstream of the TLR-activated, MyD88-dependent pathway (By similarity). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000250|UniProtKB:P56477, ECO:0000269|PubMed:11303025, ECO:0000269|PubMed:15695821, ECO:0000269|PubMed:22412986, ECO:0000269|PubMed:25326418, ECO:0000269|PubMed:32433612, ECO:0000269|PubMed:33440148}. |
Q14974 | KPNB1 | T10 | ochoa | Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) | Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). Acting autonomously, serves itself as NLS receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:24699649, PubMed:7615630, PubMed:9687515). Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607, PubMed:9687515). In association with IPO7, mediates the nuclear import of H1 histone (PubMed:10228156). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones (By similarity). Imports MRTFA, SNAI1 and PRKCI into the nucleus (PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649). {ECO:0000250|UniProtKB:P70168, ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:20818336, ECO:0000269|PubMed:24699649, ECO:0000269|PubMed:7615630, ECO:0000269|PubMed:9687515}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:16704975, ECO:0000269|PubMed:9405152, ECO:0000269|PubMed:9891055}. |
Q15417 | CNN3 | Y10 | ochoa|psp | Calponin-3 (Calponin, acidic isoform) | Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
Q15651 | HMGN3 | T10 | ochoa | High mobility group nucleosome-binding domain-containing protein 3 (Thyroid receptor-interacting protein 7) (TR-interacting protein 7) (TRIP-7) | Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity). {ECO:0000250}. |
Q15907 | RAB11B | Y10 | ochoa | Ras-related protein Rab-11B (EC 3.6.5.2) (GTP-binding protein YPT3) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970, PubMed:26032412). The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). {ECO:0000269|PubMed:14627637, ECO:0000269|PubMed:19029296, ECO:0000269|PubMed:19244346, ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21248079, ECO:0000269|PubMed:22129970, ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26032412, ECO:0000269|PubMed:31204173}. |
Q16623 | STX1A | T10 | ochoa | Syntaxin-1A (Neuron-specific antigen HPC-1) | Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:26635000). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (PubMed:23091057). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). {ECO:0000250|UniProtKB:O35526, ECO:0000269|PubMed:23091057, ECO:0000269|PubMed:26635000}. |
Q3T8J9 | GON4L | T10 | ochoa | GON-4-like protein (GON-4 homolog) | Has transcriptional repressor activity, probably as part of a complex with YY1, SIN3A and HDAC1. Required for B cell lymphopoiesis. {ECO:0000250|UniProtKB:Q9DB00}. |
Q5EBL8 | PDZD11 | Y10 | ochoa | PDZ domain-containing protein 11 (ATPase-interacting PDZ protein) (Plasma membrane calcium ATPase-interacting single-PDZ protein) (PMCA-interacting single-PDZ protein) | Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-binding protein TSPAN33. {ECO:0000269|PubMed:30463011}. |
Q5T0Z8 | C6orf132 | T10 | ochoa | Uncharacterized protein C6orf132 | None |
Q5T6S3 | PHF19 | T10 | ochoa | PHD finger protein 19 (Polycomb-like protein 3) (hPCL3) | Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (PubMed:15563832, PubMed:18691976, PubMed:23104054, PubMed:23160351, PubMed:23228662, PubMed:23273982, PubMed:29499137, PubMed:31959557). Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing (PubMed:23160351). Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds histone H3 dimethylated at 'Lys-36' (H3K36me2) (PubMed:23104054). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter (PubMed:15563832). {ECO:0000269|PubMed:15563832, ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:23104054, ECO:0000269|PubMed:23160351, ECO:0000269|PubMed:23228662, ECO:0000269|PubMed:23273982, ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. |
Q6SZW1 | SARM1 | Y10 | 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}. |
Q6ZSS7 | MFSD6 | T10 | ochoa | Major facilitator superfamily domain-containing protein 6 (Macrophage MHC class I receptor 2 homolog) | None |
Q7Z7L9 | ZSCAN2 | T11 | ochoa | Zinc finger and SCAN domain-containing protein 2 (Zinc finger protein 29 homolog) (Zfp-29) (Zinc finger protein 854) | May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis. {ECO:0000250}. |
Q86VR2 | RETREG3 | T10 | ochoa | Reticulophagy regulator 3 | 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). Promotes ER membrane curvature and ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes (PubMed:33826365). Required for collagen quality control in a LIR motif-dependent manner (By similarity). Mediates NRF1-enhanced neurite outgrowth (PubMed:26040720). {ECO:0000250|UniProtKB:Q9CQV4, ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:33826365, ECO:0000269|PubMed:34338405}. |
Q86WQ0 | NR2C2AP | T10 | ochoa | Nuclear receptor 2C2-associated protein (TR4 orphan receptor-associated 16 kDa protein) | May act as a repressor of NR2C2-mediated transactivation by suppressing the binding between NR2C2/TR4 and the TR4-response element in target genes. {ECO:0000269|PubMed:12486131}. |
Q8IWZ3 | ANKHD1 | T10 | ochoa | Ankyrin repeat and KH domain-containing protein 1 (HIV-1 Vpr-binding ankyrin repeat protein) (Multiple ankyrin repeats single KH domain) (hMASK) | May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}. |
Q8IY18 | SMC5 | T10 | ochoa | Structural maintenance of chromosomes protein 5 (SMC protein 5) (SMC-5) (hSMC5) | Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541). {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:26983541}. |
Q8N0S6 | CENPL | T10 | ochoa | Centromere protein L (CENP-L) (Interphase centromere complex protein 33) | Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16716197}. |
Q8TAA9 | VANGL1 | Y10 | ochoa | Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) | None |
Q8TAP9 | MPLKIP | T10 | ochoa | M-phase-specific PLK1-interacting protein (TTD non-photosensitive 1 protein) | May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. {ECO:0000269|PubMed:17310276}. |
Q8WUM0 | NUP133 | T10 | 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}. |
Q8WW01 | TSEN15 | T10 | ochoa | tRNA-splicing endonuclease subunit Sen15 (SEN15 homolog) (HsSEN15) (tRNA-intron endonuclease Sen15) | Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini (PubMed:15109492, PubMed:27392077). There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (PubMed:15109492). {ECO:0000269|PubMed:15109492, ECO:0000269|PubMed:27392077}. |
Q92536 | SLC7A6 | T10 | 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}. |
Q92616 | GCN1 | T10 | ochoa | Stalled ribosome sensor GCN1 (GCN1 eIF-2-alpha kinase activator homolog) (GCN1-like protein 1) (General control of amino-acid synthesis 1-like protein 1) (Translational activator GCN1) (HsGCN1) | Ribosome collision sensor that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (PubMed:32610081, PubMed:36638793, PubMed:37651229, PubMed:37951215, PubMed:37951216). Directly binds to the ribosome and acts as a sentinel for colliding ribosomes: activated following ribosome stalling and promotes recruitment of RNF14, which directly ubiquitinates EEF1A1/eEF1A, leading to its degradation (PubMed:36638793, PubMed:37951215, PubMed:37951216). In addition to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal protein (PubMed:36638793, PubMed:37651229). GCN1 also acts as a positive activator of the integrated stress response (ISR) by mediating activation of EIF2AK4/GCN2 in response to amino acid starvation (By similarity). Interaction with EIF2AK4/GCN2 on translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading to phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) (By similarity). EIF2S1/eIF-2-alpha phosphorylation converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity). {ECO:0000250|UniProtKB:E9PVA8, ECO:0000269|PubMed:32610081, ECO:0000269|PubMed:36638793, ECO:0000269|PubMed:37651229, ECO:0000269|PubMed:37951215, ECO:0000269|PubMed:37951216}. |
Q96A32 | MYL11 | T10 | ochoa | Myosin regulatory light chain 11 (Fast skeletal myosin light chain 2) (MLC2B) (Myosin light chain 11) (Myosin regulatory light chain 2, skeletal muscle isoform) | Myosin regulatory subunit that plays an essential role to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction (By similarity). {ECO:0000250|UniProtKB:O93409}. |
Q96ET8 | TVP23C | T10 | ochoa | Golgi apparatus membrane protein TVP23 homolog C | None |
Q96FZ5 | CMTM7 | T10 | ochoa | CKLF-like MARVEL transmembrane domain-containing protein 7 (Chemokine-like factor superfamily member 7) | None |
Q96RD7 | PANX1 | Y10 | psp | Pannexin-1 (PANX1) [Cleaved into: Caspase-activated pannexin-1 (Caspase-activated PANX1)] | Ion channel involved in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and oogenesis (PubMed:15304325, PubMed:16908669, PubMed:20829356, PubMed:20944749, PubMed:30918116). Forms anion-selective channels with relatively low conductance and an order of permeabilities: nitrate>iodide>chlroride>>aspartate=glutamate=gluconate (By similarity). Can release ATP upon activation through phosphorylation or cleavage at C-terminus (PubMed:32238926). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (PubMed:16908669). {ECO:0000250|UniProtKB:Q9JIP4, ECO:0000269|PubMed:15304325, ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:20944749, ECO:0000269|PubMed:32238926}.; FUNCTION: [Caspase-activated pannexin-1]: During apoptosis, the C terminal tail is cleaved by caspases, which opens the main pore acting as a large-pore ATP efflux channel with a broad distribution, which allows the regulated release of molecules and ions smaller than 1 kDa, such as nucleotides ATP and UTP, and selective plasma membrane permeability to attract phagocytes that engulf the dying cells. {ECO:0000269|PubMed:20944749, ECO:0000269|PubMed:32238926, ECO:0000269|PubMed:32494015}. |
Q99618 | CDCA3 | T10 | ochoa | Cell division cycle-associated protein 3 (Gene-rich cluster protein C8) (Trigger of mitotic entry protein 1) (TOME-1) | F-box-like protein which is required for entry into mitosis. Acts by participating in E3 ligase complexes that mediate the ubiquitination and degradation of WEE1 kinase at G2/M phase (By similarity). {ECO:0000250}. |
Q99959 | PKP2 | Y10 | ochoa | Plakophilin-2 | A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:25208567). Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (PubMed:23884246). Required to maintain gingival epithelial barrier function (PubMed:34368962). Important component of the desmosome that is also required for localization of desmosome component proteins such as DSC2, DSG2 and JUP to the desmosome cell-cell junction (PubMed:22781308, PubMed:25208567). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (By similarity). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (By similarity). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes, via ANK3 stabilization and modulation of SCN5A/Nav1.5 localization to cell-cell junctions (By similarity). Required for mitochondrial function, nuclear envelope integrity and positive regulation of SIRT3 transcription via maintaining DES localization at its nuclear envelope and cell tip anchoring points, and thereby preserving regulation of the transcriptional program (PubMed:35959657). Maintenance of nuclear envelope integrity protects against DNA damage and transcriptional dysregulation of genes, especially those involved in the electron transport chain, thereby preserving mitochondrial function and protecting against superoxide radical anion generation (PubMed:35959657). Binds single-stranded DNA (ssDNA) (PubMed:20613778). May regulate the localization of GJA1 to gap junctions in intercalated disks of the heart (PubMed:18662195). Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297). Acts as a host restriction factor for IAV viral propagation, potentially via disrupting the interaction of IAV polymerase complex proteins (PubMed:28169297). {ECO:0000250|UniProtKB:F1M7L9, ECO:0000250|UniProtKB:Q9CQ73, ECO:0000269|PubMed:18662195, ECO:0000269|PubMed:20613778, ECO:0000269|PubMed:22781308, ECO:0000269|PubMed:23884246, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:28169297, ECO:0000269|PubMed:34368962, ECO:0000269|PubMed:35959657}. |
Q9BPY8 | HOPX | T10 | ochoa | Homeodomain-only protein (Lung cancer-associated Y protein) (Not expressed in choriocarcinoma protein 1) (Odd homeobox protein 1) | Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy (By similarity). May act as a tumor suppressor. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and assists in chaperone-mediated protein refolding (PubMed:27708256). {ECO:0000250|UniProtKB:Q8R1H0, ECO:0000269|PubMed:27708256}. |
Q9BQ67 | GRWD1 | T10 | ochoa | Glutamate-rich WD repeat-containing protein 1 | Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness (PubMed:25990725). {ECO:0000269|PubMed:25990725}. |
Q9BTX7 | TTPAL | T10 | ochoa | Alpha-tocopherol transfer protein-like | May act as a protein that binds a hydrophobic ligand. {ECO:0000305}. |
Q9BXK1 | KLF16 | Y10 | psp | 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}. |
Q9C086 | INO80B | T10 | ochoa | INO80 complex subunit B (High mobility group AT-hook 1-like 4) (IES2 homolog) (hIes2) (PAP-1-associated protein 1) (PAPA-1) (Zinc finger HIT domain-containing protein 4) | Induces growth and cell cycle arrests at the G1 phase of the cell cycle. {ECO:0000269|PubMed:15556297}.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000269|PubMed:15556297}. |
Q9GZX9 | TWSG1 | T10 | ochoa | Twisted gastrulation protein homolog 1 | May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development (By similarity). {ECO:0000250}. |
Q9H0U9 | TSPYL1 | T10 | ochoa | Testis-specific Y-encoded-like protein 1 (TSPY-like protein 1) | None |
Q9H1K6 | TLNRD1 | T10 | ochoa | Talin rod domain-containing protein 1 (Mesoderm development candidate 1) | Actin-binding protein which may have an oncogenic function and regulates cell proliferation, migration and invasion in cancer cells. {ECO:0000269|PubMed:22179486}. |
Q9H813 | PACC1 | Y10 | ochoa | Proton-activated chloride channel (PAC) (hPAC) (Acid-sensitive outwardly-rectifying anion channel) (ASOR) (Proton-activated outwardly rectifying anion channel) (PAORAC) (Transmembrane protein 206) (hTMEM206) | Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925, ECO:0000269|PubMed:31318332}. |
Q9H8V3 | ECT2 | T10 | 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}. |
Q9HB90 | RRAGC | T10 | 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}. |
Q9HCU5 | PREB | Y10 | psp | Guanine nucleotide-exchange factor SEC12 (Prolactin regulatory element-binding protein) | Guanine nucleotide exchange factor (GEF) that regulates the assembly of the coat protein complex II/COPII in endoplasmic reticulum (ER) to Golgi vesicle-mediated transport. Selectively activates SAR1A and SAR1B by promoting the exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) in these small GTPases (PubMed:32358066). In their activated GTP-bound state, SAR1A and SAR1B insert into the membrane of the endoplasmic reticulum where they recruit the remainder of the coat protein complex II/COPII which is responsible for both the sorting of proteins and the deformation and budding of membranes into vesicles destined to the Golgi (PubMed:32358066). {ECO:0000269|PubMed:32358066}.; FUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription. {ECO:0000250|UniProtKB:Q9WTV0}. |
Q9NP80 | PNPLA8 | Y10 | ochoa | Calcium-independent phospholipase A2-gamma (EC 3.1.1.-) (EC 3.1.1.5) (Intracellular membrane-associated calcium-independent phospholipase A2 gamma) (iPLA2-gamma) (PNPLA-gamma) (Patatin-like phospholipase domain-containing protein 8) (iPLA2-2) | Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors (PubMed:10744668, PubMed:10833412, PubMed:15695510, PubMed:15908428, PubMed:17213206, PubMed:18171998, PubMed:28442572). Hydrolyzes phosphatidylethanolamine, phosphatidylcholine and probably phosphatidylinositol with a possible preference for the former (PubMed:15695510). Also has a broad substrate specificity in terms of fatty acid moieties, hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal rates from either the sn-1 or sn-2 position in diacyl phosphatidylcholine (PubMed:10744668, PubMed:10833412, PubMed:15695510, PubMed:15908428). However, has a weak activity toward polyunsaturated fatty acids at the sn-2 position, and thereby favors the production of 2-arachidonoyl lysophosphatidylcholine, a key branch point metabolite in eicosanoid signaling (PubMed:15908428). On the other hand, can produce arachidonic acid from the sn-1 position of diacyl phospholipid and from the sn-2 position of arachidonate-containing plasmalogen substrates (PubMed:15908428). Therefore, plays an important role in the mobilization of arachidonic acid in response to cellular stimuli and the generation of lipid second messengers (PubMed:15695510, PubMed:15908428). Can also hydrolyze lysophosphatidylcholine (PubMed:15695510). In the mitochondrial compartment, catalyzes the hydrolysis and release of oxidized aliphatic chains from cardiolipin and integrates mitochondrial bioenergetics and signaling. It is essential for maintaining efficient bioenergetic mitochondrial function through tailoring mitochondrial membrane lipid metabolism and composition (PubMed:28442572). {ECO:0000250|UniProtKB:Q8K1N1, ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:10833412, ECO:0000269|PubMed:15695510, ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:18171998, ECO:0000269|PubMed:28442572}. |
Q9NWV8 | BABAM1 | T10 | ochoa | BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) | Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}. |
Q9NX76 | CMTM6 | T10 | ochoa | CKLF-like MARVEL transmembrane domain-containing protein 6 (Chemokine-like factor superfamily member 6) | Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its STUB1-mediated ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy. {ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417}. |
Q9NXH3 | PPP1R14D | T10 | ochoa | Protein phosphatase 1 regulatory subunit 14D (Gastrointestinal and brain-specific PP1-inhibitory protein 1) (GBPI-1) | Inhibitor of PPP1CA. Has inhibitory activity only when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000269|PubMed:12974676}. |
Q9NYZ1 | TVP23B | T10 | ochoa | Golgi apparatus membrane protein TVP23 homolog B | None |
Q9P0K8 | FOXJ2 | T10 | ochoa | Forkhead box protein J2 (Fork head homologous X) | [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to two different type of DNA binding sites. More effective than isoform FOXJ2.S in transcriptional activation (PubMed:10777590, PubMed:10966786). Plays an important role in spermatogenesis, especially in spermatocyte meiosis (By similarity). {ECO:0000250|UniProtKB:Q9ES18, ECO:0000269|PubMed:10777590, ECO:0000269|PubMed:10966786}.; FUNCTION: [Isoform FOXJ2.S]: Transcriptional activator. {ECO:0000269|PubMed:10966786}. |
Q9UBF6 | RNF7 | T10 | psp | RING-box protein 2 (Rbx2) (EC 2.3.2.27) (EC 2.3.2.32) (CKII beta-binding protein 1) (CKBBP1) (RING finger protein 7) (Regulator of cullins 2) (Sensitive to apoptosis gene protein) | Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733, PubMed:35512830). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed:21980433, PubMed:33268465). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type and brings it into close proximity to the substrate (PubMed:34518685). Catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex, that regulate reelin signaling by mediating ubiquitination and degradation of DAB1 (By similarity). The ECS(SOCS2) complex mediates the ubiquitination and subsequent proteasomal degradation of phosphorylated EPOR and GHR (PubMed:21980433, PubMed:25505247). Promotes ubiquitination and degradation of NF1, thereby regulating Ras protein signal transduction (By similarity). As part of the ECS(ASB9) complex, catalyzes ubiquitination and degradation of CKB (PubMed:33268465). The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS (PubMed:38418882). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). As part of some ECS complex, catalyzes 'Lys-11'-linked ubiquitination and degradation of BTRC (PubMed:27910872). ECS complexes and ARIH2 collaborate in tandem to mediate ubiquitination of target proteins; ARIH2 mediating addition of the first ubiquitin on CRLs targets (PubMed:34518685, PubMed:38418882). Specifically catalyzes the neddylation of CUL5 via its interaction with UBE2F (PubMed:19250909). Does not catalyze neddylation of other cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed:19250909). May play a role in protecting cells from apoptosis induced by redox agents (PubMed:10082581). {ECO:0000250|UniProtKB:Q9WTZ1, ECO:0000269|PubMed:10082581, ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:21980433, ECO:0000269|PubMed:25505247, ECO:0000269|PubMed:27910872, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:34518685, ECO:0000269|PubMed:35512830, ECO:0000269|PubMed:38418882, ECO:0000269|PubMed:38574733}.; FUNCTION: [Isoform 2]: Inactive. {ECO:0000269|PubMed:11506706}.; FUNCTION: (Microbial infection) Following infection by HIV-1 virus, catalytic component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G. {ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:23300442}. |
Q9UKT5 | FBXO4 | T10 | ochoa | F-box only protein 4 | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10531035, PubMed:18598945, PubMed:20181953, PubMed:29142209). Promotes ubiquitination of cyclin-D1 (CCND1) and its subsequent proteasomal degradation (PubMed:18598945). However, it does not act as a major regulator of CCND1 stability during the G1/S transition (By similarity). Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 (PubMed:16275645, PubMed:20159592). Promotes ubiquitination of FXR1 following phosphorylation of FXR1 by GSK3B, leading to FXR1 degradation by the proteasome (PubMed:29142209). {ECO:0000250|UniProtKB:Q8CHQ0, ECO:0000269|PubMed:10531035, ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:29142209}. |
Q9Y2Z0 | SUGT1 | T10 | ochoa | Protein SGT1 homolog (Protein 40-6-3) (Sgt1) (Suppressor of G2 allele of SKP1 homolog) | May play a role in ubiquitination and subsequent proteasomal degradation of target proteins. |
Q9Y4P1 | ATG4B | T10 | ochoa | Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 1) (Autophagin-1) (Autophagy-related protein 4 homolog B) (HsAPG4B) (hAPG4B) | Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004, PubMed:26378241, PubMed:27527864, PubMed:28633005, PubMed:28821708, PubMed:29232556, PubMed:30076329, PubMed:30443548, PubMed:30661429). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed:33773106, PubMed:33909989). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:20818167, PubMed:21177865, PubMed:22302004, PubMed:27527864, PubMed:28287329, PubMed:28633005, PubMed:29458288, PubMed:30661429). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed:15169837, PubMed:15187094, PubMed:17347651, PubMed:19322194, PubMed:21177865, PubMed:22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed:31315929, PubMed:33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:15187094, PubMed:19322194, PubMed:28633005, PubMed:29458288, PubMed:32686895, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:15187094, PubMed:19322194, PubMed:29458288, PubMed:32686895, PubMed:33909989). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed:29458288, PubMed:30661429). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed:33773106). {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:22302004, ECO:0000269|PubMed:26378241, ECO:0000269|PubMed:27527864, ECO:0000269|PubMed:28287329, ECO:0000269|PubMed:28633005, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:29232556, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30076329, ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:32686895, ECO:0000269|PubMed:33773106, ECO:0000269|PubMed:33909989}. |
P08758 | ANXA5 | T10 | Sugiyama | Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CPB-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) | This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. |
Q16576 | RBBP7 | T10 | Sugiyama | Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46) | Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:28977666}. |
P25789 | PSMA4 | T10 | Sugiyama | Proteasome subunit alpha type-4 (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) (Proteasome subunit alpha-3) (alpha-3) | Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
A1L429 | GAGE12B; | Y10 | Sugiyama | G antigen 12B/C/D/E (GAGE-12B) (GAGE-12C) (GAGE-12D) (GAGE-12E) | None |
A6NDE8 | GAGE12H | Y10 | Sugiyama | G antigen 12H (GAGE-12H) | None |
A6NER3 | GAGE12J | Y10 | Sugiyama | G antigen 12J (GAGE-12J) | None |
O76087 | GAGE7 | Y10 | Sugiyama | G antigen 7 (GAGE-7) (AL4) (Cancer/testis antigen 4.7) (CT4.7) (GAGE-12I) (GAGE-7B) (GAGE-8) | None |
P0CL80 | GAGE12F | Y10 | Sugiyama | G antigen 12F (GAGE-12F) | None |
P0DSO3 | GAGE4 | Y10 | Sugiyama | G antigen 4 (Cancer/testis antigen 4.4) (CT4.4) | Antigen, recognized on melanoma by autologous cytolytic T-lymphocytes. {ECO:0000269|PubMed:7544395}. |
Q13069 | GAGE5 | Y10 | Sugiyama | G antigen 5 (GAGE-5) (Cancer/testis antigen 4.5) (CT4.5) | None |
Q13070 | GAGE6 | Y10 | Sugiyama | G antigen 6 (GAGE-6) (Cancer/testis antigen 4.6) (CT4.6) | None |
O43813 | LANCL1 | Y10 | Sugiyama | Glutathione S-transferase LANCL1 (EC 2.5.1.18) (40 kDa erythrocyte membrane protein) (p40) (LanC-like protein 1) | Functions as a glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione (PubMed:19528316). {ECO:0000250|UniProtKB:O89112, ECO:0000269|PubMed:19528316}. |
O75683 | SURF6 | Y10 | Sugiyama | Surfeit locus protein 6 | Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity). {ECO:0000250}. |
P31483 | TIA1 | Y10 | Sugiyama | Cytotoxic granule associated RNA binding protein TIA1 (Nucleolysin TIA-1 isoform p40) (RNA-binding protein TIA-1) (T-cell-restricted intracellular antigen-1) (TIA-1) (p40-TIA-1) | RNA-binding protein involved in the regulation of alternative pre-RNA splicing and mRNA translation by binding to uridine-rich (U-rich) RNA sequences (PubMed:11106748, PubMed:12486009, PubMed:17488725, PubMed:8576255). Binds to U-rich sequences immediately downstream from a 5' splice sites in a uridine-rich small nuclear ribonucleoprotein (U snRNP)-dependent fashion, thereby modulating alternative pre-RNA splicing (PubMed:11106748, PubMed:8576255). Preferably binds to the U-rich IAS1 sequence in a U1 snRNP-dependent manner; this binding is optimal if a 5' splice site is adjacent to IAS1 (By similarity). Activates the use of heterologous 5' splice sites; the activation depends on the intron sequence downstream from the 5' splice site, with a preference for a downstream U-rich sequence (PubMed:11106748). By interacting with SNRPC/U1-C, promotes recruitment and binding of spliceosomal U1 snRNP to 5' splice sites followed by U-rich sequences, thereby facilitating atypical 5' splice site recognition by U1 snRNP (PubMed:11106748, PubMed:12486009, PubMed:17488725). Activates splicing of alternative exons with weak 5' splice sites followed by a U-rich stretch on its own pre-mRNA and on TIAR mRNA (By similarity). Acts as a modulator of alternative splicing for the apoptotic FAS receptor, thereby promoting apoptosis (PubMed:11106748, PubMed:17488725, PubMed:1934064). Binds to the 5' splice site region of FAS intron 5 to promote accumulation of transcripts that include exon 6 at the expense of transcripts in which exon 6 is skipped, thereby leading to the transcription of a membrane-bound apoptotic FAS receptor, which promotes apoptosis (PubMed:11106748, PubMed:17488725, PubMed:1934064). Binds to a conserved AU-rich cis element in COL2A1 intron 2 and modulates alternative splicing of COL2A1 exon 2 (PubMed:17580305). Also binds to the equivalent AT-rich element in COL2A1 genomic DNA, and may thereby be involved in the regulation of transcription (PubMed:17580305). Binds specifically to a polypyrimidine-rich controlling element (PCE) located between the weak 5' splice site and the intronic splicing silencer of CFTR mRNA to promote exon 9 inclusion, thereby antagonizing PTB1 and its role in exon skipping of CFTR exon 9 (PubMed:14966131). Involved in the repression of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs), including target ARE-bearing mRNAs encoding TNF and PTGS2 (By similarity). Also participates in the cellular response to environmental stress, by acting downstream of the stress-induced phosphorylation of EIF2S1/EIF2A to promote the recruitment of untranslated mRNAs to cytoplasmic stress granules (SGs), leading to stress-induced translational arrest (PubMed:10613902). Formation and recruitment to SGs is regulated by Zn(2+) (By similarity). Possesses nucleolytic activity against cytotoxic lymphocyte target cells (PubMed:1934064). {ECO:0000250|UniProtKB:P52912, ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:11106748, ECO:0000269|PubMed:12486009, ECO:0000269|PubMed:14966131, ECO:0000269|PubMed:17488725, ECO:0000269|PubMed:17580305, ECO:0000269|PubMed:1934064, ECO:0000269|PubMed:8576255}.; FUNCTION: [Isoform Short]: Displays enhanced splicing regulatory activity compared with TIA isoform Long. {ECO:0000269|PubMed:17488725}. |
Q9NZD8 | SPG21 | Y10 | Sugiyama | Maspardin (Acid cluster protein 33) (Spastic paraplegia 21 autosomal recessive Mast syndrome protein) (Spastic paraplegia 21 protein) | May play a role as a negative regulatory factor in CD4-dependent T-cell activation. {ECO:0000269|PubMed:11113139}. |
Q9Y5K6 | CD2AP | Y10 | GPS6 | CD2-associated protein (Adapter protein CMS) (Cas ligand with multiple SH3 domains) | Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (PubMed:10339567). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis (PubMed:15800069). Plays a role in epithelial cell junctions formation (PubMed:22891260). {ECO:0000250|UniProtKB:F1LRS8, ECO:0000250|UniProtKB:Q9JLQ0, ECO:0000269|PubMed:10339567, ECO:0000269|PubMed:15800069, ECO:0000269|PubMed:22891260}. |
P62280 | RPS11 | Y10 | Sugiyama | Small ribosomal subunit protein uS17 (40S ribosomal protein S11) | Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. |
P51674 | GPM6A | T10 | GPS6|SIGNOR|ELM|iPTMNet|EPSD | Neuronal membrane glycoprotein M6-a (M6a) | Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. GPM6A-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor. {ECO:0000269|PubMed:19298174}. |
P21673 | SAT1 | T10 | ELM|iPTMNet | Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (SSAT) (SSAT-1) | Enzyme which catalyzes the acetylation of polyamines (PubMed:15283699, PubMed:16455797, PubMed:17516632). Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine (PubMed:17516632). This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines (PubMed:16455797). Also involved in the regulation of polyamine transport out of cells (PubMed:16455797). Also acts on 1,3-diaminopropane and 1,5-diaminopentane (PubMed:16455797, PubMed:17516632). {ECO:0000269|PubMed:15283699, ECO:0000269|PubMed:16455797, ECO:0000269|PubMed:17516632}. |
P22612 | PRKACG | T10 | Sugiyama | cAMP-dependent protein kinase catalytic subunit gamma (PKA C-gamma) (EC 2.7.11.11) | Phosphorylates a large number of substrates in the cytoplasm and the nucleus. |
Q96D96 | HVCN1 | T10 | SIGNOR | Voltage-gated hydrogen channel 1 (Hydrogen voltage-gated channel 1) (HV1) (Voltage sensor domain-only protein) | Voltage-gated proton-selective channel that conducts outward proton currents in response to intracellular acidification. Lacks a canonical ion-channel pore domain and mediates proton permeability via its voltage sensor domain (PubMed:16554753, PubMed:20037153, PubMed:20548053, PubMed:22020278, PubMed:27859356, PubMed:30478045, PubMed:37669933). Appears to play a dominant role in regulation of CO2/HCO3(-)/H(+) equilibrium in sperm flagellum. Prevents the acidification resulting from HCO3(-) synthesis and thus sustains high HCO3(-) levels inside sperm for capacitation (PubMed:20144758, PubMed:30478045, PubMed:37669933). Provides for proton efflux that compensates for electron charge generated by NADPH oxidase activity either in the extracellular or phagosomal compartments, thus enabling the production of high levels of bactericidal reactive oxygen species during the respiratory burst (PubMed:20037153, PubMed:30478045). Opens when the pH of airway surface liquid exceeds 7 and contributes to respiratory epithelial acid secretion to maintain pH in the mucosa (PubMed:20548053). {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:20144758, ECO:0000269|PubMed:20548053, ECO:0000269|PubMed:22020278, ECO:0000269|PubMed:27859356, ECO:0000269|PubMed:30478045, ECO:0000269|PubMed:37669933}. |
Download
reactome_id | name | p | -log10_p |
---|---|---|---|
R-HSA-69620 | Cell Cycle Checkpoints | 2.101501e-10 | 9.677 |
R-HSA-383280 | Nuclear Receptor transcription pathway | 3.976137e-08 | 7.401 |
R-HSA-72737 | Cap-dependent Translation Initiation | 1.937328e-07 | 6.713 |
R-HSA-72613 | Eukaryotic Translation Initiation | 1.937328e-07 | 6.713 |
R-HSA-9692914 | SARS-CoV-1-host interactions | 1.255487e-07 | 6.901 |
R-HSA-8953897 | Cellular responses to stimuli | 3.047102e-07 | 6.516 |
R-HSA-68882 | Mitotic Anaphase | 3.889494e-07 | 6.410 |
R-HSA-2555396 | Mitotic Metaphase and Anaphase | 4.279377e-07 | 6.369 |
R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 6.234688e-07 | 6.205 |
R-HSA-69481 | G2/M Checkpoints | 9.417799e-07 | 6.026 |
R-HSA-1640170 | Cell Cycle | 1.122025e-06 | 5.950 |
R-HSA-69278 | Cell Cycle, Mitotic | 1.256330e-06 | 5.901 |
R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 2.375006e-06 | 5.624 |
R-HSA-3700989 | Transcriptional Regulation by TP53 | 2.749510e-06 | 5.561 |
R-HSA-2467813 | Separation of Sister Chromatids | 2.815291e-06 | 5.550 |
R-HSA-9948299 | Ribosome-associated quality control | 4.273718e-06 | 5.369 |
R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 4.006520e-06 | 5.397 |
R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 4.290434e-06 | 5.367 |
R-HSA-2262752 | Cellular responses to stress | 4.930224e-06 | 5.307 |
R-HSA-72702 | Ribosomal scanning and start codon recognition | 5.417122e-06 | 5.266 |
R-HSA-8878159 | Transcriptional regulation by RUNX3 | 5.424917e-06 | 5.266 |
R-HSA-5610783 | Degradation of GLI2 by the proteasome | 6.222332e-06 | 5.206 |
R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 6.222332e-06 | 5.206 |
R-HSA-9013694 | Signaling by NOTCH4 | 6.495470e-06 | 5.187 |
R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 6.771838e-06 | 5.169 |
R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 7.759325e-06 | 5.110 |
R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 7.435401e-06 | 5.129 |
R-HSA-69206 | G1/S Transition | 7.637476e-06 | 5.117 |
R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 8.539016e-06 | 5.069 |
R-HSA-110314 | Recognition of DNA damage by PCNA-containing replication complex | 1.068338e-05 | 4.971 |
R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 1.069788e-05 | 4.971 |
R-HSA-68949 | Orc1 removal from chromatin | 1.157283e-05 | 4.937 |
R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 1.386231e-05 | 4.858 |
R-HSA-72689 | Formation of a pool of free 40S subunits | 1.438618e-05 | 4.842 |
R-HSA-376176 | Signaling by ROBO receptors | 1.501141e-05 | 4.824 |
R-HSA-72649 | Translation initiation complex formation | 1.654261e-05 | 4.781 |
R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 1.648698e-05 | 4.783 |
R-HSA-69541 | Stabilization of p53 | 1.648698e-05 | 4.783 |
R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 1.707714e-05 | 4.768 |
R-HSA-69615 | G1/S DNA Damage Checkpoints | 1.797322e-05 | 4.745 |
R-HSA-9755511 | KEAP1-NFE2L2 pathway | 1.791505e-05 | 4.747 |
R-HSA-69052 | Switching of origins to a post-replicative state | 2.142034e-05 | 4.669 |
R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 2.330576e-05 | 4.633 |
R-HSA-69275 | G2/M Transition | 2.373196e-05 | 4.625 |
R-HSA-212436 | Generic Transcription Pathway | 2.460558e-05 | 4.609 |
R-HSA-69002 | DNA Replication Pre-Initiation | 2.690472e-05 | 4.570 |
R-HSA-5610780 | Degradation of GLI1 by the proteasome | 3.025049e-05 | 4.519 |
R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 2.962707e-05 | 4.528 |
R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 2.962707e-05 | 4.528 |
R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 2.856758e-05 | 4.544 |
R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 2.856758e-05 | 4.544 |
R-HSA-9766229 | Degradation of CDH1 | 2.962707e-05 | 4.528 |
R-HSA-453274 | Mitotic G2-G2/M phases | 2.806143e-05 | 4.552 |
R-HSA-453279 | Mitotic G1 phase and G1/S transition | 3.091269e-05 | 4.510 |
R-HSA-6782135 | Dual incision in TC-NER | 3.238975e-05 | 4.490 |
R-HSA-69242 | S Phase | 3.727221e-05 | 4.429 |
R-HSA-5633007 | Regulation of TP53 Activity | 4.105336e-05 | 4.387 |
R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 4.364261e-05 | 4.360 |
R-HSA-73857 | RNA Polymerase II Transcription | 4.280323e-05 | 4.369 |
R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 4.754690e-05 | 4.323 |
R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 5.306707e-05 | 4.275 |
R-HSA-4641258 | Degradation of DVL | 5.345700e-05 | 4.272 |
R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 5.153816e-05 | 4.288 |
R-HSA-9706377 | FLT3 signaling by CBL mutants | 5.584927e-05 | 4.253 |
R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 6.141035e-05 | 4.212 |
R-HSA-453276 | Regulation of mitotic cell cycle | 5.929131e-05 | 4.227 |
R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 5.929131e-05 | 4.227 |
R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 6.024779e-05 | 4.220 |
R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 6.342306e-05 | 4.198 |
R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 6.342306e-05 | 4.198 |
R-HSA-9678108 | SARS-CoV-1 Infection | 6.192766e-05 | 4.208 |
R-HSA-68886 | M Phase | 6.937807e-05 | 4.159 |
R-HSA-69239 | Synthesis of DNA | 6.632041e-05 | 4.178 |
R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 7.547829e-05 | 4.122 |
R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 7.887231e-05 | 4.103 |
R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 8.034854e-05 | 4.095 |
R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 8.945773e-05 | 4.048 |
R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 9.374667e-05 | 4.028 |
R-HSA-156842 | Eukaryotic Translation Elongation | 9.514238e-05 | 4.022 |
R-HSA-1234174 | Cellular response to hypoxia | 9.310877e-05 | 4.031 |
R-HSA-8941858 | Regulation of RUNX3 expression and activity | 9.505191e-05 | 4.022 |
R-HSA-2559580 | Oxidative Stress Induced Senescence | 1.049405e-04 | 3.979 |
R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 1.120921e-04 | 3.950 |
R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 1.120921e-04 | 3.950 |
R-HSA-9764561 | Regulation of CDH1 Function | 1.090342e-04 | 3.962 |
R-HSA-5689877 | Josephin domain DUBs | 1.113094e-04 | 3.953 |
R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 1.139840e-04 | 3.943 |
R-HSA-180534 | Vpu mediated degradation of CD4 | 1.153865e-04 | 3.938 |
R-HSA-73893 | DNA Damage Bypass | 1.242015e-04 | 3.906 |
R-HSA-74160 | Gene expression (Transcription) | 1.218711e-04 | 3.914 |
R-HSA-109581 | Apoptosis | 1.258888e-04 | 3.900 |
R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 1.298788e-04 | 3.886 |
R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 1.335727e-04 | 3.874 |
R-HSA-5696400 | Dual Incision in GG-NER | 1.405593e-04 | 3.852 |
R-HSA-9932298 | Degradation of CRY and PER proteins | 1.360387e-04 | 3.866 |
R-HSA-5696398 | Nucleotide Excision Repair | 1.598777e-04 | 3.796 |
R-HSA-5658442 | Regulation of RAS by GAPs | 1.455322e-04 | 3.837 |
R-HSA-9758274 | Regulation of NF-kappa B signaling | 1.657216e-04 | 3.781 |
R-HSA-9706369 | Negative regulation of FLT3 | 1.657216e-04 | 3.781 |
R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 1.654829e-04 | 3.781 |
R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 1.699224e-04 | 3.770 |
R-HSA-2559585 | Oncogene Induced Senescence | 1.702123e-04 | 3.769 |
R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 1.702123e-04 | 3.769 |
R-HSA-169911 | Regulation of Apoptosis | 1.702123e-04 | 3.769 |
R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 1.977213e-04 | 3.704 |
R-HSA-72766 | Translation | 1.991890e-04 | 3.701 |
R-HSA-8939902 | Regulation of RUNX2 expression and activity | 1.936854e-04 | 3.713 |
R-HSA-5656169 | Termination of translesion DNA synthesis | 2.037677e-04 | 3.691 |
R-HSA-6804757 | Regulation of TP53 Degradation | 2.049610e-04 | 3.688 |
R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 2.220472e-04 | 3.654 |
R-HSA-2559583 | Cellular Senescence | 2.243117e-04 | 3.649 |
R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 2.293071e-04 | 3.640 |
R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 2.634457e-04 | 3.579 |
R-HSA-69618 | Mitotic Spindle Checkpoint | 2.528074e-04 | 3.597 |
R-HSA-4641257 | Degradation of AXIN | 2.454785e-04 | 3.610 |
R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 2.650878e-04 | 3.577 |
R-HSA-9711123 | Cellular response to chemical stress | 2.860256e-04 | 3.544 |
R-HSA-8948747 | Regulation of PTEN localization | 2.894670e-04 | 3.538 |
R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 3.087196e-04 | 3.510 |
R-HSA-68867 | Assembly of the pre-replicative complex | 3.256262e-04 | 3.487 |
R-HSA-8953854 | Metabolism of RNA | 3.327263e-04 | 3.478 |
R-HSA-8866427 | VLDLR internalisation and degradation | 3.359132e-04 | 3.474 |
R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 3.386027e-04 | 3.470 |
R-HSA-141424 | Amplification of signal from the kinetochores | 3.752964e-04 | 3.426 |
R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 3.752964e-04 | 3.426 |
R-HSA-69306 | DNA Replication | 3.802465e-04 | 3.420 |
R-HSA-9613829 | Chaperone Mediated Autophagy | 3.818089e-04 | 3.418 |
R-HSA-162909 | Host Interactions of HIV factors | 4.169844e-04 | 3.380 |
R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 4.181071e-04 | 3.379 |
R-HSA-72764 | Eukaryotic Translation Termination | 4.425123e-04 | 3.354 |
R-HSA-9828211 | Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation | 4.452899e-04 | 3.351 |
R-HSA-3785653 | Myoclonic epilepsy of Lafora | 4.452899e-04 | 3.351 |
R-HSA-8849469 | PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 | 4.452899e-04 | 3.351 |
R-HSA-174048 | APC/C:Cdc20 mediated degradation of Cyclin B | 4.902994e-04 | 3.310 |
R-HSA-174490 | Membrane binding and targetting of GAG proteins | 4.610958e-04 | 3.336 |
R-HSA-9612973 | Autophagy | 4.776076e-04 | 3.321 |
R-HSA-5362768 | Hh mutants are degraded by ERAD | 4.808564e-04 | 3.318 |
R-HSA-9607240 | FLT3 Signaling | 4.808564e-04 | 3.318 |
R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 4.808564e-04 | 3.318 |
R-HSA-156902 | Peptide chain elongation | 5.163973e-04 | 3.287 |
R-HSA-913531 | Interferon Signaling | 5.323566e-04 | 3.274 |
R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 5.486621e-04 | 3.261 |
R-HSA-69202 | Cyclin E associated events during G1/S transition | 6.061649e-04 | 3.217 |
R-HSA-174495 | Synthesis And Processing Of GAG, GAGPOL Polyproteins | 6.199350e-04 | 3.208 |
R-HSA-1169091 | Activation of NF-kappaB in B cells | 6.376597e-04 | 3.195 |
R-HSA-3315487 | SMAD2/3 MH2 Domain Mutants in Cancer | 7.000159e-04 | 3.155 |
R-HSA-3311021 | SMAD4 MH2 Domain Mutants in Cancer | 7.000159e-04 | 3.155 |
R-HSA-3304347 | Loss of Function of SMAD4 in Cancer | 7.000159e-04 | 3.155 |
R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 7.005217e-04 | 3.155 |
R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 7.299770e-04 | 3.137 |
R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 7.619250e-04 | 3.118 |
R-HSA-5610787 | Hedgehog 'off' state | 7.175257e-04 | 3.144 |
R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 7.603567e-04 | 3.119 |
R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 7.299770e-04 | 3.137 |
R-HSA-5387390 | Hh mutants abrogate ligand secretion | 7.603567e-04 | 3.119 |
R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 7.619250e-04 | 3.118 |
R-HSA-9020702 | Interleukin-1 signaling | 7.872362e-04 | 3.104 |
R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 8.023181e-04 | 3.096 |
R-HSA-1295596 | Spry regulation of FGF signaling | 8.182187e-04 | 3.087 |
R-HSA-110312 | Translesion synthesis by REV1 | 8.182187e-04 | 3.087 |
R-HSA-8875360 | InlB-mediated entry of Listeria monocytogenes into host cell | 8.182187e-04 | 3.087 |
R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 8.366549e-04 | 3.077 |
R-HSA-5696397 | Gap-filling DNA repair synthesis and ligation in GG-NER | 9.690321e-04 | 3.014 |
R-HSA-9615710 | Late endosomal microautophagy | 9.639802e-04 | 3.016 |
R-HSA-8876384 | Listeria monocytogenes entry into host cells | 9.690321e-04 | 3.014 |
R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 9.690321e-04 | 3.014 |
R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 9.085984e-04 | 3.042 |
R-HSA-9617828 | FOXO-mediated transcription of cell cycle genes | 9.690321e-04 | 3.014 |
R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 1.012225e-03 | 2.995 |
R-HSA-4608870 | Asymmetric localization of PCP proteins | 1.012225e-03 | 2.995 |
R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 1.012225e-03 | 2.995 |
R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 1.028534e-03 | 2.988 |
R-HSA-5689896 | Ovarian tumor domain proteases | 1.028534e-03 | 2.988 |
R-HSA-162906 | HIV Infection | 1.039878e-03 | 2.983 |
R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 1.047337e-03 | 2.980 |
R-HSA-1169408 | ISG15 antiviral mechanism | 1.057779e-03 | 2.976 |
R-HSA-5656121 | Translesion synthesis by POLI | 1.062155e-03 | 2.974 |
R-HSA-168255 | Influenza Infection | 1.101577e-03 | 2.958 |
R-HSA-5689603 | UCH proteinases | 1.175549e-03 | 2.930 |
R-HSA-9694493 | Maturation of protein E | 1.180645e-03 | 2.928 |
R-HSA-9683683 | Maturation of protein E | 1.180645e-03 | 2.928 |
R-HSA-5688426 | Deubiquitination | 1.185793e-03 | 2.926 |
R-HSA-166208 | mTORC1-mediated signalling | 1.191809e-03 | 2.924 |
R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 1.191809e-03 | 2.924 |
R-HSA-5357801 | Programmed Cell Death | 1.258592e-03 | 2.900 |
R-HSA-8876493 | InlA-mediated entry of Listeria monocytogenes into host cells | 1.296386e-03 | 2.887 |
R-HSA-5655862 | Translesion synthesis by POLK | 1.358337e-03 | 2.867 |
R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 1.444032e-03 | 2.840 |
R-HSA-9645460 | Alpha-protein kinase 1 signaling pathway | 1.296386e-03 | 2.887 |
R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 1.358337e-03 | 2.867 |
R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 1.359141e-03 | 2.867 |
R-HSA-9711097 | Cellular response to starvation | 1.288286e-03 | 2.890 |
R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 1.456069e-03 | 2.837 |
R-HSA-9700206 | Signaling by ALK in cancer | 1.456069e-03 | 2.837 |
R-HSA-9833109 | Evasion by RSV of host interferon responses | 1.365225e-03 | 2.865 |
R-HSA-5696395 | Formation of Incision Complex in GG-NER | 1.608738e-03 | 2.794 |
R-HSA-8982491 | Glycogen metabolism | 1.608738e-03 | 2.794 |
R-HSA-1236974 | ER-Phagosome pathway | 1.626892e-03 | 2.789 |
R-HSA-6807070 | PTEN Regulation | 1.705526e-03 | 2.768 |
R-HSA-3229121 | Glycogen storage diseases | 1.713702e-03 | 2.766 |
R-HSA-9824878 | Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 | 1.748830e-03 | 2.757 |
R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 1.748830e-03 | 2.757 |
R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 1.809769e-03 | 2.742 |
R-HSA-110313 | Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa... | 1.851931e-03 | 2.732 |
R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 1.874068e-03 | 2.727 |
R-HSA-73894 | DNA Repair | 2.054828e-03 | 2.687 |
R-HSA-5693532 | DNA Double-Strand Break Repair | 2.079809e-03 | 2.682 |
R-HSA-2408557 | Selenocysteine synthesis | 2.091214e-03 | 2.680 |
R-HSA-1296041 | Activation of G protein gated Potassium channels | 2.107059e-03 | 2.676 |
R-HSA-997272 | Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits | 2.107059e-03 | 2.676 |
R-HSA-1296059 | G protein gated Potassium channels | 2.107059e-03 | 2.676 |
R-HSA-192823 | Viral mRNA Translation | 2.465611e-03 | 2.608 |
R-HSA-163359 | Glucagon signaling in metabolic regulation | 2.204433e-03 | 2.657 |
R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 2.549825e-03 | 2.593 |
R-HSA-5696394 | DNA Damage Recognition in GG-NER | 2.204433e-03 | 2.657 |
R-HSA-937039 | IRAK1 recruits IKK complex | 2.307375e-03 | 2.637 |
R-HSA-975144 | IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation | 2.307375e-03 | 2.637 |
R-HSA-9705683 | SARS-CoV-2-host interactions | 2.236492e-03 | 2.650 |
R-HSA-209543 | p75NTR recruits signalling complexes | 2.307375e-03 | 2.637 |
R-HSA-5358346 | Hedgehog ligand biogenesis | 2.202672e-03 | 2.657 |
R-HSA-5205647 | Mitophagy | 2.559751e-03 | 2.592 |
R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 2.559751e-03 | 2.592 |
R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 2.570517e-03 | 2.590 |
R-HSA-68877 | Mitotic Prometaphase | 2.580250e-03 | 2.588 |
R-HSA-912631 | Regulation of signaling by CBL | 2.631205e-03 | 2.580 |
R-HSA-937041 | IKK complex recruitment mediated by RIP1 | 2.631205e-03 | 2.580 |
R-HSA-110320 | Translesion Synthesis by POLH | 2.631205e-03 | 2.580 |
R-HSA-72163 | mRNA Splicing - Major Pathway | 2.731231e-03 | 2.564 |
R-HSA-8948751 | Regulation of PTEN stability and activity | 2.786992e-03 | 2.555 |
R-HSA-5687128 | MAPK6/MAPK4 signaling | 2.814299e-03 | 2.551 |
R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 2.968518e-03 | 2.527 |
R-HSA-2559584 | Formation of Senescence-Associated Heterochromatin Foci (SAHF) | 2.985521e-03 | 2.525 |
R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 2.994431e-03 | 2.524 |
R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 3.076640e-03 | 2.512 |
R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 3.122324e-03 | 2.506 |
R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 3.129928e-03 | 2.504 |
R-HSA-69231 | Cyclin D associated events in G1 | 3.133500e-03 | 2.504 |
R-HSA-69236 | G1 Phase | 3.133500e-03 | 2.504 |
R-HSA-3322077 | Glycogen synthesis | 3.208544e-03 | 2.494 |
R-HSA-6807004 | Negative regulation of MET activity | 3.208544e-03 | 2.494 |
R-HSA-179409 | APC-Cdc20 mediated degradation of Nek2A | 3.875373e-03 | 2.412 |
R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 3.871934e-03 | 2.412 |
R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 3.899267e-03 | 2.409 |
R-HSA-6783310 | Fanconi Anemia Pathway | 3.543291e-03 | 2.451 |
R-HSA-432040 | Vasopressin regulates renal water homeostasis via Aquaporins | 3.543291e-03 | 2.451 |
R-HSA-205043 | NRIF signals cell death from the nucleus | 3.796869e-03 | 2.421 |
R-HSA-5684264 | MAP3K8 (TPL2)-dependent MAPK1/3 activation | 3.796869e-03 | 2.421 |
R-HSA-1253288 | Downregulation of ERBB4 signaling | 3.699366e-03 | 2.432 |
R-HSA-9637628 | Modulation by Mtb of host immune system | 3.699366e-03 | 2.432 |
R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 3.592198e-03 | 2.445 |
R-HSA-5693538 | Homology Directed Repair | 3.964391e-03 | 2.402 |
R-HSA-5357905 | Regulation of TNFR1 signaling | 3.993996e-03 | 2.399 |
R-HSA-4086400 | PCP/CE pathway | 4.065175e-03 | 2.391 |
R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 4.154451e-03 | 2.381 |
R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 4.154451e-03 | 2.381 |
R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 4.154451e-03 | 2.381 |
R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 4.238053e-03 | 2.373 |
R-HSA-8878166 | Transcriptional regulation by RUNX2 | 4.253189e-03 | 2.371 |
R-HSA-446652 | Interleukin-1 family signaling | 4.277494e-03 | 2.369 |
R-HSA-1632852 | Macroautophagy | 4.405880e-03 | 2.356 |
R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 4.559989e-03 | 2.341 |
R-HSA-166166 | MyD88-independent TLR4 cascade | 4.559989e-03 | 2.341 |
R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 4.639663e-03 | 2.334 |
R-HSA-175474 | Assembly Of The HIV Virion | 4.639663e-03 | 2.334 |
R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 4.639663e-03 | 2.334 |
R-HSA-68962 | Activation of the pre-replicative complex | 4.735990e-03 | 2.325 |
R-HSA-937072 | TRAF6-mediated induction of TAK1 complex within TLR4 complex | 4.754987e-03 | 2.323 |
R-HSA-8964315 | G beta:gamma signalling through BTK | 4.754987e-03 | 2.323 |
R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 4.754987e-03 | 2.323 |
R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 4.754987e-03 | 2.323 |
R-HSA-168927 | TICAM1, RIP1-mediated IKK complex recruitment | 4.754987e-03 | 2.323 |
R-HSA-193639 | p75NTR signals via NF-kB | 4.754987e-03 | 2.323 |
R-HSA-2644607 | Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling | 4.945553e-03 | 2.306 |
R-HSA-2644605 | FBXW7 Mutants and NOTCH1 in Cancer | 4.945553e-03 | 2.306 |
R-HSA-5693607 | Processing of DNA double-strand break ends | 5.287490e-03 | 2.277 |
R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 6.145356e-03 | 2.211 |
R-HSA-72172 | mRNA Splicing | 4.945696e-03 | 2.306 |
R-HSA-182971 | EGFR downregulation | 5.472652e-03 | 2.262 |
R-HSA-937042 | IRAK2 mediated activation of TAK1 complex | 5.015242e-03 | 2.300 |
R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 5.472652e-03 | 2.262 |
R-HSA-2465910 | MASTL Facilitates Mitotic Progression | 5.015242e-03 | 2.300 |
R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 5.646879e-03 | 2.248 |
R-HSA-201681 | TCF dependent signaling in response to WNT | 6.150540e-03 | 2.211 |
R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 5.865151e-03 | 2.232 |
R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 5.865151e-03 | 2.232 |
R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 5.865151e-03 | 2.232 |
R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 5.865151e-03 | 2.232 |
R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 5.865151e-03 | 2.232 |
R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 5.618896e-03 | 2.250 |
R-HSA-9708530 | Regulation of BACH1 activity | 5.873280e-03 | 2.231 |
R-HSA-5632684 | Hedgehog 'on' state | 5.886316e-03 | 2.230 |
R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 6.253213e-03 | 2.204 |
R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 6.291943e-03 | 2.201 |
R-HSA-1296065 | Inwardly rectifying K+ channels | 6.291943e-03 | 2.201 |
R-HSA-8853884 | Transcriptional Regulation by VENTX | 6.458364e-03 | 2.190 |
R-HSA-450294 | MAP kinase activation | 6.463999e-03 | 2.189 |
R-HSA-392451 | G beta:gamma signalling through PI3Kgamma | 6.492754e-03 | 2.188 |
R-HSA-9860931 | Response of endothelial cells to shear stress | 6.517032e-03 | 2.186 |
R-HSA-140342 | Apoptosis induced DNA fragmentation | 6.612873e-03 | 2.180 |
R-HSA-9014325 | TICAM1,TRAF6-dependent induction of TAK1 complex | 6.612873e-03 | 2.180 |
R-HSA-9664873 | Pexophagy | 6.612873e-03 | 2.180 |
R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 6.851458e-03 | 2.164 |
R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 6.933888e-03 | 2.159 |
R-HSA-3858494 | Beta-catenin independent WNT signaling | 7.009819e-03 | 2.154 |
R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 7.024545e-03 | 2.153 |
R-HSA-9912633 | Antigen processing: Ub, ATP-independent proteasomal degradation | 7.164863e-03 | 2.145 |
R-HSA-8964616 | G beta:gamma signalling through CDC42 | 7.164863e-03 | 2.145 |
R-HSA-975110 | TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling | 7.164863e-03 | 2.145 |
R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 7.164863e-03 | 2.145 |
R-HSA-5689880 | Ub-specific processing proteases | 7.228557e-03 | 2.141 |
R-HSA-9675108 | Nervous system development | 7.346335e-03 | 2.134 |
R-HSA-909733 | Interferon alpha/beta signaling | 7.411624e-03 | 2.130 |
R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 7.536441e-03 | 2.123 |
R-HSA-991365 | Activation of GABAB receptors | 8.137270e-03 | 2.090 |
R-HSA-977444 | GABA B receptor activation | 8.137270e-03 | 2.090 |
R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 8.137270e-03 | 2.090 |
R-HSA-165159 | MTOR signalling | 8.137270e-03 | 2.090 |
R-HSA-933543 | NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 | 8.515670e-03 | 2.070 |
R-HSA-1660517 | Synthesis of PIPs at the late endosome membrane | 8.642455e-03 | 2.063 |
R-HSA-195721 | Signaling by WNT | 8.664773e-03 | 2.062 |
R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 8.679784e-03 | 2.061 |
R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 9.215641e-03 | 2.035 |
R-HSA-1236975 | Antigen processing-Cross presentation | 9.215641e-03 | 2.035 |
R-HSA-9006925 | Intracellular signaling by second messengers | 9.228602e-03 | 2.035 |
R-HSA-168638 | NOD1/2 Signaling Pathway | 9.299477e-03 | 2.032 |
R-HSA-1980145 | Signaling by NOTCH2 | 9.299477e-03 | 2.032 |
R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 9.848140e-03 | 2.007 |
R-HSA-9907900 | Proteasome assembly | 1.012388e-02 | 1.995 |
R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 1.079709e-02 | 1.967 |
R-HSA-418217 | G beta:gamma signalling through PLC beta | 1.031828e-02 | 1.986 |
R-HSA-8866652 | Synthesis of active ubiquitin: roles of E1 and E2 enzymes | 1.171951e-02 | 1.931 |
R-HSA-167287 | HIV elongation arrest and recovery | 1.338788e-02 | 1.873 |
R-HSA-167290 | Pausing and recovery of HIV elongation | 1.338788e-02 | 1.873 |
R-HSA-5689901 | Metalloprotease DUBs | 1.020329e-02 | 1.991 |
R-HSA-8951664 | Neddylation | 1.114993e-02 | 1.953 |
R-HSA-5654732 | Negative regulation of FGFR3 signaling | 1.338788e-02 | 1.873 |
R-HSA-6804760 | Regulation of TP53 Activity through Methylation | 1.031828e-02 | 1.986 |
R-HSA-9660821 | ADORA2B mediated anti-inflammatory cytokines production | 1.124234e-02 | 1.949 |
R-HSA-202424 | Downstream TCR signaling | 1.158354e-02 | 1.936 |
R-HSA-8941855 | RUNX3 regulates CDKN1A transcription | 1.079709e-02 | 1.967 |
R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 1.031828e-02 | 1.986 |
R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 1.020329e-02 | 1.991 |
R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 1.171951e-02 | 1.931 |
R-HSA-1358803 | Downregulation of ERBB2:ERBB3 signaling | 1.331950e-02 | 1.876 |
R-HSA-2980766 | Nuclear Envelope Breakdown | 1.245891e-02 | 1.905 |
R-HSA-75893 | TNF signaling | 1.137001e-02 | 1.944 |
R-HSA-392851 | Prostacyclin signalling through prostacyclin receptor | 1.220396e-02 | 1.913 |
R-HSA-5693606 | DNA Double Strand Break Response | 1.111345e-02 | 1.954 |
R-HSA-500657 | Presynaptic function of Kainate receptors | 1.031828e-02 | 1.986 |
R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 1.240746e-02 | 1.906 |
R-HSA-156711 | Polo-like kinase mediated events | 1.031828e-02 | 1.986 |
R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 1.240746e-02 | 1.906 |
R-HSA-9861718 | Regulation of pyruvate metabolism | 1.244941e-02 | 1.905 |
R-HSA-9855142 | Cellular responses to mechanical stimuli | 1.353791e-02 | 1.868 |
R-HSA-2691232 | Constitutive Signaling by NOTCH1 HD Domain Mutants | 1.331950e-02 | 1.876 |
R-HSA-2691230 | Signaling by NOTCH1 HD Domain Mutants in Cancer | 1.331950e-02 | 1.876 |
R-HSA-75153 | Apoptotic execution phase | 1.244941e-02 | 1.905 |
R-HSA-209560 | NF-kB is activated and signals survival | 1.074489e-02 | 1.969 |
R-HSA-382556 | ABC-family proteins mediated transport | 1.147216e-02 | 1.940 |
R-HSA-9614085 | FOXO-mediated transcription | 1.071651e-02 | 1.970 |
R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 1.374892e-02 | 1.862 |
R-HSA-422475 | Axon guidance | 1.400018e-02 | 1.854 |
R-HSA-389948 | Co-inhibition by PD-1 | 1.412950e-02 | 1.850 |
R-HSA-448424 | Interleukin-17 signaling | 1.422315e-02 | 1.847 |
R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 1.422315e-02 | 1.847 |
R-HSA-1280215 | Cytokine Signaling in Immune system | 1.457650e-02 | 1.836 |
R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 1.486695e-02 | 1.828 |
R-HSA-388841 | Regulation of T cell activation by CD28 family | 1.511958e-02 | 1.820 |
R-HSA-9634597 | GPER1 signaling | 1.514465e-02 | 1.820 |
R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 1.520060e-02 | 1.818 |
R-HSA-917729 | Endosomal Sorting Complex Required For Transport (ESCRT) | 1.521549e-02 | 1.818 |
R-HSA-5654733 | Negative regulation of FGFR4 signaling | 1.521549e-02 | 1.818 |
R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 1.521549e-02 | 1.818 |
R-HSA-9796292 | Formation of axial mesoderm | 1.625608e-02 | 1.789 |
R-HSA-5358351 | Signaling by Hedgehog | 1.631263e-02 | 1.787 |
R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 1.646300e-02 | 1.783 |
R-HSA-8964043 | Plasma lipoprotein clearance | 1.646300e-02 | 1.783 |
R-HSA-8953750 | Transcriptional Regulation by E2F6 | 1.646300e-02 | 1.783 |
R-HSA-202040 | G-protein activation | 1.664800e-02 | 1.779 |
R-HSA-392170 | ADP signalling through P2Y purinoceptor 12 | 1.664800e-02 | 1.779 |
R-HSA-450321 | JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ... | 1.664800e-02 | 1.779 |
R-HSA-2979096 | NOTCH2 Activation and Transmission of Signal to the Nucleus | 1.664800e-02 | 1.779 |
R-HSA-210991 | Basigin interactions | 1.664800e-02 | 1.779 |
R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 1.664800e-02 | 1.779 |
R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 1.664800e-02 | 1.779 |
R-HSA-2408522 | Selenoamino acid metabolism | 1.670258e-02 | 1.777 |
R-HSA-445717 | Aquaporin-mediated transport | 1.760147e-02 | 1.754 |
R-HSA-9646399 | Aggrephagy | 1.826435e-02 | 1.738 |
R-HSA-9679506 | SARS-CoV Infections | 1.829101e-02 | 1.738 |
R-HSA-9609507 | Protein localization | 1.878053e-02 | 1.726 |
R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 1.922601e-02 | 1.716 |
R-HSA-69473 | G2/M DNA damage checkpoint | 1.932660e-02 | 1.714 |
R-HSA-162588 | Budding and maturation of HIV virion | 1.937530e-02 | 1.713 |
R-HSA-139915 | Activation of PUMA and translocation to mitochondria | 1.943248e-02 | 1.711 |
R-HSA-975163 | IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation | 1.956878e-02 | 1.708 |
R-HSA-1433559 | Regulation of KIT signaling | 1.956878e-02 | 1.708 |
R-HSA-73887 | Death Receptor Signaling | 1.972388e-02 | 1.705 |
R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 2.019978e-02 | 1.695 |
R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 2.039529e-02 | 1.690 |
R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 2.039529e-02 | 1.690 |
R-HSA-373755 | Semaphorin interactions | 2.068528e-02 | 1.684 |
R-HSA-8848021 | Signaling by PTK6 | 2.068528e-02 | 1.684 |
R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 2.068528e-02 | 1.684 |
R-HSA-8939211 | ESR-mediated signaling | 2.164381e-02 | 1.665 |
R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 2.165363e-02 | 1.664 |
R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 2.172008e-02 | 1.663 |
R-HSA-6804754 | Regulation of TP53 Expression | 2.172036e-02 | 1.663 |
R-HSA-9630747 | Diseases of Cellular Senescence | 2.172036e-02 | 1.663 |
R-HSA-9675132 | Diseases of cellular response to stress | 2.172036e-02 | 1.663 |
R-HSA-9013507 | NOTCH3 Activation and Transmission of Signal to the Nucleus | 2.205307e-02 | 1.657 |
R-HSA-1257604 | PIP3 activates AKT signaling | 2.225925e-02 | 1.652 |
R-HSA-1980143 | Signaling by NOTCH1 | 2.232998e-02 | 1.651 |
R-HSA-162587 | HIV Life Cycle | 2.277255e-02 | 1.643 |
R-HSA-9663891 | Selective autophagy | 2.335558e-02 | 1.632 |
R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 2.340762e-02 | 1.631 |
R-HSA-193704 | p75 NTR receptor-mediated signalling | 2.390870e-02 | 1.621 |
R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 2.402720e-02 | 1.619 |
R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 2.402720e-02 | 1.619 |
R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 2.424918e-02 | 1.615 |
R-HSA-397795 | G-protein beta:gamma signalling | 2.424918e-02 | 1.615 |
R-HSA-5654726 | Negative regulation of FGFR1 signaling | 2.424918e-02 | 1.615 |
R-HSA-176187 | Activation of ATR in response to replication stress | 2.424918e-02 | 1.615 |
R-HSA-5675482 | Regulation of necroptotic cell death | 2.424918e-02 | 1.615 |
R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 2.424918e-02 | 1.615 |
R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 2.449041e-02 | 1.611 |
R-HSA-5674400 | Constitutive Signaling by AKT1 E17K in Cancer | 2.513686e-02 | 1.600 |
R-HSA-5619084 | ABC transporter disorders | 2.565801e-02 | 1.591 |
R-HSA-9764265 | Regulation of CDH1 Expression and Function | 2.646972e-02 | 1.577 |
R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 2.646972e-02 | 1.577 |
R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 2.696790e-02 | 1.569 |
R-HSA-9818027 | NFE2L2 regulating anti-oxidant/detoxification enzymes | 2.696790e-02 | 1.569 |
R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 2.822309e-02 | 1.549 |
R-HSA-428930 | Thromboxane signalling through TP receptor | 2.848417e-02 | 1.545 |
R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 2.848417e-02 | 1.545 |
R-HSA-5654738 | Signaling by FGFR2 | 2.932742e-02 | 1.533 |
R-HSA-9833482 | PKR-mediated signaling | 2.932742e-02 | 1.533 |
R-HSA-9927426 | Developmental Lineage of Mammary Gland Alveolar Cells | 2.988110e-02 | 1.525 |
R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 2.988110e-02 | 1.525 |
R-HSA-5654727 | Negative regulation of FGFR2 signaling | 2.988110e-02 | 1.525 |
R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 3.020158e-02 | 1.520 |
R-HSA-177929 | Signaling by EGFR | 3.020158e-02 | 1.520 |
R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 4.534810e-02 | 1.343 |
R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 4.534810e-02 | 1.343 |
R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 4.534810e-02 | 1.343 |
R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 4.016091e-02 | 1.396 |
R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 4.016091e-02 | 1.396 |
R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 4.171974e-02 | 1.380 |
R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 3.944444e-02 | 1.404 |
R-HSA-5628897 | TP53 Regulates Metabolic Genes | 3.165248e-02 | 1.500 |
R-HSA-162599 | Late Phase of HIV Life Cycle | 4.009152e-02 | 1.397 |
R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 3.599178e-02 | 1.444 |
R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 4.470738e-02 | 1.350 |
R-HSA-1660516 | Synthesis of PIPs at the early endosome membrane | 3.210085e-02 | 1.493 |
R-HSA-977443 | GABA receptor activation | 4.065218e-02 | 1.391 |
R-HSA-68875 | Mitotic Prophase | 4.280538e-02 | 1.369 |
R-HSA-2028269 | Signaling by Hippo | 3.677914e-02 | 1.434 |
R-HSA-3371556 | Cellular response to heat stress | 4.490178e-02 | 1.348 |
R-HSA-4839744 | Signaling by APC mutants | 4.534810e-02 | 1.343 |
R-HSA-4641263 | Regulation of FZD by ubiquitination | 3.677914e-02 | 1.434 |
R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 3.335399e-02 | 1.477 |
R-HSA-8943724 | Regulation of PTEN gene transcription | 4.065218e-02 | 1.391 |
R-HSA-111885 | Opioid Signalling | 3.193057e-02 | 1.496 |
R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 4.099680e-02 | 1.387 |
R-HSA-5213460 | RIPK1-mediated regulated necrosis | 4.355954e-02 | 1.361 |
R-HSA-2122948 | Activated NOTCH1 Transmits Signal to the Nucleus | 3.599178e-02 | 1.444 |
R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 3.944444e-02 | 1.404 |
R-HSA-9637687 | Suppression of phagosomal maturation | 3.599178e-02 | 1.444 |
R-HSA-451326 | Activation of kainate receptors upon glutamate binding | 4.461122e-02 | 1.351 |
R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 3.775237e-02 | 1.423 |
R-HSA-1643713 | Signaling by EGFR in Cancer | 3.599178e-02 | 1.444 |
R-HSA-8952158 | RUNX3 regulates BCL2L11 (BIM) transcription | 4.543365e-02 | 1.343 |
R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 4.543365e-02 | 1.343 |
R-HSA-205025 | NADE modulates death signalling | 4.543365e-02 | 1.343 |
R-HSA-9022927 | MECP2 regulates transcription of genes involved in GABA signaling | 4.543365e-02 | 1.343 |
R-HSA-202403 | TCR signaling | 4.616554e-02 | 1.336 |
R-HSA-9694516 | SARS-CoV-2 Infection | 4.727530e-02 | 1.325 |
R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 4.750153e-02 | 1.323 |
R-HSA-917937 | Iron uptake and transport | 4.766162e-02 | 1.322 |
R-HSA-390466 | Chaperonin-mediated protein folding | 4.771698e-02 | 1.321 |
R-HSA-167242 | Abortive elongation of HIV-1 transcript in the absence of Tat | 4.783365e-02 | 1.320 |
R-HSA-844456 | The NLRP3 inflammasome | 4.783365e-02 | 1.320 |
R-HSA-113510 | E2F mediated regulation of DNA replication | 4.783365e-02 | 1.320 |
R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 4.934477e-02 | 1.307 |
R-HSA-420092 | Glucagon-type ligand receptors | 4.934477e-02 | 1.307 |
R-HSA-9645723 | Diseases of programmed cell death | 5.045983e-02 | 1.297 |
R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 5.165712e-02 | 1.287 |
R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 5.165712e-02 | 1.287 |
R-HSA-418990 | Adherens junctions interactions | 5.198011e-02 | 1.284 |
R-HSA-2514853 | Condensation of Prometaphase Chromosomes | 5.357985e-02 | 1.271 |
R-HSA-5339716 | Signaling by GSK3beta mutants | 5.357985e-02 | 1.271 |
R-HSA-4839748 | Signaling by AMER1 mutants | 5.357985e-02 | 1.271 |
R-HSA-4839735 | Signaling by AXIN mutants | 5.357985e-02 | 1.271 |
R-HSA-9609523 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane | 5.397636e-02 | 1.268 |
R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 5.436266e-02 | 1.265 |
R-HSA-9723907 | Loss of Function of TP53 in Cancer | 5.459356e-02 | 1.263 |
R-HSA-9646303 | Evasion of Oncogene Induced Senescence Due to p14ARF Defects | 5.459356e-02 | 1.263 |
R-HSA-9723905 | Loss of function of TP53 in cancer due to loss of tetramerization ability | 5.459356e-02 | 1.263 |
R-HSA-9646304 | Evasion of Oxidative Stress Induced Senescence Due to p14ARF Defects | 5.459356e-02 | 1.263 |
R-HSA-9009391 | Extra-nuclear estrogen signaling | 5.501978e-02 | 1.259 |
R-HSA-112382 | Formation of RNA Pol II elongation complex | 5.526890e-02 | 1.258 |
R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 5.677025e-02 | 1.246 |
R-HSA-416482 | G alpha (12/13) signalling events | 5.694047e-02 | 1.245 |
R-HSA-75955 | RNA Polymerase II Transcription Elongation | 5.926426e-02 | 1.227 |
R-HSA-3134963 | DEx/H-box helicases activate type I IFN and inflammatory cytokines production | 5.964204e-02 | 1.224 |
R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 5.964204e-02 | 1.224 |
R-HSA-9818025 | NFE2L2 regulating TCA cycle genes | 5.964204e-02 | 1.224 |
R-HSA-5250971 | Toxicity of botulinum toxin type C (botC) | 5.964204e-02 | 1.224 |
R-HSA-8854518 | AURKA Activation by TPX2 | 6.041780e-02 | 1.219 |
R-HSA-9636383 | Prevention of phagosomal-lysosomal fusion | 6.052525e-02 | 1.218 |
R-HSA-9931295 | PD-L1(CD274) glycosylation and translocation to plasma membrane | 6.052525e-02 | 1.218 |
R-HSA-5675221 | Negative regulation of MAPK pathway | 6.061434e-02 | 1.217 |
R-HSA-9683701 | Translation of Structural Proteins | 6.061434e-02 | 1.217 |
R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 6.247377e-02 | 1.204 |
R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 6.247377e-02 | 1.204 |
R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 6.247377e-02 | 1.204 |
R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 6.247377e-02 | 1.204 |
R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 6.247377e-02 | 1.204 |
R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 6.541734e-02 | 1.184 |
R-HSA-73762 | RNA Polymerase I Transcription Initiation | 6.541734e-02 | 1.184 |
R-HSA-157118 | Signaling by NOTCH | 6.561551e-02 | 1.183 |
R-HSA-391251 | Protein folding | 6.574178e-02 | 1.182 |
R-HSA-1500931 | Cell-Cell communication | 6.653162e-02 | 1.177 |
R-HSA-418597 | G alpha (z) signalling events | 6.777527e-02 | 1.169 |
R-HSA-9012852 | Signaling by NOTCH3 | 6.777527e-02 | 1.169 |
R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 6.814532e-02 | 1.167 |
R-HSA-5654743 | Signaling by FGFR4 | 7.043670e-02 | 1.152 |
R-HSA-9637690 | Response of Mtb to phagocytosis | 7.043670e-02 | 1.152 |
R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 7.101700e-02 | 1.149 |
R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 7.112007e-02 | 1.148 |
R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 7.112007e-02 | 1.148 |
R-HSA-162658 | Golgi Cisternae Pericentriolar Stack Reorganization | 7.200332e-02 | 1.143 |
R-HSA-109606 | Intrinsic Pathway for Apoptosis | 7.229181e-02 | 1.141 |
R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 7.356101e-02 | 1.133 |
R-HSA-6803529 | FGFR2 alternative splicing | 7.481868e-02 | 1.126 |
R-HSA-9860276 | SLC15A4:TASL-dependent IRF5 activation | 7.514437e-02 | 1.124 |
R-HSA-9764302 | Regulation of CDH19 Expression and Function | 7.514437e-02 | 1.124 |
R-HSA-8935964 | RUNX1 regulates expression of components of tight junctions | 7.514437e-02 | 1.124 |
R-HSA-5693537 | Resolution of D-Loop Structures | 7.726868e-02 | 1.112 |
R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 7.788445e-02 | 1.109 |
R-HSA-72312 | rRNA processing | 8.102178e-02 | 1.091 |
R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 8.112179e-02 | 1.091 |
R-HSA-774815 | Nucleosome assembly | 8.112179e-02 | 1.091 |
R-HSA-5654741 | Signaling by FGFR3 | 8.112179e-02 | 1.091 |
R-HSA-9824272 | Somitogenesis | 8.112179e-02 | 1.091 |
R-HSA-446728 | Cell junction organization | 8.206829e-02 | 1.086 |
R-HSA-399956 | CRMPs in Sema3A signaling | 8.213903e-02 | 1.085 |
R-HSA-2032785 | YAP1- and WWTR1 (TAZ)-stimulated gene expression | 8.213903e-02 | 1.085 |
R-HSA-9648895 | Response of EIF2AK1 (HRI) to heme deficiency | 8.254785e-02 | 1.083 |
R-HSA-180746 | Nuclear import of Rev protein | 8.369408e-02 | 1.077 |
R-HSA-392518 | Signal amplification | 8.369408e-02 | 1.077 |
R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 8.369408e-02 | 1.077 |
R-HSA-9680350 | Signaling by CSF1 (M-CSF) in myeloid cells | 8.369408e-02 | 1.077 |
R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 8.369408e-02 | 1.077 |
R-HSA-72165 | mRNA Splicing - Minor Pathway | 8.678501e-02 | 1.062 |
R-HSA-9675135 | Diseases of DNA repair | 8.678501e-02 | 1.062 |
R-HSA-168898 | Toll-like Receptor Cascades | 8.884878e-02 | 1.051 |
R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 9.000433e-02 | 1.046 |
R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 9.039237e-02 | 1.044 |
R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 9.039237e-02 | 1.044 |
R-HSA-421270 | Cell-cell junction organization | 9.040105e-02 | 1.044 |
R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 9.065272e-02 | 1.043 |
R-HSA-8863678 | Neurodegenerative Diseases | 9.065272e-02 | 1.043 |
R-HSA-422356 | Regulation of insulin secretion | 9.165358e-02 | 1.038 |
R-HSA-190236 | Signaling by FGFR | 9.165358e-02 | 1.038 |
R-HSA-8951671 | RUNX3 regulates YAP1-mediated transcription | 9.175736e-02 | 1.037 |
R-HSA-69478 | G2/M DNA replication checkpoint | 9.175736e-02 | 1.037 |
R-HSA-113507 | E2F-enabled inhibition of pre-replication complex formation | 9.175736e-02 | 1.037 |
R-HSA-2980767 | Activation of NIMA Kinases NEK9, NEK6, NEK7 | 9.175736e-02 | 1.037 |
R-HSA-351202 | Metabolism of polyamines | 9.209420e-02 | 1.036 |
R-HSA-196299 | Beta-catenin phosphorylation cascade | 9.284916e-02 | 1.032 |
R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 9.284916e-02 | 1.032 |
R-HSA-1502540 | Signaling by Activin | 9.284916e-02 | 1.032 |
R-HSA-9018519 | Estrogen-dependent gene expression | 9.538608e-02 | 1.021 |
R-HSA-70268 | Pyruvate metabolism | 9.585680e-02 | 1.018 |
R-HSA-212300 | PRC2 methylates histones and DNA | 9.735890e-02 | 1.012 |
R-HSA-111933 | Calmodulin induced events | 9.735890e-02 | 1.012 |
R-HSA-111997 | CaM pathway | 9.735890e-02 | 1.012 |
R-HSA-3371511 | HSF1 activation | 9.735890e-02 | 1.012 |
R-HSA-9682385 | FLT3 signaling in disease | 9.735890e-02 | 1.012 |
R-HSA-9632697 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 1.062098e-01 | 0.974 |
R-HSA-5632968 | Defective Mismatch Repair Associated With MSH6 | 1.062098e-01 | 0.974 |
R-HSA-9630791 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4 | 1.062098e-01 | 0.974 |
R-HSA-9645722 | Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function | 1.062098e-01 | 0.974 |
R-HSA-9630750 | Evasion of Oncogene Induced Senescence Due to p16INK4A Defects | 1.550109e-01 | 0.810 |
R-HSA-9632693 | Evasion of Oxidative Stress Induced Senescence Due to p16INK4A Defects | 1.550109e-01 | 0.810 |
R-HSA-5602636 | IKBKB deficiency causes SCID | 1.550109e-01 | 0.810 |
R-HSA-5602571 | TRAF3 deficiency - HSE | 1.550109e-01 | 0.810 |
R-HSA-9632700 | Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding... | 1.550109e-01 | 0.810 |
R-HSA-5603027 | IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (E... | 1.550109e-01 | 0.810 |
R-HSA-9630794 | Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4... | 1.550109e-01 | 0.810 |
R-HSA-5619050 | Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tu... | 1.550109e-01 | 0.810 |
R-HSA-163767 | PP2A-mediated dephosphorylation of key metabolic factors | 1.093138e-01 | 0.961 |
R-HSA-72731 | Recycling of eIF2:GDP | 1.093138e-01 | 0.961 |
R-HSA-204626 | Hypusine synthesis from eIF5A-lysine | 1.466619e-01 | 0.834 |
R-HSA-73843 | 5-Phosphoribose 1-diphosphate biosynthesis | 1.466619e-01 | 0.834 |
R-HSA-164843 | 2-LTR circle formation | 1.661893e-01 | 0.779 |
R-HSA-176412 | Phosphorylation of the APC/C | 1.041002e-01 | 0.983 |
R-HSA-5651801 | PCNA-Dependent Long Patch Base Excision Repair | 1.407468e-01 | 0.852 |
R-HSA-164378 | PKA activation in glucagon signalling | 1.407468e-01 | 0.852 |
R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 1.538066e-01 | 0.813 |
R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 1.171059e-01 | 0.931 |
R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 1.672280e-01 | 0.777 |
R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.672280e-01 | 0.777 |
R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 1.672280e-01 | 0.777 |
R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.672280e-01 | 0.777 |
R-HSA-167158 | Formation of the HIV-1 Early Elongation Complex | 1.265929e-01 | 0.898 |
R-HSA-113418 | Formation of the Early Elongation Complex | 1.265929e-01 | 0.898 |
R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 1.363907e-01 | 0.865 |
R-HSA-8866654 | E3 ubiquitin ligases ubiquitinate target proteins | 1.251047e-01 | 0.903 |
R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 1.894883e-01 | 0.722 |
R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 1.087432e-01 | 0.964 |
R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 1.087432e-01 | 0.964 |
R-HSA-73856 | RNA Polymerase II Transcription Termination | 1.950679e-01 | 0.710 |
R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 1.745700e-01 | 0.758 |
R-HSA-8852135 | Protein ubiquitination | 1.894449e-01 | 0.723 |
R-HSA-380287 | Centrosome maturation | 1.894449e-01 | 0.723 |
R-HSA-6807878 | COPI-mediated anterograde transport | 1.527800e-01 | 0.816 |
R-HSA-167169 | HIV Transcription Elongation | 1.277920e-01 | 0.893 |
R-HSA-9823730 | Formation of definitive endoderm | 1.672280e-01 | 0.777 |
R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 1.819436e-01 | 0.740 |
R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 1.277920e-01 | 0.893 |
R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 1.464839e-01 | 0.834 |
R-HSA-450341 | Activation of the AP-1 family of transcription factors | 1.466619e-01 | 0.834 |
R-HSA-9762292 | Regulation of CDH11 function | 1.661893e-01 | 0.779 |
R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 1.198117e-01 | 0.922 |
R-HSA-163615 | PKA activation | 1.407468e-01 | 0.852 |
R-HSA-3371571 | HSF1-dependent transactivation | 1.182174e-01 | 0.927 |
R-HSA-6804114 | TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest | 1.158574e-01 | 0.936 |
R-HSA-111931 | PKA-mediated phosphorylation of CREB | 1.809751e-01 | 0.742 |
R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 1.623090e-01 | 0.790 |
R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 1.413813e-01 | 0.850 |
R-HSA-8849473 | PTK6 Expression | 1.093138e-01 | 0.961 |
R-HSA-8866904 | Negative regulation of activity of TFAP2 (AP-2) family transcription factors | 1.276615e-01 | 0.894 |
R-HSA-9909505 | Modulation of host responses by IFN-stimulated genes | 1.280850e-01 | 0.893 |
R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 1.783756e-01 | 0.749 |
R-HSA-9619665 | EGR2 and SOX10-mediated initiation of Schwann cell myelination | 1.894883e-01 | 0.722 |
R-HSA-9033241 | Peroxisomal protein import | 1.783833e-01 | 0.749 |
R-HSA-9010642 | ROBO receptors bind AKAP5 | 1.276615e-01 | 0.894 |
R-HSA-379716 | Cytosolic tRNA aminoacylation | 1.531148e-01 | 0.815 |
R-HSA-427413 | NoRC negatively regulates rRNA expression | 1.602238e-01 | 0.795 |
R-HSA-75072 | mRNA Editing | 1.466619e-01 | 0.834 |
R-HSA-918233 | TRAF3-dependent IRF activation pathway | 1.158574e-01 | 0.936 |
R-HSA-9754189 | Germ layer formation at gastrulation | 1.538066e-01 | 0.813 |
R-HSA-69190 | DNA strand elongation | 1.674928e-01 | 0.776 |
R-HSA-77042 | Formation of editosomes by ADAR proteins | 1.062098e-01 | 0.974 |
R-HSA-5632928 | Defective Mismatch Repair Associated With MSH2 | 1.550109e-01 | 0.810 |
R-HSA-176974 | Unwinding of DNA | 1.466619e-01 | 0.834 |
R-HSA-9634600 | Regulation of glycolysis by fructose 2,6-bisphosphate metabolism | 1.041002e-01 | 0.983 |
R-HSA-181429 | Serotonin Neurotransmitter Release Cycle | 1.407468e-01 | 0.852 |
R-HSA-8851708 | Signaling by FGFR2 IIIa TM | 1.538066e-01 | 0.813 |
R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 1.120748e-01 | 0.950 |
R-HSA-8863795 | Downregulation of ERBB2 signaling | 1.464839e-01 | 0.834 |
R-HSA-177243 | Interactions of Rev with host cellular proteins | 1.277920e-01 | 0.893 |
R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 1.088528e-01 | 0.963 |
R-HSA-168325 | Viral Messenger RNA Synthesis | 1.950679e-01 | 0.710 |
R-HSA-114452 | Activation of BH3-only proteins | 1.464839e-01 | 0.834 |
R-HSA-9006931 | Signaling by Nuclear Receptors | 1.888677e-01 | 0.724 |
R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 1.030252e-01 | 0.987 |
R-HSA-1181150 | Signaling by NODAL | 1.672280e-01 | 0.777 |
R-HSA-180024 | DARPP-32 events | 1.363907e-01 | 0.865 |
R-HSA-1483255 | PI Metabolism | 1.088528e-01 | 0.963 |
R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 1.466619e-01 | 0.834 |
R-HSA-977225 | Amyloid fiber formation | 1.324096e-01 | 0.878 |
R-HSA-163685 | Integration of energy metabolism | 1.580375e-01 | 0.801 |
R-HSA-9031628 | NGF-stimulated transcription | 9.874311e-02 | 1.005 |
R-HSA-352238 | Breakdown of the nuclear lamina | 1.550109e-01 | 0.810 |
R-HSA-9958517 | SLC-mediated bile acid transport | 1.276615e-01 | 0.894 |
R-HSA-9662834 | CD163 mediating an anti-inflammatory response | 1.861298e-01 | 0.730 |
R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 1.198117e-01 | 0.922 |
R-HSA-111996 | Ca-dependent events | 1.531148e-01 | 0.815 |
R-HSA-9816359 | Maternal to zygotic transition (MZT) | 1.537685e-01 | 0.813 |
R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 1.368050e-01 | 0.864 |
R-HSA-622312 | Inflammasomes | 1.265929e-01 | 0.898 |
R-HSA-1489509 | DAG and IP3 signaling | 1.803295e-01 | 0.744 |
R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 1.218426e-01 | 0.914 |
R-HSA-1296071 | Potassium Channels | 1.527800e-01 | 0.816 |
R-HSA-9833110 | RSV-host interactions | 1.228787e-01 | 0.911 |
R-HSA-9694631 | Maturation of nucleoprotein | 1.538066e-01 | 0.813 |
R-HSA-352230 | Amino acid transport across the plasma membrane | 1.783833e-01 | 0.749 |
R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 1.268813e-01 | 0.897 |
R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 1.257667e-01 | 0.900 |
R-HSA-5218859 | Regulated Necrosis | 1.397673e-01 | 0.855 |
R-HSA-70171 | Glycolysis | 1.768717e-01 | 0.752 |
R-HSA-983712 | Ion channel transport | 1.317139e-01 | 0.880 |
R-HSA-187037 | Signaling by NTRK1 (TRKA) | 1.129752e-01 | 0.947 |
R-HSA-112315 | Transmission across Chemical Synapses | 1.632638e-01 | 0.787 |
R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 1.646836e-01 | 0.783 |
R-HSA-9758941 | Gastrulation | 1.520839e-01 | 0.818 |
R-HSA-9659379 | Sensory processing of sound | 1.209752e-01 | 0.917 |
R-HSA-9824446 | Viral Infection Pathways | 1.491795e-01 | 0.826 |
R-HSA-5654736 | Signaling by FGFR1 | 1.545161e-01 | 0.811 |
R-HSA-432142 | Platelet sensitization by LDL | 1.407468e-01 | 0.852 |
R-HSA-901032 | ER Quality Control Compartment (ERQC) | 1.171059e-01 | 0.931 |
R-HSA-9013695 | NOTCH4 Intracellular Domain Regulates Transcription | 1.809751e-01 | 0.742 |
R-HSA-9825895 | Regulation of MITF-M-dependent genes involved in DNA replication, damage repair ... | 1.276615e-01 | 0.894 |
R-HSA-5682910 | LGI-ADAM interactions | 1.861298e-01 | 0.730 |
R-HSA-5621481 | C-type lectin receptors (CLRs) | 1.875887e-01 | 0.727 |
R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.674928e-01 | 0.776 |
R-HSA-8878171 | Transcriptional regulation by RUNX1 | 1.578596e-01 | 0.802 |
R-HSA-2672351 | Stimuli-sensing channels | 1.430399e-01 | 0.845 |
R-HSA-400685 | Sema4D in semaphorin signaling | 9.912226e-02 | 1.004 |
R-HSA-1433557 | Signaling by SCF-KIT | 1.619882e-01 | 0.791 |
R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 1.444518e-01 | 0.840 |
R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 1.672280e-01 | 0.777 |
R-HSA-9648002 | RAS processing | 1.198117e-01 | 0.922 |
R-HSA-1236394 | Signaling by ERBB4 | 1.819436e-01 | 0.740 |
R-HSA-9020591 | Interleukin-12 signaling | 1.048538e-01 | 0.979 |
R-HSA-447115 | Interleukin-12 family signaling | 1.764833e-01 | 0.753 |
R-HSA-9793380 | Formation of paraxial mesoderm | 1.950679e-01 | 0.710 |
R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 1.971373e-01 | 0.705 |
R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 1.993989e-01 | 0.700 |
R-HSA-901042 | Calnexin/calreticulin cycle | 2.008139e-01 | 0.697 |
R-HSA-9768919 | NPAS4 regulates expression of target genes | 2.008139e-01 | 0.697 |
R-HSA-8854521 | Interaction between PHLDA1 and AURKA | 2.011502e-01 | 0.696 |
R-HSA-3858516 | Glycogen storage disease type 0 (liver GYS2) | 2.011502e-01 | 0.696 |
R-HSA-3814836 | Glycogen storage disease type XV (GYG1) | 2.011502e-01 | 0.696 |
R-HSA-3656535 | TGFBR1 LBD Mutants in Cancer | 2.011502e-01 | 0.696 |
R-HSA-3878781 | Glycogen storage disease type IV (GBE1) | 2.011502e-01 | 0.696 |
R-HSA-1296067 | Potassium transport channels | 2.011502e-01 | 0.696 |
R-HSA-3828062 | Glycogen storage disease type 0 (muscle GYS1) | 2.011502e-01 | 0.696 |
R-HSA-75064 | mRNA Editing: A to I Conversion | 2.011502e-01 | 0.696 |
R-HSA-75102 | C6 deamination of adenosine | 2.011502e-01 | 0.696 |
R-HSA-446343 | Localization of the PINCH-ILK-PARVIN complex to focal adhesions | 2.011502e-01 | 0.696 |
R-HSA-75108 | Activation, myristolyation of BID and translocation to mitochondria | 2.011502e-01 | 0.696 |
R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 2.025667e-01 | 0.693 |
R-HSA-199991 | Membrane Trafficking | 2.025673e-01 | 0.693 |
R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 2.036230e-01 | 0.691 |
R-HSA-1268020 | Mitochondrial protein import | 2.036230e-01 | 0.691 |
R-HSA-9694635 | Translation of Structural Proteins | 2.048126e-01 | 0.689 |
R-HSA-2871837 | FCERI mediated NF-kB activation | 2.052940e-01 | 0.688 |
R-HSA-162592 | Integration of provirus | 2.063800e-01 | 0.685 |
R-HSA-202670 | ERKs are inactivated | 2.063800e-01 | 0.685 |
R-HSA-113501 | Inhibition of replication initiation of damaged DNA by RB1/E2F1 | 2.063800e-01 | 0.685 |
R-HSA-9818028 | NFE2L2 regulates pentose phosphate pathway genes | 2.063800e-01 | 0.685 |
R-HSA-1234158 | Regulation of gene expression by Hypoxia-inducible Factor | 2.063800e-01 | 0.685 |
R-HSA-9007101 | Rab regulation of trafficking | 2.064048e-01 | 0.685 |
R-HSA-9006936 | Signaling by TGFB family members | 2.066906e-01 | 0.685 |
R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 2.093053e-01 | 0.679 |
R-HSA-212676 | Dopamine Neurotransmitter Release Cycle | 2.093053e-01 | 0.679 |
R-HSA-112316 | Neuronal System | 2.127998e-01 | 0.672 |
R-HSA-8856688 | Golgi-to-ER retrograde transport | 2.150374e-01 | 0.667 |
R-HSA-9909396 | Circadian clock | 2.150374e-01 | 0.667 |
R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 2.187242e-01 | 0.660 |
R-HSA-936837 | Ion transport by P-type ATPases | 2.211251e-01 | 0.655 |
R-HSA-418346 | Platelet homeostasis | 2.227899e-01 | 0.652 |
R-HSA-167160 | RNA Pol II CTD phosphorylation and interaction with CE during HIV infection | 2.238199e-01 | 0.650 |
R-HSA-77075 | RNA Pol II CTD phosphorylation and interaction with CE | 2.238199e-01 | 0.650 |
R-HSA-9634638 | Estrogen-dependent nuclear events downstream of ESR-membrane signaling | 2.238199e-01 | 0.650 |
R-HSA-9820865 | Z-decay: degradation of maternal mRNAs by zygotically expressed factors | 2.268470e-01 | 0.644 |
R-HSA-8941856 | RUNX3 regulates NOTCH signaling | 2.268470e-01 | 0.644 |
R-HSA-877312 | Regulation of IFNG signaling | 2.268470e-01 | 0.644 |
R-HSA-1247673 | Erythrocytes take up oxygen and release carbon dioxide | 2.268470e-01 | 0.644 |
R-HSA-8951936 | RUNX3 regulates p14-ARF | 2.268470e-01 | 0.644 |
R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 2.268470e-01 | 0.644 |
R-HSA-198323 | AKT phosphorylates targets in the cytosol | 2.268470e-01 | 0.644 |
R-HSA-2197563 | NOTCH2 intracellular domain regulates transcription | 2.268470e-01 | 0.644 |
R-HSA-9617629 | Regulation of FOXO transcriptional activity by acetylation | 2.268470e-01 | 0.644 |
R-HSA-166520 | Signaling by NTRKs | 2.280878e-01 | 0.642 |
R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 2.287051e-01 | 0.641 |
R-HSA-6806834 | Signaling by MET | 2.287051e-01 | 0.641 |
R-HSA-73886 | Chromosome Maintenance | 2.319728e-01 | 0.635 |
R-HSA-180910 | Vpr-mediated nuclear import of PICs | 2.358973e-01 | 0.627 |
R-HSA-429947 | Deadenylation of mRNA | 2.385232e-01 | 0.622 |
R-HSA-933542 | TRAF6 mediated NF-kB activation | 2.385232e-01 | 0.622 |
R-HSA-9673240 | Defective gamma-carboxylation of F9 | 2.447728e-01 | 0.611 |
R-HSA-4719377 | Defective DPM2 causes DPM2-CDG | 2.447728e-01 | 0.611 |
R-HSA-4717374 | Defective DPM1 causes DPM1-CDG | 2.447728e-01 | 0.611 |
R-HSA-5578999 | Defective GCLC causes HAGGSD | 2.447728e-01 | 0.611 |
R-HSA-4719360 | Defective DPM3 causes DPM3-CDG | 2.447728e-01 | 0.611 |
R-HSA-5660862 | Defective SLC7A7 causes lysinuric protein intolerance (LPI) | 2.447728e-01 | 0.611 |
R-HSA-1296053 | Classical Kir channels | 2.447728e-01 | 0.611 |
R-HSA-5603037 | IRAK4 deficiency (TLR5) | 2.447728e-01 | 0.611 |
R-HSA-9636249 | Inhibition of nitric oxide production | 2.447728e-01 | 0.611 |
R-HSA-9022538 | Loss of MECP2 binding ability to 5mC-DNA | 2.447728e-01 | 0.611 |
R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 2.447728e-01 | 0.611 |
R-HSA-75157 | FasL/ CD95L signaling | 2.447728e-01 | 0.611 |
R-HSA-442720 | CREB1 phosphorylation through the activation of Adenylate Cyclase | 2.474468e-01 | 0.607 |
R-HSA-6811555 | PI5P Regulates TP53 Acetylation | 2.474468e-01 | 0.607 |
R-HSA-75035 | Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex | 2.474468e-01 | 0.607 |
R-HSA-9683610 | Maturation of nucleoprotein | 2.474468e-01 | 0.607 |
R-HSA-9958863 | SLC-mediated transport of amino acids | 2.482543e-01 | 0.605 |
R-HSA-72187 | mRNA 3'-end processing | 2.497293e-01 | 0.603 |
R-HSA-6794361 | Neurexins and neuroligins | 2.497293e-01 | 0.603 |
R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 2.497293e-01 | 0.603 |
R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 2.521435e-01 | 0.598 |
R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 2.533836e-01 | 0.596 |
R-HSA-70221 | Glycogen breakdown (glycogenolysis) | 2.533836e-01 | 0.596 |
R-HSA-203927 | MicroRNA (miRNA) biogenesis | 2.533836e-01 | 0.596 |
R-HSA-9839394 | TGFBR3 expression | 2.533836e-01 | 0.596 |
R-HSA-167172 | Transcription of the HIV genome | 2.575026e-01 | 0.589 |
R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 2.575026e-01 | 0.589 |
R-HSA-9725554 | Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin | 2.600393e-01 | 0.585 |
R-HSA-445355 | Smooth Muscle Contraction | 2.601681e-01 | 0.585 |
R-HSA-391160 | Signal regulatory protein family interactions | 2.681040e-01 | 0.572 |
R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 2.683703e-01 | 0.571 |
R-HSA-3371568 | Attenuation phase | 2.722862e-01 | 0.565 |
R-HSA-176033 | Interactions of Vpr with host cellular proteins | 2.722862e-01 | 0.565 |
R-HSA-6803204 | TP53 Regulates Transcription of Genes Involved in Cytochrome C Release | 2.834538e-01 | 0.548 |
R-HSA-73863 | RNA Polymerase I Transcription Termination | 2.834538e-01 | 0.548 |
R-HSA-3928663 | EPHA-mediated growth cone collapse | 2.834538e-01 | 0.548 |
R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 2.846287e-01 | 0.546 |
R-HSA-5218920 | VEGFR2 mediated vascular permeability | 2.846287e-01 | 0.546 |
R-HSA-3214841 | PKMTs methylate histone lysines | 2.846287e-01 | 0.546 |
R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 2.846287e-01 | 0.546 |
R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 2.857631e-01 | 0.544 |
R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 2.857631e-01 | 0.544 |
R-HSA-2978092 | Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate | 2.860158e-01 | 0.544 |
R-HSA-5626978 | TNFR1-mediated ceramide production | 2.860158e-01 | 0.544 |
R-HSA-9013957 | TLR3-mediated TICAM1-dependent programmed cell death | 2.860158e-01 | 0.544 |
R-HSA-69560 | Transcriptional activation of p53 responsive genes | 2.860158e-01 | 0.544 |
R-HSA-69895 | Transcriptional activation of cell cycle inhibitor p21 | 2.860158e-01 | 0.544 |
R-HSA-888568 | GABA synthesis | 2.860158e-01 | 0.544 |
R-HSA-111448 | Activation of NOXA and translocation to mitochondria | 2.860158e-01 | 0.544 |
R-HSA-9729555 | Sensory perception of sour taste | 2.860158e-01 | 0.544 |
R-HSA-112303 | Electric Transmission Across Gap Junctions | 2.860158e-01 | 0.544 |
R-HSA-112307 | Transmission across Electrical Synapses | 2.860158e-01 | 0.544 |
R-HSA-1810476 | RIP-mediated NFkB activation via ZBP1 | 2.887511e-01 | 0.539 |
R-HSA-5676934 | Protein repair | 2.887511e-01 | 0.539 |
R-HSA-446353 | Cell-extracellular matrix interactions | 2.887511e-01 | 0.539 |
R-HSA-212165 | Epigenetic regulation of gene expression | 2.932580e-01 | 0.533 |
R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 3.025339e-01 | 0.519 |
R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 3.025676e-01 | 0.519 |
R-HSA-4086398 | Ca2+ pathway | 3.049611e-01 | 0.516 |
R-HSA-5663084 | Diseases of carbohydrate metabolism | 3.049611e-01 | 0.516 |
R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 3.051518e-01 | 0.515 |
R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 3.093276e-01 | 0.510 |
R-HSA-6803207 | TP53 Regulates Transcription of Caspase Activators and Caspases | 3.093276e-01 | 0.510 |
R-HSA-399955 | SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion | 3.093276e-01 | 0.510 |
R-HSA-5099900 | WNT5A-dependent internalization of FZD4 | 3.093276e-01 | 0.510 |
R-HSA-6804116 | TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest | 3.093276e-01 | 0.510 |
R-HSA-210744 | Regulation of gene expression in late stage (branching morphogenesis) pancreatic... | 3.093276e-01 | 0.510 |
R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 3.138004e-01 | 0.503 |
R-HSA-72086 | mRNA Capping | 3.138004e-01 | 0.503 |
R-HSA-70326 | Glucose metabolism | 3.177520e-01 | 0.498 |
R-HSA-8854214 | TBC/RABGAPs | 3.220738e-01 | 0.492 |
R-HSA-191859 | snRNP Assembly | 3.245434e-01 | 0.489 |
R-HSA-194441 | Metabolism of non-coding RNA | 3.245434e-01 | 0.489 |
R-HSA-111463 | SMAC (DIABLO) binds to IAPs | 3.250088e-01 | 0.488 |
R-HSA-111464 | SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes | 3.250088e-01 | 0.488 |
R-HSA-9673768 | Signaling by membrane-tethered fusions of PDGFRA or PDGFRB | 3.250088e-01 | 0.488 |
R-HSA-165158 | Activation of AKT2 | 3.250088e-01 | 0.488 |
R-HSA-74713 | IRS activation | 3.250088e-01 | 0.488 |
R-HSA-9927353 | Co-inhibition by BTLA | 3.250088e-01 | 0.488 |
R-HSA-8849468 | PTK6 Regulates Proteins Involved in RNA Processing | 3.250088e-01 | 0.488 |
R-HSA-199977 | ER to Golgi Anterograde Transport | 3.251341e-01 | 0.488 |
R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 3.290110e-01 | 0.483 |
R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 3.290110e-01 | 0.483 |
R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 3.290110e-01 | 0.483 |
R-HSA-9008059 | Interleukin-37 signaling | 3.290110e-01 | 0.483 |
R-HSA-141430 | Inactivation of APC/C via direct inhibition of the APC/C complex | 3.297797e-01 | 0.482 |
R-HSA-141405 | Inhibition of the proteolytic activity of APC/C required for the onset of anapha... | 3.297797e-01 | 0.482 |
R-HSA-73854 | RNA Polymerase I Promoter Clearance | 3.341521e-01 | 0.476 |
R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 3.346444e-01 | 0.475 |
R-HSA-379724 | tRNA Aminoacylation | 3.354691e-01 | 0.474 |
R-HSA-1227986 | Signaling by ERBB2 | 3.354691e-01 | 0.474 |
R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 3.442137e-01 | 0.463 |
R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 3.442137e-01 | 0.463 |
R-HSA-449147 | Signaling by Interleukins | 3.442598e-01 | 0.463 |
R-HSA-9679191 | Potential therapeutics for SARS | 3.458323e-01 | 0.461 |
R-HSA-112043 | PLC beta mediated events | 3.464251e-01 | 0.460 |
R-HSA-2682334 | EPH-Ephrin signaling | 3.496626e-01 | 0.456 |
R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 3.496626e-01 | 0.456 |
R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 3.500597e-01 | 0.456 |
R-HSA-176407 | Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase | 3.500597e-01 | 0.456 |
R-HSA-73864 | RNA Polymerase I Transcription | 3.537941e-01 | 0.451 |
R-HSA-6784531 | tRNA processing in the nucleus | 3.574019e-01 | 0.447 |
R-HSA-4791275 | Signaling by WNT in cancer | 3.593858e-01 | 0.444 |
R-HSA-9675126 | Diseases of mitotic cell cycle | 3.593858e-01 | 0.444 |
R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 3.598333e-01 | 0.444 |
R-HSA-9839373 | Signaling by TGFBR3 | 3.598333e-01 | 0.444 |
R-HSA-182218 | Nef Mediated CD8 Down-regulation | 3.618746e-01 | 0.441 |
R-HSA-9833576 | CDH11 homotypic and heterotypic interactions | 3.618746e-01 | 0.441 |
R-HSA-187706 | Signalling to p38 via RIT and RIN | 3.618746e-01 | 0.441 |
R-HSA-8849470 | PTK6 Regulates Cell Cycle | 3.618746e-01 | 0.441 |
R-HSA-111469 | SMAC, XIAP-regulated apoptotic response | 3.618746e-01 | 0.441 |
R-HSA-5660668 | CLEC7A/inflammasome pathway | 3.618746e-01 | 0.441 |
R-HSA-163358 | PKA-mediated phosphorylation of key metabolic factors | 3.618746e-01 | 0.441 |
R-HSA-111457 | Release of apoptotic factors from the mitochondria | 3.618746e-01 | 0.441 |
R-HSA-68689 | CDC6 association with the ORC:origin complex | 3.618746e-01 | 0.441 |
R-HSA-162699 | Synthesis of dolichyl-phosphate mannose | 3.618746e-01 | 0.441 |
R-HSA-5603029 | IkBA variant leads to EDA-ID | 3.618746e-01 | 0.441 |
R-HSA-176417 | Phosphorylation of Emi1 | 3.618746e-01 | 0.441 |
R-HSA-9017802 | Noncanonical activation of NOTCH3 | 3.618746e-01 | 0.441 |
R-HSA-1483101 | Synthesis of PS | 3.618746e-01 | 0.441 |
R-HSA-75094 | Formation of the Editosome | 3.618746e-01 | 0.441 |
R-HSA-446388 | Regulation of cytoskeletal remodeling and cell spreading by IPP complex componen... | 3.618746e-01 | 0.441 |
R-HSA-9758919 | Epithelial-Mesenchymal Transition (EMT) during gastrulation | 3.618746e-01 | 0.441 |
R-HSA-75158 | TRAIL signaling | 3.618746e-01 | 0.441 |
R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 3.677065e-01 | 0.434 |
R-HSA-416993 | Trafficking of GluR2-containing AMPA receptors | 3.701256e-01 | 0.432 |
R-HSA-5358508 | Mismatch Repair | 3.701256e-01 | 0.432 |
R-HSA-111471 | Apoptotic factor-mediated response | 3.701256e-01 | 0.432 |
R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 3.701256e-01 | 0.432 |
R-HSA-9614657 | FOXO-mediated transcription of cell death genes | 3.701256e-01 | 0.432 |
R-HSA-1855170 | IPs transport between nucleus and cytosol | 3.745057e-01 | 0.427 |
R-HSA-9764260 | Regulation of Expression and Function of Type II Classical Cadherins | 3.745057e-01 | 0.427 |
R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 3.849965e-01 | 0.415 |
R-HSA-389356 | Co-stimulation by CD28 | 3.849965e-01 | 0.415 |
R-HSA-194138 | Signaling by VEGF | 3.877490e-01 | 0.411 |
R-HSA-390522 | Striated Muscle Contraction | 3.895531e-01 | 0.409 |
R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 3.895531e-01 | 0.409 |
R-HSA-392517 | Rap1 signalling | 3.899401e-01 | 0.409 |
R-HSA-1237044 | Erythrocytes take up carbon dioxide and release oxygen | 3.899401e-01 | 0.409 |
R-HSA-1480926 | O2/CO2 exchange in erythrocytes | 3.899401e-01 | 0.409 |
R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 3.947975e-01 | 0.404 |
R-HSA-8869496 | TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif... | 3.967290e-01 | 0.402 |
R-HSA-177539 | Autointegration results in viral DNA circles | 3.967290e-01 | 0.402 |
R-HSA-9912529 | H139Hfs13* PPM1K causes a mild variant of MSUD | 3.967290e-01 | 0.402 |
R-HSA-389542 | NADPH regeneration | 3.967290e-01 | 0.402 |
R-HSA-175567 | Integration of viral DNA into host genomic DNA | 3.967290e-01 | 0.402 |
R-HSA-199920 | CREB phosphorylation | 3.967290e-01 | 0.402 |
R-HSA-8964011 | HDL clearance | 3.967290e-01 | 0.402 |
R-HSA-532668 | N-glycan trimming in the ER and Calnexin/Calreticulin cycle | 3.975369e-01 | 0.401 |
R-HSA-9707564 | Cytoprotection by HMOX1 | 4.031436e-01 | 0.395 |
R-HSA-389513 | Co-inhibition by CTLA4 | 4.094711e-01 | 0.388 |
R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 4.094711e-01 | 0.388 |
R-HSA-9629569 | Protein hydroxylation | 4.094711e-01 | 0.388 |
R-HSA-112040 | G-protein mediated events | 4.122888e-01 | 0.385 |
R-HSA-8856828 | Clathrin-mediated endocytosis | 4.176643e-01 | 0.379 |
R-HSA-381042 | PERK regulates gene expression | 4.193566e-01 | 0.377 |
R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 4.193566e-01 | 0.377 |
R-HSA-187687 | Signalling to ERKs | 4.193566e-01 | 0.377 |
R-HSA-2514856 | The phototransduction cascade | 4.224768e-01 | 0.374 |
R-HSA-6794362 | Protein-protein interactions at synapses | 4.228482e-01 | 0.374 |
R-HSA-69186 | Lagging Strand Synthesis | 4.286903e-01 | 0.368 |
R-HSA-162594 | Early Phase of HIV Life Cycle | 4.286903e-01 | 0.368 |
R-HSA-198753 | ERK/MAPK targets | 4.286903e-01 | 0.368 |
R-HSA-397014 | Muscle contraction | 4.296286e-01 | 0.367 |
R-HSA-203641 | NOSTRIN mediated eNOS trafficking | 4.296816e-01 | 0.367 |
R-HSA-9031528 | NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipo... | 4.296816e-01 | 0.367 |
R-HSA-2470946 | Cohesin Loading onto Chromatin | 4.296816e-01 | 0.367 |
R-HSA-114516 | Disinhibition of SNARE formation | 4.296816e-01 | 0.367 |
R-HSA-9031525 | NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake | 4.296816e-01 | 0.367 |
R-HSA-111367 | SLBP independent Processing of Histone Pre-mRNAs | 4.296816e-01 | 0.367 |
R-HSA-72200 | mRNA Editing: C to U Conversion | 4.296816e-01 | 0.367 |
R-HSA-2562578 | TRIF-mediated programmed cell death | 4.296816e-01 | 0.367 |
R-HSA-167590 | Nef Mediated CD4 Down-regulation | 4.296816e-01 | 0.367 |
R-HSA-9032845 | Activated NTRK2 signals through CDK5 | 4.296816e-01 | 0.367 |
R-HSA-8847453 | Synthesis of PIPs in the nucleus | 4.296816e-01 | 0.367 |
R-HSA-428890 | Role of ABL in ROBO-SLIT signaling | 4.296816e-01 | 0.367 |
R-HSA-9686347 | Microbial modulation of RIPK1-mediated regulated necrosis | 4.296816e-01 | 0.367 |
R-HSA-110357 | Displacement of DNA glycosylase by APEX1 | 4.296816e-01 | 0.367 |
R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 4.326691e-01 | 0.364 |
R-HSA-8853659 | RET signaling | 4.340785e-01 | 0.362 |
R-HSA-1839126 | FGFR2 mutant receptor activation | 4.340785e-01 | 0.362 |
R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 4.340897e-01 | 0.362 |
R-HSA-6798695 | Neutrophil degranulation | 4.361748e-01 | 0.360 |
R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 4.449262e-01 | 0.352 |
R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 4.471569e-01 | 0.350 |
R-HSA-8956320 | Nucleotide biosynthesis | 4.471569e-01 | 0.350 |
R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 4.475737e-01 | 0.349 |
R-HSA-3371378 | Regulation by c-FLIP | 4.608361e-01 | 0.336 |
R-HSA-69416 | Dimerization of procaspase-8 | 4.608361e-01 | 0.336 |
R-HSA-8875656 | MET receptor recycling | 4.608361e-01 | 0.336 |
R-HSA-629597 | Highly calcium permeable nicotinic acetylcholine receptors | 4.608361e-01 | 0.336 |
R-HSA-77588 | SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs | 4.608361e-01 | 0.336 |
R-HSA-111453 | BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members | 4.608361e-01 | 0.336 |
R-HSA-9839383 | TGFBR3 PTM regulation | 4.608361e-01 | 0.336 |
R-HSA-210455 | Astrocytic Glutamate-Glutamine Uptake And Metabolism | 4.608361e-01 | 0.336 |
R-HSA-112313 | Neurotransmitter uptake and metabolism In glial cells | 4.608361e-01 | 0.336 |
R-HSA-444257 | RSK activation | 4.608361e-01 | 0.336 |
R-HSA-442729 | CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde | 4.608361e-01 | 0.336 |
R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 4.608361e-01 | 0.336 |
R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 4.630871e-01 | 0.334 |
R-HSA-452723 | Transcriptional regulation of pluripotent stem cells | 4.630871e-01 | 0.334 |
R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 4.661005e-01 | 0.332 |
R-HSA-168799 | Neurotoxicity of clostridium toxins | 4.661005e-01 | 0.332 |
R-HSA-5578749 | Transcriptional regulation by small RNAs | 4.664364e-01 | 0.331 |
R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 4.714982e-01 | 0.327 |
R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 4.756687e-01 | 0.323 |
R-HSA-5619507 | Activation of HOX genes during differentiation | 4.756687e-01 | 0.323 |
R-HSA-71336 | Pentose phosphate pathway | 4.773470e-01 | 0.321 |
R-HSA-112310 | Neurotransmitter release cycle | 4.812412e-01 | 0.318 |
R-HSA-5578775 | Ion homeostasis | 4.835194e-01 | 0.316 |
R-HSA-193648 | NRAGE signals death through JNK | 4.835194e-01 | 0.316 |
R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 4.842534e-01 | 0.315 |
R-HSA-9634635 | Estrogen-stimulated signaling through PRKCZ | 4.902906e-01 | 0.310 |
R-HSA-5218900 | CASP8 activity is inhibited | 4.902906e-01 | 0.310 |
R-HSA-9700645 | ALK mutants bind TKIs | 4.902906e-01 | 0.310 |
R-HSA-2025928 | Calcineurin activates NFAT | 4.902906e-01 | 0.310 |
R-HSA-198693 | AKT phosphorylates targets in the nucleus | 4.902906e-01 | 0.310 |
R-HSA-9768777 | Regulation of NPAS4 gene transcription | 4.902906e-01 | 0.310 |
R-HSA-193692 | Regulated proteolysis of p75NTR | 4.902906e-01 | 0.310 |
R-HSA-9613354 | Lipophagy | 4.902906e-01 | 0.310 |
R-HSA-9013700 | NOTCH4 Activation and Transmission of Signal to the Nucleus | 4.902906e-01 | 0.310 |
R-HSA-9840373 | Cellular response to mitochondrial stress | 4.902906e-01 | 0.310 |
R-HSA-450520 | HuR (ELAVL1) binds and stabilizes mRNA | 4.902906e-01 | 0.310 |
R-HSA-73779 | RNA Polymerase II Transcription Pre-Initiation And Promoter Opening | 4.914279e-01 | 0.309 |
R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 4.914279e-01 | 0.309 |
R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 4.914279e-01 | 0.309 |
R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 4.914279e-01 | 0.309 |
R-HSA-5602358 | Diseases associated with the TLR signaling cascade | 4.914279e-01 | 0.309 |
R-HSA-5260271 | Diseases of Immune System | 4.914279e-01 | 0.309 |
R-HSA-1251985 | Nuclear signaling by ERBB4 | 4.914279e-01 | 0.309 |
R-HSA-392499 | Metabolism of proteins | 4.926002e-01 | 0.308 |
R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 5.020180e-01 | 0.299 |
R-HSA-9821993 | Replacement of protamines by nucleosomes in the male pronucleus | 5.020180e-01 | 0.299 |
R-HSA-2132295 | MHC class II antigen presentation | 5.035663e-01 | 0.298 |
R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 5.053192e-01 | 0.296 |
R-HSA-8875555 | MET activates RAP1 and RAC1 | 5.181376e-01 | 0.286 |
R-HSA-2468052 | Establishment of Sister Chromatid Cohesion | 5.181376e-01 | 0.286 |
R-HSA-629594 | Highly calcium permeable postsynaptic nicotinic acetylcholine receptors | 5.181376e-01 | 0.286 |
R-HSA-390450 | Folding of actin by CCT/TriC | 5.181376e-01 | 0.286 |
R-HSA-68952 | DNA replication initiation | 5.181376e-01 | 0.286 |
R-HSA-5140745 | WNT5A-dependent internalization of FZD2, FZD5 and ROR2 | 5.181376e-01 | 0.286 |
R-HSA-6803544 | Ion influx/efflux at host-pathogen interface | 5.181376e-01 | 0.286 |
R-HSA-2151209 | Activation of PPARGC1A (PGC-1alpha) by phosphorylation | 5.181376e-01 | 0.286 |
R-HSA-9761174 | Formation of intermediate mesoderm | 5.181376e-01 | 0.286 |
R-HSA-2179392 | EGFR Transactivation by Gastrin | 5.181376e-01 | 0.286 |
R-HSA-9693928 | Defective RIPK1-mediated regulated necrosis | 5.181376e-01 | 0.286 |
R-HSA-9022702 | MECP2 regulates transcription of neuronal ligands | 5.181376e-01 | 0.286 |
R-HSA-1300642 | Sperm Motility And Taxes | 5.181376e-01 | 0.286 |
R-HSA-9668250 | Defective factor IX causes hemophilia B | 5.181376e-01 | 0.286 |
R-HSA-6799990 | Metal sequestration by antimicrobial proteins | 5.181376e-01 | 0.286 |
R-HSA-9627069 | Regulation of the apoptosome activity | 5.181376e-01 | 0.286 |
R-HSA-111932 | CaMK IV-mediated phosphorylation of CREB | 5.181376e-01 | 0.286 |
R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 5.181376e-01 | 0.286 |
R-HSA-74749 | Signal attenuation | 5.181376e-01 | 0.286 |
R-HSA-111458 | Formation of apoptosome | 5.181376e-01 | 0.286 |
R-HSA-429914 | Deadenylation-dependent mRNA decay | 5.188903e-01 | 0.285 |
R-HSA-167162 | RNA Polymerase II HIV Promoter Escape | 5.190112e-01 | 0.285 |
R-HSA-167161 | HIV Transcription Initiation | 5.190112e-01 | 0.285 |
R-HSA-75953 | RNA Polymerase II Transcription Initiation | 5.190112e-01 | 0.285 |
R-HSA-6811438 | Intra-Golgi traffic | 5.190112e-01 | 0.285 |
R-HSA-5218921 | VEGFR2 mediated cell proliferation | 5.193826e-01 | 0.285 |
R-HSA-9932444 | ATP-dependent chromatin remodelers | 5.193826e-01 | 0.285 |
R-HSA-9932451 | SWI/SNF chromatin remodelers | 5.193826e-01 | 0.285 |
R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 5.193826e-01 | 0.285 |
R-HSA-9734767 | Developmental Cell Lineages | 5.228142e-01 | 0.282 |
R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 5.304262e-01 | 0.275 |
R-HSA-5619115 | Disorders of transmembrane transporters | 5.340685e-01 | 0.272 |
R-HSA-877300 | Interferon gamma signaling | 5.347572e-01 | 0.272 |
R-HSA-210500 | Glutamate Neurotransmitter Release Cycle | 5.363377e-01 | 0.271 |
R-HSA-1660514 | Synthesis of PIPs at the Golgi membrane | 5.363377e-01 | 0.271 |
R-HSA-3295583 | TRP channels | 5.363377e-01 | 0.271 |
R-HSA-1483248 | Synthesis of PIPs at the ER membrane | 5.444648e-01 | 0.264 |
R-HSA-425381 | Bicarbonate transporters | 5.444648e-01 | 0.264 |
R-HSA-427601 | Inorganic anion exchange by SLC26 transporters | 5.444648e-01 | 0.264 |
R-HSA-9754560 | SARS-CoV-2 modulates autophagy | 5.444648e-01 | 0.264 |
R-HSA-9635465 | Suppression of apoptosis | 5.444648e-01 | 0.264 |
R-HSA-210990 | PECAM1 interactions | 5.444648e-01 | 0.264 |
R-HSA-73776 | RNA Polymerase II Promoter Escape | 5.457636e-01 | 0.263 |
R-HSA-9710421 | Defective pyroptosis | 5.457636e-01 | 0.263 |
R-HSA-9730414 | MITF-M-regulated melanocyte development | 5.465561e-01 | 0.262 |
R-HSA-8949613 | Cristae formation | 5.528765e-01 | 0.257 |
R-HSA-389357 | CD28 dependent PI3K/Akt signaling | 5.528765e-01 | 0.257 |
R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 5.641859e-01 | 0.249 |
R-HSA-1280218 | Adaptive Immune System | 5.668683e-01 | 0.247 |
R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 5.689936e-01 | 0.245 |
R-HSA-73614 | Pyrimidine salvage | 5.689936e-01 | 0.245 |
R-HSA-159740 | Gamma-carboxylation of protein precursors | 5.693552e-01 | 0.245 |
R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 5.693552e-01 | 0.245 |
R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 5.693552e-01 | 0.245 |
R-HSA-68884 | Mitotic Telophase/Cytokinesis | 5.693552e-01 | 0.245 |
R-HSA-622323 | Presynaptic nicotinic acetylcholine receptors | 5.693552e-01 | 0.245 |
R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 5.693552e-01 | 0.245 |
R-HSA-5693548 | Sensing of DNA Double Strand Breaks | 5.693552e-01 | 0.245 |
R-HSA-416550 | Sema4D mediated inhibition of cell attachment and migration | 5.693552e-01 | 0.245 |
R-HSA-111461 | Cytochrome c-mediated apoptotic response | 5.693552e-01 | 0.245 |
R-HSA-76042 | RNA Polymerase II Transcription Initiation And Promoter Clearance | 5.716270e-01 | 0.243 |
R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 5.716270e-01 | 0.243 |
R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 5.842108e-01 | 0.233 |
R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 5.842108e-01 | 0.233 |
R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 5.842108e-01 | 0.233 |
R-HSA-204174 | Regulation of pyruvate dehydrogenase (PDH) complex | 5.846859e-01 | 0.233 |
R-HSA-9759475 | Regulation of CDH11 Expression and Function | 5.846859e-01 | 0.233 |
R-HSA-382551 | Transport of small molecules | 5.878409e-01 | 0.231 |
R-HSA-69109 | Leading Strand Synthesis | 5.928869e-01 | 0.227 |
R-HSA-69091 | Polymerase switching | 5.928869e-01 | 0.227 |
R-HSA-159854 | Gamma-carboxylation, transport, and amino-terminal cleavage of proteins | 5.928869e-01 | 0.227 |
R-HSA-9865114 | Maple Syrup Urine Disease | 5.928869e-01 | 0.227 |
R-HSA-9005891 | Loss of function of MECP2 in Rett syndrome | 5.928869e-01 | 0.227 |
R-HSA-9005895 | Pervasive developmental disorders | 5.928869e-01 | 0.227 |
R-HSA-9697154 | Disorders of Nervous System Development | 5.928869e-01 | 0.227 |
R-HSA-4641265 | Repression of WNT target genes | 5.928869e-01 | 0.227 |
R-HSA-193144 | Estrogen biosynthesis | 5.928869e-01 | 0.227 |
R-HSA-5661231 | Metallothioneins bind metals | 5.928869e-01 | 0.227 |
R-HSA-8983711 | OAS antiviral response | 5.928869e-01 | 0.227 |
R-HSA-1483191 | Synthesis of PC | 5.965565e-01 | 0.224 |
R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 5.975214e-01 | 0.224 |
R-HSA-1500620 | Meiosis | 5.979660e-01 | 0.223 |
R-HSA-76046 | RNA Polymerase III Transcription Initiation | 5.999517e-01 | 0.222 |
R-HSA-9013508 | NOTCH3 Intracellular Domain Regulates Transcription | 5.999517e-01 | 0.222 |
R-HSA-5663205 | Infectious disease | 6.058114e-01 | 0.218 |
R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 6.085415e-01 | 0.216 |
R-HSA-1266738 | Developmental Biology | 6.144704e-01 | 0.211 |
R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 6.147906e-01 | 0.211 |
R-HSA-399719 | Trafficking of AMPA receptors | 6.147906e-01 | 0.211 |
R-HSA-5694530 | Cargo concentration in the ER | 6.147906e-01 | 0.211 |
R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 6.151341e-01 | 0.211 |
R-HSA-9029558 | NR1H2 & NR1H3 regulate gene expression linked to lipogenesis | 6.151341e-01 | 0.211 |
R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 6.151341e-01 | 0.211 |
R-HSA-170660 | Adenylate cyclase activating pathway | 6.151341e-01 | 0.211 |
R-HSA-9661069 | Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) | 6.151341e-01 | 0.211 |
R-HSA-6804759 | Regulation of TP53 Activity through Association with Co-factors | 6.151341e-01 | 0.211 |
R-HSA-181431 | Acetylcholine binding and downstream events | 6.151341e-01 | 0.211 |
R-HSA-622327 | Postsynaptic nicotinic acetylcholine receptors | 6.151341e-01 | 0.211 |
R-HSA-9659787 | Aberrant regulation of mitotic G1/S transition in cancer due to RB1 defects | 6.151341e-01 | 0.211 |
R-HSA-5676594 | TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway | 6.151341e-01 | 0.211 |
R-HSA-351200 | Interconversion of polyamines | 6.151341e-01 | 0.211 |
R-HSA-1475029 | Reversible hydration of carbon dioxide | 6.151341e-01 | 0.211 |
R-HSA-170968 | Frs2-mediated activation | 6.151341e-01 | 0.211 |
R-HSA-1059683 | Interleukin-6 signaling | 6.151341e-01 | 0.211 |
R-HSA-597592 | Post-translational protein modification | 6.152183e-01 | 0.211 |
R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 6.165448e-01 | 0.210 |
R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 6.165448e-01 | 0.210 |
R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 6.173428e-01 | 0.209 |
R-HSA-162582 | Signal Transduction | 6.191614e-01 | 0.208 |
R-HSA-438064 | Post NMDA receptor activation events | 6.256424e-01 | 0.204 |
R-HSA-5655253 | Signaling by FGFR2 in disease | 6.321316e-01 | 0.199 |
R-HSA-177504 | Retrograde neurotrophin signalling | 6.361669e-01 | 0.196 |
R-HSA-6803211 | TP53 Regulates Transcription of Death Receptors and Ligands | 6.361669e-01 | 0.196 |
R-HSA-69166 | Removal of the Flap Intermediate | 6.361669e-01 | 0.196 |
R-HSA-1170546 | Prolactin receptor signaling | 6.361669e-01 | 0.196 |
R-HSA-5578768 | Physiological factors | 6.361669e-01 | 0.196 |
R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 6.361669e-01 | 0.196 |
R-HSA-8963896 | HDL assembly | 6.361669e-01 | 0.196 |
R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 6.361925e-01 | 0.196 |
R-HSA-9664433 | Leishmania parasite growth and survival | 6.361925e-01 | 0.196 |
R-HSA-204005 | COPII-mediated vesicle transport | 6.374340e-01 | 0.196 |
R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 6.374340e-01 | 0.196 |
R-HSA-68616 | Assembly of the ORC complex at the origin of replication | 6.431934e-01 | 0.192 |
R-HSA-9930044 | Nuclear RNA decay | 6.431934e-01 | 0.192 |
R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 6.431934e-01 | 0.192 |
R-HSA-9022692 | Regulation of MECP2 expression and activity | 6.431934e-01 | 0.192 |
R-HSA-373080 | Class B/2 (Secretin family receptors) | 6.521419e-01 | 0.186 |
R-HSA-73772 | RNA Polymerase I Promoter Escape | 6.546077e-01 | 0.184 |
R-HSA-9027284 | Erythropoietin activates RAS | 6.560515e-01 | 0.183 |
R-HSA-170670 | Adenylate cyclase inhibitory pathway | 6.560515e-01 | 0.183 |
R-HSA-73780 | RNA Polymerase III Chain Elongation | 6.560515e-01 | 0.183 |
R-HSA-69183 | Processive synthesis on the lagging strand | 6.560515e-01 | 0.183 |
R-HSA-111447 | Activation of BAD and translocation to mitochondria | 6.560515e-01 | 0.183 |
R-HSA-9701898 | STAT3 nuclear events downstream of ALK signaling | 6.560515e-01 | 0.183 |
R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 6.560515e-01 | 0.183 |
R-HSA-174362 | Transport and metabolism of PAPS | 6.560515e-01 | 0.183 |
R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 6.560515e-01 | 0.183 |
R-HSA-171007 | p38MAPK events | 6.560515e-01 | 0.183 |
R-HSA-3270619 | IRF3-mediated induction of type I IFN | 6.560515e-01 | 0.183 |
R-HSA-450385 | Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA | 6.560515e-01 | 0.183 |
R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 6.560515e-01 | 0.183 |
R-HSA-8876725 | Protein methylation | 6.560515e-01 | 0.183 |
R-HSA-196780 | Biotin transport and metabolism | 6.560515e-01 | 0.183 |
R-HSA-199992 | trans-Golgi Network Vesicle Budding | 6.568267e-01 | 0.183 |
R-HSA-211000 | Gene Silencing by RNA | 6.575102e-01 | 0.182 |
R-HSA-8986944 | Transcriptional Regulation by MECP2 | 6.607049e-01 | 0.180 |
R-HSA-5673001 | RAF/MAP kinase cascade | 6.612880e-01 | 0.180 |
R-HSA-1221632 | Meiotic synapsis | 6.654699e-01 | 0.177 |
R-HSA-9639288 | Amino acids regulate mTORC1 | 6.654699e-01 | 0.177 |
R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 6.654699e-01 | 0.177 |
R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 6.662572e-01 | 0.176 |
R-HSA-5653656 | Vesicle-mediated transport | 6.698079e-01 | 0.174 |
R-HSA-2142845 | Hyaluronan metabolism | 6.699159e-01 | 0.174 |
R-HSA-5673000 | RAF activation | 6.699159e-01 | 0.174 |
R-HSA-5683057 | MAPK family signaling cascades | 6.701932e-01 | 0.174 |
R-HSA-140534 | Caspase activation via Death Receptors in the presence of ligand | 6.748504e-01 | 0.171 |
R-HSA-9603798 | Class I peroxisomal membrane protein import | 6.748504e-01 | 0.171 |
R-HSA-5576886 | Phase 4 - resting membrane potential | 6.748504e-01 | 0.171 |
R-HSA-169893 | Prolonged ERK activation events | 6.748504e-01 | 0.171 |
R-HSA-1362300 | Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL... | 6.748504e-01 | 0.171 |
R-HSA-9664420 | Killing mechanisms | 6.748504e-01 | 0.171 |
R-HSA-9673324 | WNT5:FZD7-mediated leishmania damping | 6.748504e-01 | 0.171 |
R-HSA-76002 | Platelet activation, signaling and aggregation | 6.798748e-01 | 0.168 |
R-HSA-917977 | Transferrin endocytosis and recycling | 6.826579e-01 | 0.166 |
R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 6.826579e-01 | 0.166 |
R-HSA-114608 | Platelet degranulation | 6.842293e-01 | 0.165 |
R-HSA-5633008 | TP53 Regulates Transcription of Cell Death Genes | 6.845812e-01 | 0.165 |
R-HSA-3214815 | HDACs deacetylate histones | 6.864416e-01 | 0.163 |
R-HSA-1483257 | Phospholipid metabolism | 6.900380e-01 | 0.161 |
R-HSA-430039 | mRNA decay by 5' to 3' exoribonuclease | 6.926230e-01 | 0.160 |
R-HSA-77595 | Processing of Intronless Pre-mRNAs | 6.926230e-01 | 0.160 |
R-HSA-9927020 | Heme assimilation | 6.926230e-01 | 0.160 |
R-HSA-9690406 | Transcriptional regulation of testis differentiation | 6.926230e-01 | 0.160 |
R-HSA-399997 | Acetylcholine regulates insulin secretion | 6.926230e-01 | 0.160 |
R-HSA-9675151 | Disorders of Developmental Biology | 6.926230e-01 | 0.160 |
R-HSA-8866910 | TFAP2 (AP-2) family regulates transcription of growth factors and their receptor... | 6.926230e-01 | 0.160 |
R-HSA-5660526 | Response to metal ions | 6.926230e-01 | 0.160 |
R-HSA-9651496 | Defects of contact activation system (CAS) and kallikrein/kinin system (KKS) | 6.926230e-01 | 0.160 |
R-HSA-5684996 | MAPK1/MAPK3 signaling | 6.946909e-01 | 0.158 |
R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 6.949942e-01 | 0.158 |
R-HSA-74158 | RNA Polymerase III Transcription | 6.949942e-01 | 0.158 |
R-HSA-432720 | Lysosome Vesicle Biogenesis | 6.949942e-01 | 0.158 |
R-HSA-114604 | GPVI-mediated activation cascade | 6.949942e-01 | 0.158 |
R-HSA-8941326 | RUNX2 regulates bone development | 6.949942e-01 | 0.158 |
R-HSA-163560 | Triglyceride catabolism | 6.949942e-01 | 0.158 |
R-HSA-948021 | Transport to the Golgi and subsequent modification | 6.955335e-01 | 0.158 |
R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 6.965522e-01 | 0.157 |
R-HSA-1296072 | Voltage gated Potassium channels | 7.069313e-01 | 0.151 |
R-HSA-933541 | TRAF6 mediated IRF7 activation | 7.069313e-01 | 0.151 |
R-HSA-196757 | Metabolism of folate and pterines | 7.069313e-01 | 0.151 |
R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 7.094251e-01 | 0.149 |
R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 7.094251e-01 | 0.149 |
R-HSA-139853 | Elevation of cytosolic Ca2+ levels | 7.094251e-01 | 0.149 |
R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 7.094251e-01 | 0.149 |
R-HSA-9768759 | Regulation of NPAS4 gene expression | 7.094251e-01 | 0.149 |
R-HSA-1614517 | Sulfide oxidation to sulfate | 7.094251e-01 | 0.149 |
R-HSA-6787639 | GDP-fucose biosynthesis | 7.094251e-01 | 0.149 |
R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 7.094251e-01 | 0.149 |
R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 7.094251e-01 | 0.149 |
R-HSA-201722 | Formation of the beta-catenin:TCF transactivating complex | 7.160282e-01 | 0.145 |
R-HSA-9958790 | SLC-mediated transport of inorganic anions | 7.184758e-01 | 0.144 |
R-HSA-73980 | RNA Polymerase III Transcription Termination | 7.253097e-01 | 0.139 |
R-HSA-8849932 | Synaptic adhesion-like molecules | 7.253097e-01 | 0.139 |
R-HSA-3928664 | Ephrin signaling | 7.253097e-01 | 0.139 |
R-HSA-9856651 | MITF-M-dependent gene expression | 7.254923e-01 | 0.139 |
R-HSA-201556 | Signaling by ALK | 7.296349e-01 | 0.137 |
R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 7.304096e-01 | 0.136 |
R-HSA-8873719 | RAB geranylgeranylation | 7.345221e-01 | 0.134 |
R-HSA-983189 | Kinesins | 7.345221e-01 | 0.134 |
R-HSA-156590 | Glutathione conjugation | 7.345221e-01 | 0.134 |
R-HSA-5617833 | Cilium Assembly | 7.351650e-01 | 0.134 |
R-HSA-418555 | G alpha (s) signalling events | 7.385706e-01 | 0.132 |
R-HSA-3214847 | HATs acetylate histones | 7.386557e-01 | 0.132 |
R-HSA-500753 | Pyrimidine biosynthesis | 7.403269e-01 | 0.131 |
R-HSA-9856532 | Mechanical load activates signaling by PIEZO1 and integrins in osteocytes | 7.403269e-01 | 0.131 |
R-HSA-881907 | Gastrin-CREB signalling pathway via PKC and MAPK | 7.403269e-01 | 0.131 |
R-HSA-449836 | Other interleukin signaling | 7.403269e-01 | 0.131 |
R-HSA-1834941 | STING mediated induction of host immune responses | 7.403269e-01 | 0.131 |
R-HSA-9671793 | Diseases of hemostasis | 7.403269e-01 | 0.131 |
R-HSA-9670095 | Inhibition of DNA recombination at telomere | 7.404164e-01 | 0.131 |
R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 7.545239e-01 | 0.122 |
R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 7.545239e-01 | 0.122 |
R-HSA-5620916 | VxPx cargo-targeting to cilium | 7.545239e-01 | 0.122 |
R-HSA-373753 | Nephrin family interactions | 7.545239e-01 | 0.122 |
R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 7.608783e-01 | 0.119 |
R-HSA-168256 | Immune System | 7.655135e-01 | 0.116 |
R-HSA-264642 | Acetylcholine Neurotransmitter Release Cycle | 7.679456e-01 | 0.115 |
R-HSA-5357786 | TNFR1-induced proapoptotic signaling | 7.679456e-01 | 0.115 |
R-HSA-8964208 | Phenylalanine metabolism | 7.679456e-01 | 0.115 |
R-HSA-9824594 | Regulation of MITF-M-dependent genes involved in apoptosis | 7.679456e-01 | 0.115 |
R-HSA-9819196 | Zygotic genome activation (ZGA) | 7.679456e-01 | 0.115 |
R-HSA-196836 | Vitamin C (ascorbate) metabolism | 7.679456e-01 | 0.115 |
R-HSA-167044 | Signalling to RAS | 7.679456e-01 | 0.115 |
R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 7.682157e-01 | 0.115 |
R-HSA-381119 | Unfolded Protein Response (UPR) | 7.715640e-01 | 0.113 |
R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 7.765881e-01 | 0.110 |
R-HSA-381038 | XBP1(S) activates chaperone genes | 7.795112e-01 | 0.108 |
R-HSA-5603041 | IRAK4 deficiency (TLR2/4) | 7.806342e-01 | 0.108 |
R-HSA-9617324 | Negative regulation of NMDA receptor-mediated neuronal transmission | 7.806342e-01 | 0.108 |
R-HSA-174403 | Glutathione synthesis and recycling | 7.806342e-01 | 0.108 |
R-HSA-9671555 | Signaling by PDGFR in disease | 7.806342e-01 | 0.108 |
R-HSA-3214858 | RMTs methylate histone arginines | 7.889439e-01 | 0.103 |
R-HSA-156581 | Methylation | 7.889439e-01 | 0.103 |
R-HSA-6803205 | TP53 regulates transcription of several additional cell death genes whose specif... | 7.926297e-01 | 0.101 |
R-HSA-76071 | RNA Polymerase III Transcription Initiation From Type 3 Promoter | 7.926297e-01 | 0.101 |
R-HSA-912694 | Regulation of IFNA/IFNB signaling | 7.926297e-01 | 0.101 |
R-HSA-8964038 | LDL clearance | 7.926297e-01 | 0.101 |
R-HSA-71384 | Ethanol oxidation | 7.926297e-01 | 0.101 |
R-HSA-9658195 | Leishmania infection | 7.947892e-01 | 0.100 |
R-HSA-9824443 | Parasitic Infection Pathways | 7.947892e-01 | 0.100 |
R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 8.039700e-01 | 0.095 |
R-HSA-912526 | Interleukin receptor SHC signaling | 8.039700e-01 | 0.095 |
R-HSA-879518 | Organic anion transport by SLCO transporters | 8.039700e-01 | 0.095 |
R-HSA-200425 | Carnitine shuttle | 8.039700e-01 | 0.095 |
R-HSA-1369062 | ABC transporters in lipid homeostasis | 8.039700e-01 | 0.095 |
R-HSA-982772 | Growth hormone receptor signaling | 8.039700e-01 | 0.095 |
R-HSA-9830674 | Formation of the ureteric bud | 8.039700e-01 | 0.095 |
R-HSA-3000170 | Syndecan interactions | 8.039700e-01 | 0.095 |
R-HSA-73884 | Base Excision Repair | 8.056264e-01 | 0.094 |
R-HSA-109582 | Hemostasis | 8.060328e-01 | 0.094 |
R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 8.117478e-01 | 0.091 |
R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 8.140652e-01 | 0.089 |
R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 8.146907e-01 | 0.089 |
R-HSA-181430 | Norepinephrine Neurotransmitter Release Cycle | 8.146907e-01 | 0.089 |
R-HSA-5621575 | CD209 (DC-SIGN) signaling | 8.146907e-01 | 0.089 |
R-HSA-5669034 | TNFs bind their physiological receptors | 8.146907e-01 | 0.089 |
R-HSA-8963898 | Plasma lipoprotein assembly | 8.146907e-01 | 0.089 |
R-HSA-6783589 | Interleukin-6 family signaling | 8.146907e-01 | 0.089 |
R-HSA-381070 | IRE1alpha activates chaperones | 8.177106e-01 | 0.087 |
R-HSA-71291 | Metabolism of amino acids and derivatives | 8.190534e-01 | 0.087 |
R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 8.196695e-01 | 0.086 |
R-HSA-4839726 | Chromatin organization | 8.240970e-01 | 0.084 |
R-HSA-1483249 | Inositol phosphate metabolism | 8.244986e-01 | 0.084 |
R-HSA-174411 | Polymerase switching on the C-strand of the telomere | 8.248258e-01 | 0.084 |
R-HSA-420029 | Tight junction interactions | 8.248258e-01 | 0.084 |
R-HSA-2160916 | Hyaluronan degradation | 8.248258e-01 | 0.084 |
R-HSA-3214842 | HDMs demethylate histones | 8.248258e-01 | 0.084 |
R-HSA-1187000 | Fertilization | 8.248258e-01 | 0.084 |
R-HSA-389887 | Beta-oxidation of pristanoyl-CoA | 8.248258e-01 | 0.084 |
R-HSA-1474165 | Reproduction | 8.273215e-01 | 0.082 |
R-HSA-5576891 | Cardiac conduction | 8.320428e-01 | 0.080 |
R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 8.344071e-01 | 0.079 |
R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 8.344071e-01 | 0.079 |
R-HSA-1855183 | Synthesis of IP2, IP, and Ins in the cytosol | 8.344071e-01 | 0.079 |
R-HSA-9865118 | Diseases of branched-chain amino acid catabolism | 8.344071e-01 | 0.079 |
R-HSA-8934593 | Regulation of RUNX1 Expression and Activity | 8.344071e-01 | 0.079 |
R-HSA-9748787 | Azathioprine ADME | 8.364794e-01 | 0.078 |
R-HSA-1226099 | Signaling by FGFR in disease | 8.384236e-01 | 0.077 |
R-HSA-168249 | Innate Immune System | 8.400726e-01 | 0.076 |
R-HSA-3247509 | Chromatin modifying enzymes | 8.429460e-01 | 0.074 |
R-HSA-912446 | Meiotic recombination | 8.433900e-01 | 0.074 |
R-HSA-73728 | RNA Polymerase I Promoter Opening | 8.434649e-01 | 0.074 |
R-HSA-445095 | Interaction between L1 and Ankyrins | 8.434649e-01 | 0.074 |
R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 8.434649e-01 | 0.074 |
R-HSA-201451 | Signaling by BMP | 8.434649e-01 | 0.074 |
R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 8.434649e-01 | 0.074 |
R-HSA-9006115 | Signaling by NTRK2 (TRKB) | 8.434649e-01 | 0.074 |
R-HSA-264876 | Insulin processing | 8.434649e-01 | 0.074 |
R-HSA-9828806 | Maturation of hRSV A proteins | 8.434649e-01 | 0.074 |
R-HSA-5339562 | Uptake and actions of bacterial toxins | 8.500345e-01 | 0.071 |
R-HSA-9609690 | HCMV Early Events | 8.512400e-01 | 0.070 |
R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 8.520278e-01 | 0.070 |
R-HSA-5620971 | Pyroptosis | 8.520278e-01 | 0.070 |
R-HSA-8940973 | RUNX2 regulates osteoblast differentiation | 8.520278e-01 | 0.070 |
R-HSA-157579 | Telomere Maintenance | 8.552171e-01 | 0.068 |
R-HSA-209968 | Thyroxine biosynthesis | 8.601227e-01 | 0.065 |
R-HSA-9006335 | Signaling by Erythropoietin | 8.601227e-01 | 0.065 |
R-HSA-418360 | Platelet calcium homeostasis | 8.601227e-01 | 0.065 |
R-HSA-9955298 | SLC-mediated transport of organic anions | 8.607917e-01 | 0.065 |
R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 8.623241e-01 | 0.064 |
R-HSA-2424491 | DAP12 signaling | 8.677753e-01 | 0.062 |
R-HSA-1250196 | SHC1 events in ERBB2 signaling | 8.677753e-01 | 0.062 |
R-HSA-9753281 | Paracetamol ADME | 8.684548e-01 | 0.061 |
R-HSA-3299685 | Detoxification of Reactive Oxygen Species | 8.741177e-01 | 0.058 |
R-HSA-9913351 | Formation of the dystrophin-glycoprotein complex (DGC) | 8.750096e-01 | 0.058 |
R-HSA-186763 | Downstream signal transduction | 8.750096e-01 | 0.058 |
R-HSA-8963693 | Aspartate and asparagine metabolism | 8.750096e-01 | 0.058 |
R-HSA-9842860 | Regulation of endogenous retroelements | 8.778087e-01 | 0.057 |
R-HSA-1538133 | G0 and Early G1 | 8.818486e-01 | 0.055 |
R-HSA-6809371 | Formation of the cornified envelope | 8.859889e-01 | 0.053 |
R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 8.883137e-01 | 0.051 |
R-HSA-5609975 | Diseases associated with glycosylation precursor biosynthesis | 8.883137e-01 | 0.051 |
R-HSA-442742 | CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling | 8.883137e-01 | 0.051 |
R-HSA-1855204 | Synthesis of IP3 and IP4 in the cytosol | 8.883137e-01 | 0.051 |
R-HSA-9733709 | Cardiogenesis | 8.883137e-01 | 0.051 |
R-HSA-354192 | Integrin signaling | 8.883137e-01 | 0.051 |
R-HSA-180786 | Extension of Telomeres | 8.897848e-01 | 0.051 |
R-HSA-8979227 | Triglyceride metabolism | 8.897848e-01 | 0.051 |
R-HSA-186712 | Regulation of beta-cell development | 8.897848e-01 | 0.051 |
R-HSA-9609646 | HCMV Infection | 8.909915e-01 | 0.050 |
R-HSA-6802957 | Oncogenic MAPK signaling | 8.934470e-01 | 0.049 |
R-HSA-5223345 | Miscellaneous transport and binding events | 8.944254e-01 | 0.048 |
R-HSA-1482788 | Acyl chain remodelling of PC | 8.944254e-01 | 0.048 |
R-HSA-199220 | Vitamin B5 (pantothenate) metabolism | 8.944254e-01 | 0.048 |
R-HSA-189483 | Heme degradation | 8.944254e-01 | 0.048 |
R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 8.945917e-01 | 0.048 |
R-HSA-5362517 | Signaling by Retinoic Acid | 8.945917e-01 | 0.048 |
R-HSA-8956321 | Nucleotide salvage | 8.992030e-01 | 0.046 |
R-HSA-203615 | eNOS activation | 9.002031e-01 | 0.046 |
R-HSA-110328 | Recognition and association of DNA glycosylase with site containing an affected ... | 9.002031e-01 | 0.046 |
R-HSA-2393930 | Phosphate bond hydrolysis by NUDT proteins | 9.002031e-01 | 0.046 |
R-HSA-72306 | tRNA processing | 9.052086e-01 | 0.043 |
R-HSA-1482839 | Acyl chain remodelling of PE | 9.056649e-01 | 0.043 |
R-HSA-2408508 | Metabolism of ingested SeMet, Sec, MeSec into H2Se | 9.056649e-01 | 0.043 |
R-HSA-1852241 | Organelle biogenesis and maintenance | 9.072289e-01 | 0.042 |
R-HSA-9845576 | Glycosphingolipid transport | 9.108281e-01 | 0.041 |
R-HSA-69205 | G1/S-Specific Transcription | 9.108281e-01 | 0.041 |
R-HSA-74751 | Insulin receptor signalling cascade | 9.119324e-01 | 0.040 |
R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 9.146882e-01 | 0.039 |
R-HSA-9843745 | Adipogenesis | 9.149124e-01 | 0.039 |
R-HSA-8963691 | Phenylalanine and tyrosine metabolism | 9.157089e-01 | 0.038 |
R-HSA-6782315 | tRNA modification in the nucleus and cytosol | 9.195641e-01 | 0.036 |
R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 9.198363e-01 | 0.036 |
R-HSA-1912422 | Pre-NOTCH Expression and Processing | 9.199388e-01 | 0.036 |
R-HSA-8875878 | MET promotes cell motility | 9.203230e-01 | 0.036 |
R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 9.203230e-01 | 0.036 |
R-HSA-74217 | Purine salvage | 9.203230e-01 | 0.036 |
R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 9.246847e-01 | 0.034 |
R-HSA-71240 | Tryptophan catabolism | 9.288078e-01 | 0.032 |
R-HSA-451927 | Interleukin-2 family signaling | 9.288078e-01 | 0.032 |
R-HSA-5625886 | Activated PKN1 stimulates transcription of AR (androgen receptor) regulated gene... | 9.327055e-01 | 0.030 |
R-HSA-9821002 | Chromatin modifications during the maternal to zygotic transition (MZT) | 9.327055e-01 | 0.030 |
R-HSA-1592230 | Mitochondrial biogenesis | 9.356801e-01 | 0.029 |
R-HSA-74259 | Purine catabolism | 9.388900e-01 | 0.027 |
R-HSA-110329 | Cleavage of the damaged pyrimidine | 9.398731e-01 | 0.027 |
R-HSA-73928 | Depyrimidination | 9.398731e-01 | 0.027 |
R-HSA-2172127 | DAP12 interactions | 9.462779e-01 | 0.024 |
R-HSA-2142691 | Synthesis of Leukotrienes (LT) and Eoxins (EX) | 9.462779e-01 | 0.024 |
R-HSA-3928662 | EPHB-mediated forward signaling | 9.462779e-01 | 0.024 |
R-HSA-373752 | Netrin-1 signaling | 9.462779e-01 | 0.024 |
R-HSA-3000171 | Non-integrin membrane-ECM interactions | 9.468141e-01 | 0.024 |
R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 9.485611e-01 | 0.023 |
R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 9.492200e-01 | 0.023 |
R-HSA-1614558 | Degradation of cysteine and homocysteine | 9.492200e-01 | 0.023 |
R-HSA-76009 | Platelet Aggregation (Plug Formation) | 9.492200e-01 | 0.023 |
R-HSA-15869 | Metabolism of nucleotides | 9.496984e-01 | 0.022 |
R-HSA-2299718 | Condensation of Prophase Chromosomes | 9.520012e-01 | 0.021 |
R-HSA-2187338 | Visual phototransduction | 9.540675e-01 | 0.020 |
R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 9.540733e-01 | 0.020 |
R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 9.540733e-01 | 0.020 |
R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 9.540733e-01 | 0.020 |
R-HSA-437239 | Recycling pathway of L1 | 9.546302e-01 | 0.020 |
R-HSA-70263 | Gluconeogenesis | 9.571153e-01 | 0.019 |
R-HSA-389661 | Glyoxylate metabolism and glycine degradation | 9.594645e-01 | 0.018 |
R-HSA-109704 | PI3K Cascade | 9.616851e-01 | 0.017 |
R-HSA-199418 | Negative regulation of the PI3K/AKT network | 9.620652e-01 | 0.017 |
R-HSA-446203 | Asparagine N-linked glycosylation | 9.621569e-01 | 0.017 |
R-HSA-9864848 | Complex IV assembly | 9.637842e-01 | 0.016 |
R-HSA-156584 | Cytosolic sulfonation of small molecules | 9.637842e-01 | 0.016 |
R-HSA-70895 | Branched-chain amino acid catabolism | 9.637842e-01 | 0.016 |
R-HSA-9610379 | HCMV Late Events | 9.679055e-01 | 0.014 |
R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 9.679055e-01 | 0.014 |
R-HSA-73929 | Base-Excision Repair, AP Site Formation | 9.694170e-01 | 0.013 |
R-HSA-1643685 | Disease | 9.724311e-01 | 0.012 |
R-HSA-209776 | Metabolism of amine-derived hormones | 9.726771e-01 | 0.012 |
R-HSA-112399 | IRS-mediated signalling | 9.741745e-01 | 0.011 |
R-HSA-1483166 | Synthesis of PA | 9.741745e-01 | 0.011 |
R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 9.755900e-01 | 0.011 |
R-HSA-202733 | Cell surface interactions at the vascular wall | 9.758956e-01 | 0.011 |
R-HSA-5619102 | SLC transporter disorders | 9.778010e-01 | 0.010 |
R-HSA-1660661 | Sphingolipid de novo biosynthesis | 9.781927e-01 | 0.010 |
R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 9.782185e-01 | 0.010 |
R-HSA-74752 | Signaling by Insulin receptor | 9.783541e-01 | 0.010 |
R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 9.793711e-01 | 0.009 |
R-HSA-2428928 | IRS-related events triggered by IGF1R | 9.793881e-01 | 0.009 |
R-HSA-375165 | NCAM signaling for neurite out-growth | 9.805181e-01 | 0.009 |
R-HSA-9707616 | Heme signaling | 9.805181e-01 | 0.009 |
R-HSA-9616222 | Transcriptional regulation of granulopoiesis | 9.805181e-01 | 0.009 |
R-HSA-186797 | Signaling by PDGF | 9.805181e-01 | 0.009 |
R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.822294e-01 | 0.008 |
R-HSA-5690714 | CD22 mediated BCR regulation | 9.825958e-01 | 0.008 |
R-HSA-2428924 | IGF1R signaling cascade | 9.825958e-01 | 0.008 |
R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 9.829954e-01 | 0.007 |
R-HSA-2404192 | Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) | 9.835501e-01 | 0.007 |
R-HSA-196071 | Metabolism of steroid hormones | 9.853048e-01 | 0.006 |
R-HSA-9830369 | Kidney development | 9.853048e-01 | 0.006 |
R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.853159e-01 | 0.006 |
R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.856052e-01 | 0.006 |
R-HSA-9638482 | Metal ion assimilation from the host | 9.882730e-01 | 0.005 |
R-HSA-8978934 | Metabolism of cofactors | 9.882730e-01 | 0.005 |
R-HSA-975634 | Retinoid metabolism and transport | 9.882730e-01 | 0.005 |
R-HSA-189445 | Metabolism of porphyrins | 9.882730e-01 | 0.005 |
R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 9.889163e-01 | 0.005 |
R-HSA-425397 | Transport of vitamins, nucleosides, and related molecules | 9.900991e-01 | 0.004 |
R-HSA-1222556 | ROS and RNS production in phagocytes | 9.900991e-01 | 0.004 |
R-HSA-71403 | Citric acid cycle (TCA cycle) | 9.906423e-01 | 0.004 |
R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 9.916410e-01 | 0.004 |
R-HSA-6803157 | Antimicrobial peptides | 9.922290e-01 | 0.003 |
R-HSA-9925561 | Developmental Lineage of Pancreatic Acinar Cells | 9.925333e-01 | 0.003 |
R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 9.925333e-01 | 0.003 |
R-HSA-5579029 | Metabolic disorders of biological oxidation enzymes | 9.925333e-01 | 0.003 |
R-HSA-2871796 | FCERI mediated MAPK activation | 9.926038e-01 | 0.003 |
R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 9.932687e-01 | 0.003 |
R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 9.933304e-01 | 0.003 |
R-HSA-6806667 | Metabolism of fat-soluble vitamins | 9.933304e-01 | 0.003 |
R-HSA-390918 | Peroxisomal lipid metabolism | 9.943695e-01 | 0.002 |
R-HSA-373760 | L1CAM interactions | 9.945081e-01 | 0.002 |
R-HSA-1614635 | Sulfur amino acid metabolism | 9.952469e-01 | 0.002 |
R-HSA-6805567 | Keratinization | 9.955223e-01 | 0.002 |
R-HSA-416476 | G alpha (q) signalling events | 9.960774e-01 | 0.002 |
R-HSA-9824439 | Bacterial Infection Pathways | 9.961034e-01 | 0.002 |
R-HSA-1989781 | PPARA activates gene expression | 9.966128e-01 | 0.001 |
R-HSA-425407 | SLC-mediated transmembrane transport | 9.968878e-01 | 0.001 |
R-HSA-9837999 | Mitochondrial protein degradation | 9.971412e-01 | 0.001 |
R-HSA-8956319 | Nucleotide catabolism | 9.972764e-01 | 0.001 |
R-HSA-2168880 | Scavenging of heme from plasma | 9.974467e-01 | 0.001 |
R-HSA-2730905 | Role of LAT2/NTAL/LAB on calcium mobilization | 9.975870e-01 | 0.001 |
R-HSA-446219 | Synthesis of substrates in N-glycan biosythesis | 9.976591e-01 | 0.001 |
R-HSA-418594 | G alpha (i) signalling events | 9.977534e-01 | 0.001 |
R-HSA-8957275 | Post-translational protein phosphorylation | 9.978449e-01 | 0.001 |
R-HSA-163125 | Post-translational modification: synthesis of GPI-anchored proteins | 9.985492e-01 | 0.001 |
R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 9.986708e-01 | 0.001 |
R-HSA-156580 | Phase II - Conjugation of compounds | 9.988655e-01 | 0.000 |
R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 9.992213e-01 | 0.000 |
R-HSA-2980736 | Peptide hormone metabolism | 9.993790e-01 | 0.000 |
R-HSA-446193 | Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, L... | 9.994393e-01 | 0.000 |
R-HSA-1630316 | Glycosaminoglycan metabolism | 9.994630e-01 | 0.000 |
R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.995697e-01 | 0.000 |
R-HSA-9717189 | Sensory perception of taste | 9.997491e-01 | 0.000 |
R-HSA-611105 | Respiratory electron transport | 9.998207e-01 | 0.000 |
R-HSA-5668914 | Diseases of metabolism | 9.998277e-01 | 0.000 |
R-HSA-9748784 | Drug ADME | 9.998483e-01 | 0.000 |
R-HSA-9664422 | FCGR3A-mediated phagocytosis | 9.998576e-01 | 0.000 |
R-HSA-9664417 | Leishmania phagocytosis | 9.998576e-01 | 0.000 |
R-HSA-9664407 | Parasite infection | 9.998576e-01 | 0.000 |
R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.999117e-01 | 0.000 |
R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 9.999237e-01 | 0.000 |
R-HSA-2142753 | Arachidonate metabolism | 9.999319e-01 | 0.000 |
R-HSA-196854 | Metabolism of vitamins and cofactors | 9.999815e-01 | 0.000 |
R-HSA-3781865 | Diseases of glycosylation | 9.999895e-01 | 0.000 |
R-HSA-428157 | Sphingolipid metabolism | 9.999960e-01 | 0.000 |
R-HSA-9640148 | Infection with Enterobacteria | 9.999965e-01 | 0.000 |
R-HSA-388396 | GPCR downstream signalling | 9.999987e-01 | 0.000 |
R-HSA-8957322 | Metabolism of steroids | 9.999999e-01 | 0.000 |
R-HSA-372790 | Signaling by GPCR | 9.999999e-01 | 0.000 |
R-HSA-1474244 | Extracellular matrix organization | 1.000000e+00 | 0.000 |
R-HSA-211945 | Phase I - Functionalization of compounds | 1.000000e+00 | 0.000 |
R-HSA-211859 | Biological oxidations | 1.000000e+00 | 0.000 |
R-HSA-8978868 | Fatty acid metabolism | 1.000000e+00 | 0.000 |
R-HSA-500792 | GPCR ligand binding | 1.000000e+00 | 0.000 |
R-HSA-556833 | Metabolism of lipids | 1.000000e+00 | 0.000 |
R-HSA-1430728 | Metabolism | 1.000000e+00 | 0.000 |
R-HSA-9709957 | Sensory Perception | 1.000000e+00 | 0.000 |
R-HSA-9752946 | Expression and translocation of olfactory receptors | 1.000000e+00 | -0.000 |
R-HSA-381753 | Olfactory Signaling Pathway | 1.000000e+00 | -0.000 |
Download
kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
---|---|---|---|---|
CLK3 |
0.920 | 0.477 | 1 | 0.906 |
MOS |
0.912 | 0.249 | 1 | 0.874 |
NLK |
0.908 | 0.330 | 1 | 0.913 |
COT |
0.907 | 0.168 | 2 | 0.871 |
CDKL1 |
0.906 | 0.246 | -3 | 0.866 |
PIM3 |
0.904 | 0.225 | -3 | 0.894 |
CDC7 |
0.903 | 0.152 | 1 | 0.848 |
ICK |
0.903 | 0.314 | -3 | 0.892 |
HIPK4 |
0.903 | 0.378 | 1 | 0.854 |
PRPK |
0.903 | -0.038 | -1 | 0.886 |
CAMK1B |
0.902 | 0.137 | -3 | 0.905 |
SRPK1 |
0.902 | 0.341 | -3 | 0.830 |
DYRK2 |
0.902 | 0.418 | 1 | 0.837 |
JNK2 |
0.902 | 0.409 | 1 | 0.800 |
ERK5 |
0.900 | 0.212 | 1 | 0.885 |
SKMLCK |
0.900 | 0.199 | -2 | 0.915 |
CDKL5 |
0.900 | 0.261 | -3 | 0.857 |
DAPK2 |
0.899 | 0.161 | -3 | 0.904 |
HIPK1 |
0.899 | 0.430 | 1 | 0.848 |
CAMLCK |
0.899 | 0.145 | -2 | 0.897 |
BMPR2 |
0.898 | -0.115 | -2 | 0.907 |
NIK |
0.897 | 0.060 | -3 | 0.908 |
JNK3 |
0.897 | 0.375 | 1 | 0.824 |
MTOR |
0.897 | 0.103 | 1 | 0.826 |
HIPK2 |
0.897 | 0.452 | 1 | 0.776 |
ATR |
0.897 | 0.017 | 1 | 0.803 |
CLK2 |
0.897 | 0.444 | -3 | 0.829 |
P38A |
0.896 | 0.370 | 1 | 0.857 |
BMPR1B |
0.895 | 0.219 | 1 | 0.812 |
P38B |
0.895 | 0.384 | 1 | 0.811 |
RAF1 |
0.895 | -0.046 | 1 | 0.822 |
PIM1 |
0.895 | 0.229 | -3 | 0.849 |
CLK4 |
0.895 | 0.346 | -3 | 0.837 |
RSK2 |
0.895 | 0.240 | -3 | 0.842 |
CDK1 |
0.894 | 0.365 | 1 | 0.812 |
P38G |
0.892 | 0.377 | 1 | 0.744 |
CAMK2G |
0.891 | -0.033 | 2 | 0.836 |
GRK1 |
0.891 | 0.186 | -2 | 0.849 |
LATS1 |
0.891 | 0.166 | -3 | 0.894 |
SRPK3 |
0.890 | 0.259 | -3 | 0.803 |
CLK1 |
0.890 | 0.357 | -3 | 0.815 |
CDK5 |
0.890 | 0.346 | 1 | 0.851 |
GRK7 |
0.890 | 0.180 | 1 | 0.786 |
ALK4 |
0.890 | 0.065 | -2 | 0.864 |
CDK18 |
0.889 | 0.383 | 1 | 0.789 |
KIS |
0.889 | 0.384 | 1 | 0.846 |
PDHK4 |
0.889 | -0.242 | 1 | 0.843 |
TGFBR1 |
0.889 | 0.117 | -2 | 0.836 |
CDK8 |
0.889 | 0.325 | 1 | 0.823 |
PKN3 |
0.889 | 0.073 | -3 | 0.874 |
MST4 |
0.889 | 0.102 | 2 | 0.863 |
WNK1 |
0.889 | 0.057 | -2 | 0.919 |
NDR2 |
0.889 | 0.161 | -3 | 0.888 |
DYRK4 |
0.889 | 0.415 | 1 | 0.795 |
ERK1 |
0.889 | 0.354 | 1 | 0.803 |
DYRK1A |
0.889 | 0.363 | 1 | 0.864 |
NUAK2 |
0.889 | 0.114 | -3 | 0.890 |
GRK5 |
0.889 | -0.060 | -3 | 0.872 |
CDK7 |
0.888 | 0.330 | 1 | 0.840 |
P90RSK |
0.888 | 0.181 | -3 | 0.845 |
GRK6 |
0.888 | 0.038 | 1 | 0.828 |
P70S6KB |
0.888 | 0.155 | -3 | 0.853 |
DSTYK |
0.887 | -0.045 | 2 | 0.894 |
SRPK2 |
0.887 | 0.292 | -3 | 0.759 |
HIPK3 |
0.887 | 0.373 | 1 | 0.841 |
CHAK2 |
0.887 | 0.007 | -1 | 0.862 |
PKR |
0.886 | 0.012 | 1 | 0.800 |
NDR1 |
0.886 | 0.110 | -3 | 0.881 |
PRKD1 |
0.886 | 0.174 | -3 | 0.870 |
TBK1 |
0.885 | -0.094 | 1 | 0.718 |
IKKB |
0.885 | -0.052 | -2 | 0.778 |
DYRK1B |
0.885 | 0.380 | 1 | 0.816 |
AMPKA1 |
0.885 | 0.080 | -3 | 0.891 |
MAK |
0.885 | 0.416 | -2 | 0.812 |
CDK13 |
0.885 | 0.314 | 1 | 0.819 |
P38D |
0.884 | 0.376 | 1 | 0.750 |
PRP4 |
0.884 | 0.220 | -3 | 0.788 |
DLK |
0.884 | -0.159 | 1 | 0.808 |
VRK2 |
0.884 | -0.123 | 1 | 0.855 |
CDK17 |
0.884 | 0.351 | 1 | 0.749 |
RSK3 |
0.884 | 0.178 | -3 | 0.836 |
CDK19 |
0.884 | 0.337 | 1 | 0.796 |
PKN2 |
0.883 | 0.074 | -3 | 0.876 |
PKCD |
0.883 | 0.094 | 2 | 0.791 |
CDK14 |
0.883 | 0.363 | 1 | 0.821 |
ALK2 |
0.883 | 0.085 | -2 | 0.842 |
MLK1 |
0.883 | -0.119 | 2 | 0.818 |
PDHK1 |
0.883 | -0.248 | 1 | 0.820 |
RSK4 |
0.882 | 0.233 | -3 | 0.820 |
AURC |
0.882 | 0.214 | -2 | 0.722 |
MEK1 |
0.882 | -0.138 | 2 | 0.851 |
MARK4 |
0.882 | 0.024 | 4 | 0.866 |
TGFBR2 |
0.882 | -0.021 | -2 | 0.825 |
RIPK3 |
0.882 | -0.078 | 3 | 0.747 |
DYRK3 |
0.882 | 0.357 | 1 | 0.836 |
ERK2 |
0.882 | 0.290 | 1 | 0.828 |
CDK3 |
0.882 | 0.330 | 1 | 0.766 |
CAMK2D |
0.882 | 0.038 | -3 | 0.870 |
PRKD2 |
0.881 | 0.191 | -3 | 0.831 |
ANKRD3 |
0.881 | -0.175 | 1 | 0.818 |
ACVR2B |
0.881 | 0.072 | -2 | 0.824 |
CDK12 |
0.881 | 0.324 | 1 | 0.797 |
PKACG |
0.881 | 0.146 | -2 | 0.798 |
MASTL |
0.881 | -0.227 | -2 | 0.847 |
PASK |
0.881 | 0.154 | -3 | 0.902 |
IKKE |
0.880 | -0.115 | 1 | 0.712 |
GAK |
0.880 | 0.145 | 1 | 0.853 |
PAK1 |
0.880 | 0.111 | -2 | 0.841 |
HUNK |
0.879 | -0.120 | 2 | 0.831 |
PIM2 |
0.879 | 0.196 | -3 | 0.813 |
CDK10 |
0.879 | 0.382 | 1 | 0.810 |
ACVR2A |
0.879 | 0.042 | -2 | 0.812 |
ULK2 |
0.879 | -0.214 | 2 | 0.797 |
TSSK2 |
0.879 | 0.011 | -5 | 0.853 |
MLK2 |
0.879 | -0.128 | 2 | 0.827 |
AKT2 |
0.879 | 0.205 | -3 | 0.769 |
NEK6 |
0.879 | -0.065 | -2 | 0.875 |
GCN2 |
0.878 | -0.173 | 2 | 0.820 |
CAMK2B |
0.878 | 0.110 | 2 | 0.806 |
CAMK2A |
0.878 | 0.136 | 2 | 0.823 |
AMPKA2 |
0.878 | 0.088 | -3 | 0.867 |
MAPKAPK3 |
0.877 | 0.084 | -3 | 0.825 |
YSK4 |
0.877 | -0.113 | 1 | 0.756 |
MST3 |
0.877 | 0.068 | 2 | 0.849 |
TSSK1 |
0.877 | 0.067 | -3 | 0.908 |
SGK3 |
0.877 | 0.173 | -3 | 0.819 |
BMPR1A |
0.877 | 0.141 | 1 | 0.789 |
CDK9 |
0.876 | 0.288 | 1 | 0.824 |
MYLK4 |
0.876 | 0.126 | -2 | 0.827 |
PKACB |
0.876 | 0.221 | -2 | 0.732 |
MSK1 |
0.876 | 0.179 | -3 | 0.811 |
CDK16 |
0.876 | 0.349 | 1 | 0.763 |
MPSK1 |
0.876 | 0.143 | 1 | 0.784 |
JNK1 |
0.876 | 0.315 | 1 | 0.794 |
LATS2 |
0.876 | 0.057 | -5 | 0.783 |
NEK7 |
0.876 | -0.205 | -3 | 0.841 |
RIPK1 |
0.875 | -0.177 | 1 | 0.763 |
MAPKAPK2 |
0.875 | 0.150 | -3 | 0.795 |
ATM |
0.875 | -0.027 | 1 | 0.737 |
PLK1 |
0.875 | -0.081 | -2 | 0.815 |
IKKA |
0.875 | -0.012 | -2 | 0.767 |
TAO3 |
0.875 | 0.025 | 1 | 0.787 |
AURB |
0.874 | 0.146 | -2 | 0.717 |
NEK9 |
0.874 | -0.215 | 2 | 0.841 |
MSK2 |
0.874 | 0.118 | -3 | 0.810 |
MLK3 |
0.874 | -0.041 | 2 | 0.751 |
CDK2 |
0.874 | 0.195 | 1 | 0.862 |
DCAMKL1 |
0.874 | 0.101 | -3 | 0.844 |
PKCA |
0.873 | 0.084 | 2 | 0.733 |
PAK3 |
0.873 | 0.048 | -2 | 0.835 |
PRKD3 |
0.873 | 0.125 | -3 | 0.812 |
MOK |
0.873 | 0.354 | 1 | 0.836 |
WNK3 |
0.872 | -0.238 | 1 | 0.776 |
MEK5 |
0.872 | -0.224 | 2 | 0.835 |
GRK4 |
0.872 | -0.100 | -2 | 0.864 |
SMMLCK |
0.872 | 0.083 | -3 | 0.867 |
DAPK3 |
0.872 | 0.158 | -3 | 0.860 |
DNAPK |
0.872 | 0.021 | 1 | 0.683 |
GSK3A |
0.872 | 0.185 | 4 | 0.518 |
TLK2 |
0.872 | -0.079 | 1 | 0.747 |
AURA |
0.871 | 0.134 | -2 | 0.692 |
BRAF |
0.871 | -0.133 | -4 | 0.851 |
MEKK2 |
0.871 | -0.113 | 2 | 0.808 |
PKCB |
0.871 | 0.067 | 2 | 0.739 |
NIM1 |
0.871 | -0.030 | 3 | 0.778 |
PKCG |
0.871 | 0.059 | 2 | 0.745 |
CAMK4 |
0.870 | -0.032 | -3 | 0.860 |
IRE1 |
0.870 | -0.087 | 1 | 0.744 |
GCK |
0.870 | 0.055 | 1 | 0.792 |
PAK2 |
0.870 | 0.031 | -2 | 0.826 |
GRK2 |
0.870 | -0.009 | -2 | 0.755 |
DRAK1 |
0.870 | -0.010 | 1 | 0.764 |
MEKK3 |
0.870 | -0.151 | 1 | 0.784 |
TTBK2 |
0.870 | -0.174 | 2 | 0.732 |
PKG2 |
0.869 | 0.142 | -2 | 0.733 |
QSK |
0.869 | 0.063 | 4 | 0.843 |
MNK2 |
0.868 | 0.080 | -2 | 0.842 |
NEK5 |
0.868 | -0.141 | 1 | 0.785 |
SMG1 |
0.868 | -0.057 | 1 | 0.748 |
PKCZ |
0.868 | 0.011 | 2 | 0.785 |
MELK |
0.868 | 0.015 | -3 | 0.850 |
DAPK1 |
0.868 | 0.161 | -3 | 0.846 |
PRKX |
0.868 | 0.245 | -3 | 0.757 |
NEK2 |
0.868 | -0.129 | 2 | 0.823 |
MLK4 |
0.867 | -0.097 | 2 | 0.734 |
MNK1 |
0.867 | 0.086 | -2 | 0.850 |
PLK3 |
0.867 | -0.085 | 2 | 0.799 |
PDK1 |
0.867 | -0.034 | 1 | 0.769 |
FAM20C |
0.866 | 0.110 | 2 | 0.653 |
PERK |
0.866 | -0.165 | -2 | 0.858 |
MEKK1 |
0.866 | -0.209 | 1 | 0.772 |
GSK3B |
0.866 | 0.091 | 4 | 0.510 |
PKCH |
0.866 | 0.012 | 2 | 0.725 |
TAO2 |
0.866 | -0.071 | 2 | 0.852 |
BCKDK |
0.866 | -0.206 | -1 | 0.798 |
CHK1 |
0.866 | -0.029 | -3 | 0.853 |
QIK |
0.866 | -0.059 | -3 | 0.864 |
WNK4 |
0.866 | -0.081 | -2 | 0.907 |
HPK1 |
0.866 | 0.057 | 1 | 0.778 |
CDK6 |
0.866 | 0.301 | 1 | 0.803 |
CDK4 |
0.865 | 0.315 | 1 | 0.787 |
LKB1 |
0.865 | -0.054 | -3 | 0.832 |
ULK1 |
0.865 | -0.263 | -3 | 0.809 |
TNIK |
0.865 | 0.034 | 3 | 0.864 |
AKT1 |
0.864 | 0.172 | -3 | 0.779 |
ZAK |
0.864 | -0.202 | 1 | 0.745 |
ERK7 |
0.864 | 0.124 | 2 | 0.558 |
ROCK2 |
0.864 | 0.176 | -3 | 0.841 |
MARK3 |
0.863 | 0.038 | 4 | 0.799 |
CHAK1 |
0.863 | -0.171 | 2 | 0.796 |
NEK11 |
0.863 | -0.161 | 1 | 0.772 |
PAK6 |
0.863 | 0.131 | -2 | 0.759 |
DCAMKL2 |
0.863 | 0.015 | -3 | 0.861 |
IRE2 |
0.863 | -0.105 | 2 | 0.749 |
SIK |
0.862 | 0.055 | -3 | 0.818 |
MINK |
0.862 | -0.035 | 1 | 0.764 |
PINK1 |
0.862 | -0.115 | 1 | 0.846 |
SGK1 |
0.862 | 0.204 | -3 | 0.694 |
LRRK2 |
0.862 | -0.094 | 2 | 0.860 |
CAMK1G |
0.862 | 0.042 | -3 | 0.822 |
EEF2K |
0.862 | -0.040 | 3 | 0.834 |
PKACA |
0.861 | 0.184 | -2 | 0.683 |
TAK1 |
0.861 | -0.090 | 1 | 0.787 |
MARK2 |
0.861 | -0.006 | 4 | 0.765 |
TLK1 |
0.861 | -0.144 | -2 | 0.855 |
PHKG1 |
0.861 | -0.016 | -3 | 0.869 |
KHS2 |
0.861 | 0.094 | 1 | 0.778 |
DMPK1 |
0.861 | 0.203 | -3 | 0.825 |
KHS1 |
0.861 | 0.057 | 1 | 0.761 |
HRI |
0.861 | -0.251 | -2 | 0.869 |
MAP3K15 |
0.860 | -0.094 | 1 | 0.738 |
PBK |
0.860 | 0.093 | 1 | 0.784 |
NUAK1 |
0.860 | 0.001 | -3 | 0.843 |
HGK |
0.860 | -0.042 | 3 | 0.862 |
MST2 |
0.860 | -0.116 | 1 | 0.791 |
NEK8 |
0.860 | -0.198 | 2 | 0.826 |
BRSK1 |
0.860 | 0.035 | -3 | 0.845 |
CAMKK2 |
0.859 | -0.166 | -2 | 0.777 |
MEKK6 |
0.859 | -0.096 | 1 | 0.766 |
MRCKB |
0.859 | 0.161 | -3 | 0.800 |
CAMKK1 |
0.859 | -0.232 | -2 | 0.773 |
CK1E |
0.858 | 0.051 | -3 | 0.592 |
MRCKA |
0.857 | 0.140 | -3 | 0.811 |
PLK4 |
0.857 | -0.132 | 2 | 0.657 |
IRAK4 |
0.857 | -0.150 | 1 | 0.740 |
P70S6K |
0.857 | 0.096 | -3 | 0.770 |
CAMK1D |
0.857 | 0.088 | -3 | 0.755 |
CK2A2 |
0.857 | 0.141 | 1 | 0.739 |
MARK1 |
0.856 | -0.032 | 4 | 0.816 |
CK1D |
0.856 | 0.055 | -3 | 0.538 |
NEK4 |
0.855 | -0.174 | 1 | 0.753 |
PKCE |
0.855 | 0.098 | 2 | 0.730 |
LOK |
0.855 | -0.039 | -2 | 0.809 |
NEK1 |
0.854 | -0.148 | 1 | 0.757 |
VRK1 |
0.854 | -0.201 | 2 | 0.832 |
BRSK2 |
0.854 | -0.049 | -3 | 0.852 |
GRK3 |
0.854 | -0.001 | -2 | 0.716 |
SSTK |
0.854 | -0.002 | 4 | 0.835 |
PKCT |
0.853 | 0.019 | 2 | 0.732 |
AKT3 |
0.853 | 0.190 | -3 | 0.712 |
MST1 |
0.853 | -0.148 | 1 | 0.768 |
PKCI |
0.853 | 0.022 | 2 | 0.751 |
SBK |
0.851 | 0.180 | -3 | 0.657 |
BUB1 |
0.851 | 0.100 | -5 | 0.791 |
CK1A2 |
0.851 | 0.037 | -3 | 0.542 |
MAPKAPK5 |
0.851 | -0.047 | -3 | 0.771 |
CHK2 |
0.850 | 0.097 | -3 | 0.715 |
SNRK |
0.850 | -0.177 | 2 | 0.705 |
SLK |
0.849 | -0.074 | -2 | 0.760 |
CRIK |
0.849 | 0.175 | -3 | 0.777 |
YSK1 |
0.849 | -0.096 | 2 | 0.816 |
CK2A1 |
0.848 | 0.126 | 1 | 0.720 |
ROCK1 |
0.847 | 0.138 | -3 | 0.810 |
PLK2 |
0.847 | -0.016 | -3 | 0.811 |
OSR1 |
0.846 | -0.080 | 2 | 0.806 |
PDHK3_TYR |
0.846 | 0.328 | 4 | 0.926 |
TTK |
0.845 | -0.067 | -2 | 0.840 |
MEK2 |
0.845 | -0.308 | 2 | 0.818 |
PAK5 |
0.845 | 0.074 | -2 | 0.705 |
BIKE |
0.845 | 0.054 | 1 | 0.751 |
PHKG2 |
0.844 | -0.026 | -3 | 0.845 |
HASPIN |
0.843 | 0.033 | -1 | 0.737 |
ASK1 |
0.842 | -0.172 | 1 | 0.728 |
CAMK1A |
0.842 | 0.079 | -3 | 0.733 |
PKN1 |
0.842 | 0.050 | -3 | 0.785 |
IRAK1 |
0.842 | -0.357 | -1 | 0.769 |
TTBK1 |
0.841 | -0.219 | 2 | 0.655 |
MYO3B |
0.841 | -0.056 | 2 | 0.835 |
PAK4 |
0.840 | 0.086 | -2 | 0.712 |
ALPHAK3 |
0.840 | -0.068 | -1 | 0.803 |
STK33 |
0.837 | -0.183 | 2 | 0.648 |
MAP2K4_TYR |
0.837 | 0.132 | -1 | 0.899 |
MYO3A |
0.836 | -0.107 | 1 | 0.745 |
PDHK4_TYR |
0.836 | 0.128 | 2 | 0.898 |
CK1G1 |
0.836 | -0.020 | -3 | 0.589 |
MAP2K6_TYR |
0.836 | 0.122 | -1 | 0.899 |
TESK1_TYR |
0.835 | 0.040 | 3 | 0.889 |
PKMYT1_TYR |
0.833 | 0.074 | 3 | 0.861 |
TAO1 |
0.833 | -0.119 | 1 | 0.703 |
BMPR2_TYR |
0.833 | 0.097 | -1 | 0.900 |
NEK3 |
0.833 | -0.211 | 1 | 0.721 |
PDHK1_TYR |
0.831 | 0.044 | -1 | 0.907 |
AAK1 |
0.831 | 0.107 | 1 | 0.665 |
MAP2K7_TYR |
0.831 | -0.104 | 2 | 0.880 |
LIMK2_TYR |
0.830 | 0.105 | -3 | 0.900 |
RIPK2 |
0.830 | -0.355 | 1 | 0.709 |
YANK3 |
0.829 | -0.047 | 2 | 0.441 |
EPHA6 |
0.827 | 0.071 | -1 | 0.879 |
PINK1_TYR |
0.826 | -0.144 | 1 | 0.828 |
EPHB4 |
0.822 | 0.014 | -1 | 0.855 |
STLK3 |
0.822 | -0.284 | 1 | 0.719 |
PKG1 |
0.822 | 0.067 | -2 | 0.651 |
TXK |
0.821 | 0.112 | 1 | 0.835 |
RET |
0.820 | -0.126 | 1 | 0.776 |
LIMK1_TYR |
0.819 | -0.146 | 2 | 0.866 |
ABL2 |
0.818 | 0.008 | -1 | 0.827 |
MST1R |
0.817 | -0.149 | 3 | 0.811 |
FGR |
0.817 | -0.056 | 1 | 0.836 |
YES1 |
0.816 | -0.031 | -1 | 0.862 |
TYRO3 |
0.815 | -0.158 | 3 | 0.792 |
LCK |
0.815 | 0.053 | -1 | 0.856 |
ABL1 |
0.815 | -0.018 | -1 | 0.818 |
ROS1 |
0.814 | -0.145 | 3 | 0.762 |
EPHA4 |
0.814 | -0.023 | 2 | 0.805 |
BLK |
0.814 | 0.080 | -1 | 0.858 |
TNK2 |
0.814 | -0.019 | 3 | 0.759 |
DDR1 |
0.813 | -0.169 | 4 | 0.850 |
CSF1R |
0.813 | -0.126 | 3 | 0.785 |
TYK2 |
0.813 | -0.266 | 1 | 0.769 |
FER |
0.813 | -0.135 | 1 | 0.851 |
JAK2 |
0.812 | -0.206 | 1 | 0.769 |
SRMS |
0.812 | -0.058 | 1 | 0.834 |
HCK |
0.812 | -0.060 | -1 | 0.852 |
JAK3 |
0.811 | -0.140 | 1 | 0.758 |
INSRR |
0.810 | -0.114 | 3 | 0.741 |
ITK |
0.810 | -0.048 | -1 | 0.821 |
FGFR2 |
0.809 | -0.138 | 3 | 0.798 |
FYN |
0.809 | 0.054 | -1 | 0.837 |
EPHB1 |
0.809 | -0.099 | 1 | 0.824 |
EPHB2 |
0.808 | -0.055 | -1 | 0.833 |
EPHB3 |
0.808 | -0.085 | -1 | 0.834 |
MERTK |
0.806 | -0.077 | 3 | 0.773 |
KDR |
0.806 | -0.116 | 3 | 0.752 |
BMX |
0.806 | -0.031 | -1 | 0.755 |
KIT |
0.805 | -0.159 | 3 | 0.788 |
CK1A |
0.805 | 0.008 | -3 | 0.451 |
MET |
0.804 | -0.098 | 3 | 0.783 |
NEK10_TYR |
0.804 | -0.131 | 1 | 0.666 |
TNK1 |
0.804 | -0.109 | 3 | 0.777 |
TNNI3K_TYR |
0.803 | -0.078 | 1 | 0.770 |
JAK1 |
0.803 | -0.110 | 1 | 0.717 |
AXL |
0.802 | -0.170 | 3 | 0.769 |
TEK |
0.802 | -0.179 | 3 | 0.727 |
EPHA7 |
0.802 | -0.072 | 2 | 0.804 |
FLT3 |
0.801 | -0.219 | 3 | 0.791 |
PDGFRB |
0.801 | -0.263 | 3 | 0.797 |
FGFR1 |
0.801 | -0.198 | 3 | 0.761 |
TEC |
0.801 | -0.106 | -1 | 0.756 |
WEE1_TYR |
0.800 | -0.122 | -1 | 0.774 |
PTK2B |
0.799 | -0.039 | -1 | 0.789 |
EPHA3 |
0.799 | -0.141 | 2 | 0.780 |
FLT1 |
0.799 | -0.133 | -1 | 0.850 |
FGFR3 |
0.798 | -0.153 | 3 | 0.767 |
LTK |
0.798 | -0.165 | 3 | 0.738 |
YANK2 |
0.798 | -0.094 | 2 | 0.452 |
BTK |
0.798 | -0.231 | -1 | 0.782 |
PTK2 |
0.797 | 0.060 | -1 | 0.819 |
ALK |
0.797 | -0.189 | 3 | 0.712 |
FRK |
0.797 | -0.115 | -1 | 0.854 |
LYN |
0.796 | -0.104 | 3 | 0.716 |
ERBB2 |
0.796 | -0.198 | 1 | 0.748 |
EPHA1 |
0.796 | -0.136 | 3 | 0.760 |
SRC |
0.795 | -0.063 | -1 | 0.829 |
PTK6 |
0.795 | -0.254 | -1 | 0.747 |
DDR2 |
0.795 | -0.054 | 3 | 0.731 |
EPHA5 |
0.794 | -0.081 | 2 | 0.789 |
NTRK1 |
0.794 | -0.270 | -1 | 0.828 |
EPHA8 |
0.793 | -0.083 | -1 | 0.823 |
SYK |
0.793 | 0.039 | -1 | 0.804 |
CK1G3 |
0.793 | -0.035 | -3 | 0.405 |
PDGFRA |
0.793 | -0.337 | 3 | 0.795 |
INSR |
0.792 | -0.216 | 3 | 0.719 |
MATK |
0.792 | -0.140 | -1 | 0.754 |
EGFR |
0.791 | -0.101 | 1 | 0.661 |
NTRK3 |
0.790 | -0.191 | -1 | 0.782 |
FLT4 |
0.790 | -0.256 | 3 | 0.748 |
CSK |
0.789 | -0.169 | 2 | 0.807 |
NTRK2 |
0.788 | -0.308 | 3 | 0.750 |
FGFR4 |
0.787 | -0.128 | -1 | 0.790 |
EPHA2 |
0.783 | -0.091 | -1 | 0.797 |
ERBB4 |
0.781 | -0.065 | 1 | 0.687 |
IGF1R |
0.778 | -0.194 | 3 | 0.660 |
CK1G2 |
0.776 | -0.032 | -3 | 0.502 |
MUSK |
0.773 | -0.218 | 1 | 0.655 |
ZAP70 |
0.772 | -0.013 | -1 | 0.735 |
FES |
0.767 | -0.172 | -1 | 0.728 |