Motif 1086 (n=291)
Position-wise Probabilities
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uniprot | genes | site | source | protein | function |
---|---|---|---|---|---|
A0A1B0GVI7 | None | T573 | ochoa | Aryl hydrocarbon receptor | None |
A6NKT7 | RGPD3 | T1030 | ochoa | RanBP2-like and GRIP domain-containing protein 3 | None |
O00410 | IPO5 | T633 | ochoa | Importin-5 (Imp5) (Importin subunit beta-3) (Karyopherin beta-3) (Ran-binding protein 5) (RanBP5) | Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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 (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607, PubMed:9687515). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation (By similarity). In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000250|UniProtKB:Q8BKC5, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}. |
O00505 | KPNA3 | T33 | ochoa | Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) (SRP1-gamma) | Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. 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. 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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9. |
O00515 | LAD1 | T387 | ochoa | Ladinin-1 (Lad-1) (Linear IgA disease antigen) (LADA) | Anchoring filament protein which is a component of the basement membrane zone. {ECO:0000250}. |
O00567 | NOP56 | T525 | ochoa | Nucleolar protein 56 (Nucleolar protein 5A) | Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (PubMed:12777385, PubMed:15574333). 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). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) complexes that function in methylation of multiple sites on ribosomal RNAs (rRNAs) and messenger RNAs (mRNAs) (PubMed:12777385, PubMed:39570315). {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:39570315}. |
O00750 | PIK3C2B | T90 | ochoa | Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta (PI3K-C2-beta) (PtdIns-3-kinase C2 subunit beta) (EC 2.7.1.137) (EC 2.7.1.154) (C2-PI3K) (Phosphoinositide 3-kinase-C2-beta) | Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns (PubMed:10805725, PubMed:11533253, PubMed:9830063). Does not phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF and PDGF signaling cascades (PubMed:10805725). {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063}. |
O14544 | SOCS6 | T22 | ochoa | Suppressor of cytokine signaling 6 (SOCS-6) (Cytokine-inducible SH2 protein 4) (CIS-4) (Suppressor of cytokine signaling 4) (SOCS-4) | SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor. {ECO:0000250, ECO:0000269|PubMed:21030588}. |
O14715 | RGPD8 | T1029 | ochoa | RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3) | None |
O14974 | PPP1R12A | T305 | ochoa | Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit) | Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:20354225}. |
O15234 | CASC3 | T155 | 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}. |
O15554 | KCNN4 | T329 | psp | Intermediate conductance calcium-activated potassium channel protein 4 (SKCa 4) (SKCa4) (hSK4) (Gardos channel) (IKCa1) (hIK1) (KCa3.1) (Putative Gardos channel) (hKCa4) | Intermediate conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening (PubMed:10026195, PubMed:10961988, PubMed:11425865, PubMed:15831468, PubMed:17157250, PubMed:18796614, PubMed:26148990, PubMed:9326665, PubMed:9380751, PubMed:9407042). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 25 picosiemens (PubMed:9326665, PubMed:9380751, PubMed:9407042). Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane potential displays positive values, above + 20 mV (PubMed:9326665, PubMed:9380751, PubMed:9407042). Controls calcium influx during vascular contractility by being responsible of membrane hyperpolarization induced by vasoactive factors in proliferative vascular smooth muscle cell types (By similarity). Following calcium influx, the consecutive activation of KCNN4 channel leads to a hyperpolarization of the cell membrane potential and hence an increase of the electrical driving force for further calcium influx promoting sustained calcium entry in response to stimulation with chemotactic peptides (PubMed:26418693). Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:17157250, PubMed:18796614). Plays a role in the late stages of EGF-induced macropinocytosis through activation by PI(3)P (PubMed:24591580). {ECO:0000250|UniProtKB:Q9QYW1, ECO:0000269|PubMed:10026195, ECO:0000269|PubMed:10961988, ECO:0000269|PubMed:11425865, ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:17157250, ECO:0000269|PubMed:18796614, ECO:0000269|PubMed:24591580, ECO:0000269|PubMed:26148990, ECO:0000269|PubMed:26418693, ECO:0000269|PubMed:9326665, ECO:0000269|PubMed:9380751, ECO:0000269|PubMed:9407042}. |
O43306 | ADCY6 | T614 | ochoa | Adenylate cyclase type 6 (EC 4.6.1.1) (ATP pyrophosphate-lyase 6) (Adenylate cyclase type VI) (Adenylyl cyclase 6) (Ca(2+)-inhibitable adenylyl cyclase) | Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:17110384, PubMed:17916776). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:17916776). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA. This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (PubMed:17916776). Contributes to bone cell responses to mechanical stimuli (By similarity). {ECO:0000250|UniProtKB:Q01341, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776}. |
O60271 | SPAG9 | T276 | ochoa | C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (Cancer/testis antigen 89) (CT89) (Human lung cancer oncogene 6 protein) (HLC-6) (JNK-associated leucine-zipper protein) (JLP) (Mitogen-activated protein kinase 8-interacting protein 4) (Proliferation-inducing protein 6) (Protein highly expressed in testis) (PHET) (Sperm surface protein) (Sperm-associated antigen 9) (Sperm-specific protein) (Sunday driver 1) | The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250|UniProtKB:Q58A65, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:29146937}. |
O60934 | NBN | T602 | ochoa | Nibrin (Cell cycle regulatory protein p95) (Nijmegen breakage syndrome protein 1) (hNbs1) | Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:10888888, PubMed:15616588, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:23115235, PubMed:28216226, PubMed:28867292, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19759395, PubMed:28867292, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:19759395, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:19759395, PubMed:28867292, PubMed:9705271). Within the MRN complex, NBN acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed:12419185, PubMed:15616588, PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:19804756, PubMed:23762398, PubMed:24534091, PubMed:27814491, PubMed:27889449, PubMed:33836577). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (PubMed:12419185, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:24534091, PubMed:26438602). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed:15064416, PubMed:15616588, PubMed:15790808, PubMed:16622404, PubMed:22464731, PubMed:30952868, PubMed:35076389). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (PubMed:19759395, PubMed:27814491, PubMed:27889449, PubMed:33836577). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). The MRN complex is also required for the processing of R-loops (PubMed:31537797). NBN also functions in telomere length maintenance via its interaction with TERF2: interaction with TERF2 during G1 phase preventing recruitment of DCLRE1B/Apollo to telomeres (PubMed:10888888, PubMed:28216226). NBN also promotes DNA repair choice at dysfunctional telomeres: NBN phosphorylation by CDK2 promotes non-homologous end joining repair at telomeres, while unphosphorylated NBN promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (PubMed:23762398). {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:15616588, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16622404, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18582474, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:22464731, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26438602, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:28216226, ECO:0000269|PubMed:28867292, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:30952868, ECO:0000269|PubMed:31537797, ECO:0000269|PubMed:33836577, ECO:0000269|PubMed:35076389, ECO:0000269|PubMed:9705271}. |
O75128 | COBL | T447 | ochoa | Protein cordon-bleu | Plays an important role in the reorganization of the actin cytoskeleton. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells (By similarity). Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. {ECO:0000250, ECO:0000269|PubMed:21816349}. |
O75369 | FLNB | T980 | ochoa | Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP) | Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro. |
O75376 | NCOR1 | T561 | ochoa | Nuclear receptor corepressor 1 (N-CoR) (N-CoR1) | Mediates transcriptional repression by certain nuclear receptors (PubMed:20812024). Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Mediates the NR1D1-dependent repression and circadian regulation of TSHB expression (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). {ECO:0000250|UniProtKB:Q60974, ECO:0000269|PubMed:14527417, ECO:0000269|PubMed:20812024}. |
O75475 | PSIP1 | T212 | ochoa | PC4 and SFRS1-interacting protein (CLL-associated antigen KW-7) (Dense fine speckles 70 kDa protein) (DFS 70) (Lens epithelium-derived growth factor) (Transcriptional coactivator p75/p52) | Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. {ECO:0000269|PubMed:15642333}. |
O75691 | UTP20 | T792 | ochoa | Small subunit processome component 20 homolog (Down-regulated in metastasis protein) (Novel nucleolar protein 73) (NNP73) (Protein Key-1A6) | Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. {ECO:0000269|PubMed:17498821, ECO:0000269|PubMed:34516797}. |
O95260 | ATE1 | T119 | ochoa | Arginyl-tRNA--protein transferase 1 (Arginyltransferase 1) (R-transferase 1) (EC 2.3.2.8) (Arginine-tRNA--protein transferase 1) | Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein (PubMed:34893540). This arginylation is required for degradation of the protein via the ubiquitin pathway (PubMed:34893540). Does not arginylate cysteine residues (By similarity). {ECO:0000250|UniProtKB:Q9Z2A5, ECO:0000269|PubMed:34893540}. |
O95340 | PAPSS2 | T579 | ochoa | Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 (PAPS synthase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK 2) (SK2) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] | Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases (PubMed:11773860, PubMed:19474428, PubMed:23824674, PubMed:25594860). In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway (PubMed:11773860, PubMed:19474428, PubMed:23824674, PubMed:25594860). Plays indirectly an important role in skeletogenesis during postnatal growth (PubMed:9771708). {ECO:0000269|PubMed:11773860, ECO:0000269|PubMed:19474428, ECO:0000269|PubMed:23824674, ECO:0000269|PubMed:25594860, ECO:0000269|PubMed:9771708}. |
O95365 | ZBTB7A | T403 | ochoa | Zinc finger and BTB domain-containing protein 7A (Factor binding IST protein 1) (FBI-1) (Factor that binds to inducer of short transcripts protein 1) (HIV-1 1st-binding protein 1) (Leukemia/lymphoma-related factor) (POZ and Krueppel erythroid myeloid ontogenic factor) (POK erythroid myeloid ontogenic factor) (Pokemon) (Pokemon 1) (TTF-I-interacting peptide 21) (TIP21) (Zinc finger protein 857A) | Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:14701838, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26455326, PubMed:26816381). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:12004059, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26816381). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (PubMed:25514493). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (PubMed:25514493). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (By similarity). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (PubMed:12004059). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (PubMed:20812024). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (By similarity). Efficiently abrogates E2F1-dependent CDKN2A transactivation (By similarity). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (By similarity). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (PubMed:26455326). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (PubMed:14701838). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (By similarity). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (By similarity). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (By similarity). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (By similarity). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (PubMed:24514149). {ECO:0000250|UniProtKB:O88939, ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:12004059, ECO:0000269|PubMed:14701838, ECO:0000269|PubMed:17595526, ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:24514149, ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26455326, ECO:0000269|PubMed:26816381}. |
P00558 | PGK1 | T35 | ochoa | Phosphoglycerate kinase 1 (EC 2.7.11.1) (EC 2.7.2.3) (Cell migration-inducing gene 10 protein) (Primer recognition protein 2) (PRP 2) | Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines (PubMed:18463139). In addition to its role as a glycolytic enzyme, it seems that PGK1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). Acts as a protein kinase when localized to the mitochondrion where it phosphorylates pyruvate dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex activity and suppress the formation of acetyl-coenzyme A from pyruvate, and consequently inhibit oxidative phosphorylation and promote glycolysis (PubMed:26942675, PubMed:36849569). May play a role in sperm motility (PubMed:26677959). {ECO:0000269|PubMed:18463139, ECO:0000269|PubMed:2324090, ECO:0000269|PubMed:26677959, ECO:0000269|PubMed:26942675, ECO:0000269|PubMed:30323285, ECO:0000269|PubMed:36849569, ECO:0000269|PubMed:7391028}. |
P04406 | GAPDH | T75 | ochoa|psp | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. |
P05412 | JUN | T90 | ochoa | 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}. |
P06733 | ENO1 | T100 | ochoa | Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein) | Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209). {ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133, ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901, ECO:0000269|PubMed:29775581}.; FUNCTION: [Isoform MBP-1]: Binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}. |
P07205 | PGK2 | T385 | ochoa | Phosphoglycerate kinase 2 (EC 2.7.2.3) (Phosphoglycerate kinase, testis specific) | Essential for sperm motility and male fertility (PubMed:26677959). Not required for the completion of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:P09041, ECO:0000269|PubMed:26677959}. |
P07237 | P4HB | T101 | ochoa | Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (p55) | This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:32149426}. |
P07900 | HSP90AA1 | T601 | ochoa | Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305|PubMed:22066472}. |
P07900 | HSP90AA1 | T713 | ochoa | Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305|PubMed:22066472}. |
P08581 | MET | T977 | ochoa | Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met) | Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (By similarity). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity). {ECO:0000250|UniProtKB:P16056}.; FUNCTION: (Microbial infection) Acts as a receptor for Listeria monocytogenes internalin InlB, mediating entry of the pathogen into cells. {ECO:0000269|PubMed:11081636, ECO:0000305|PubMed:17662939, ECO:0000305|PubMed:19900460}. |
P09936 | UCHL1 | T85 | psp | Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1) | Deubiquitinase that plays a role in the regulation of several processes such as maintenance of synaptic function, cardiac function, inflammatory response or osteoclastogenesis (PubMed:22212137, PubMed:23359680). Abrogates the ubiquitination of multiple proteins including WWTR1/TAZ, EGFR, HIF1A and beta-site amyloid precursor protein cleaving enzyme 1/BACE1 (PubMed:22212137, PubMed:25615526). In addition, recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin to maintain a stable pool of monoubiquitin that is a key requirement for the ubiquitin-proteasome and the autophagy-lysosome pathways (PubMed:12408865, PubMed:8639624, PubMed:9774100). Regulates amyloid precursor protein/APP processing by promoting BACE1 degradation resulting in decreased amyloid beta production (PubMed:22212137). Plays a role in the immune response by regulating the ability of MHC I molecules to reach cross-presentation compartments competent for generating Ag-MHC I complexes (By similarity). Mediates the 'Lys-48'-linked deubiquitination of the transcriptional coactivator WWTR1/TAZ leading to its stabilization and inhibition of osteoclastogenesis (By similarity). Deubiquitinates and stabilizes epidermal growth factor receptor EGFR to prevent its degradation and to activate its downstream mediators (By similarity). Modulates oxidative activity in skeletal muscle by regulating key mitochondrial oxidative proteins (By similarity). Enhances the activity of hypoxia-inducible factor 1-alpha/HIF1A by abrogateing its VHL E3 ligase-mediated ubiquitination and consequently inhibiting its degradation (PubMed:25615526). {ECO:0000250|UniProtKB:Q9R0P9, ECO:0000269|PubMed:12408865, ECO:0000269|PubMed:22212137, ECO:0000269|PubMed:23359680, ECO:0000269|PubMed:25615526, ECO:0000269|PubMed:8639624, ECO:0000269|PubMed:9774100}. |
P0DJD0 | RGPD1 | T1014 | ochoa | RANBP2-like and GRIP domain-containing protein 1 (Ran-binding protein 2-like 6) (RanBP2-like 6) (RanBP2L6) | None |
P0DJD1 | RGPD2 | T1022 | ochoa | RANBP2-like and GRIP domain-containing protein 2 (Ran-binding protein 2-like 2) (RanBP2-like 2) (RanBP2L2) | None |
P0DPH7 | TUBA3C | T381 | ochoa | Tubulin alpha-3C chain (EC 3.6.5.-) (Alpha-tubulin 2) (Alpha-tubulin 3C) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-3C chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
P0DPH8 | TUBA3D | T381 | ochoa | Tubulin alpha-3D chain (EC 3.6.5.-) (Alpha-tubulin 3D) [Cleaved into: Detyrosinated tubulin alpha-3D chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
P10451 | SPP1 | T190 | psp | Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin) | Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. {ECO:0000250|UniProtKB:P10923}. |
P11137 | MAP2 | Y1131 | ochoa | Microtubule-associated protein 2 (MAP-2) | The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. |
P11388 | TOP2A | T1343 | ochoa|psp | DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme) | Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612}. |
P12883 | MYH7 | T70 | ochoa | Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. |
P13569 | CFTR | T604 | psp | Cystic fibrosis transmembrane conductance regulator (CFTR) (ATP-binding cassette sub-family C member 7) (Channel conductance-controlling ATPase) (EC 5.6.1.6) (cAMP-dependent chloride channel) | Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:12529365, PubMed:12588899, PubMed:12727866, PubMed:15010471, PubMed:17036051, PubMed:1712898, PubMed:17182731, PubMed:19398555, PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:26846474, PubMed:28087700, PubMed:8910473, PubMed:9804160). Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (PubMed:11524016, PubMed:15284228, PubMed:26627831, PubMed:8910473). The ion channel is also permeable to HCO(3)(-); selectivity depends on the extracellular chloride concentration (PubMed:15010471, PubMed:19019741). In vitro, mediates ATP-dependent glutathione flux (PubMed:12727866). Exerts its function also by modulating the activity of other ion channels and transporters (PubMed:12403779, PubMed:22121115, PubMed:22178883, PubMed:27941075). Plays an important role in airway fluid homeostasis (PubMed:16645176, PubMed:19621064, PubMed:26823428). Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens (PubMed:14668433, PubMed:16645176, PubMed:26823428). Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex (PubMed:17182731, PubMed:17434346, PubMed:27941075). Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731). Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731, PubMed:27941075). May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7 (PubMed:12403779). Can inhibit the chloride channel activity of ANO1 (PubMed:22178883). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:19923167, PubMed:27714810, PubMed:29393851). {ECO:0000269|PubMed:10792060, ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:12403779, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:12588899, ECO:0000269|PubMed:12727866, ECO:0000269|PubMed:14668433, ECO:0000269|PubMed:15010471, ECO:0000269|PubMed:15284228, ECO:0000269|PubMed:16645176, ECO:0000269|PubMed:17036051, ECO:0000269|PubMed:1712898, ECO:0000269|PubMed:17182731, ECO:0000269|PubMed:19019741, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:19621064, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:26627831, ECO:0000269|PubMed:26823428, ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:27714810, ECO:0000269|PubMed:27941075, ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:29393851, ECO:0000269|PubMed:8910473, ECO:0000269|PubMed:9804160, ECO:0000305|PubMed:19923167}. |
P14625 | HSP90B1 | T155 | ochoa | Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) | ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}. |
P15153 | RAC2 | T167 | ochoa | Ras-related C3 botulinum toxin substrate 2 (EC 3.6.5.2) (GX) (Small G protein) (p21-Rac2) | Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state (PubMed:30723080). In its active state, binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Regulatory subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:1660188). {ECO:0000269|PubMed:1660188, ECO:0000269|PubMed:30723080}. |
P17706 | PTPN2 | T310 | ochoa | Tyrosine-protein phosphatase non-receptor type 2 (EC 3.1.3.48) (T-cell protein-tyrosine phosphatase) (TCPTP) | Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Also plays an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA. {ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15592458, ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:9488479}. |
P18206 | VCL | T719 | ochoa | Vinculin (Metavinculin) (MV) | Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}. |
P19525 | EIF2AK2 | T89 | ochoa|psp | Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase) | IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:Q03963, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035, ECO:0000269|PubMed:32197074}. |
P19525 | EIF2AK2 | T258 | psp | Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase) | IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:Q03963, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035, ECO:0000269|PubMed:32197074}. |
P20336 | RAB3A | T193 | ochoa | Ras-related protein Rab-3A (EC 3.6.5.2) | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:2501306). 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:2501306). RAB3A plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (PubMed:2501306). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (PubMed:27325790). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (PubMed:22248876, PubMed:30599141). Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). {ECO:0000250|UniProtKB:P63011, ECO:0000250|UniProtKB:P63012, ECO:0000269|PubMed:22248876, ECO:0000269|PubMed:2501306, ECO:0000269|PubMed:27325790, ECO:0000269|PubMed:30599141}. |
P21359 | NF1 | T2540 | ochoa | Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated] | Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269|PubMed:2121371, ECO:0000269|PubMed:8417346}. |
P23508 | MCC | T712 | ochoa | Colorectal mutant cancer protein (Protein MCC) | Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}. |
P24534 | EEF1B2 | T93 | 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}. |
P27797 | CALR | T229 | ochoa | Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (grp60) | Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity). {ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7, ECO:0000269|PubMed:11149926, ECO:0000269|PubMed:7876246}. |
P29375 | KDM5A | T209 | ochoa | Lysine-specific demethylase 5A (EC 1.14.11.67) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2) ([histone H3]-trimethyl-L-lysine(4) demethylase 5A) | Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511). May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228). {ECO:0000250|UniProtKB:Q3UXZ9, ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:15949438, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17320163, ECO:0000269|PubMed:18270511, ECO:0000269|PubMed:19430464, ECO:0000269|PubMed:27427228}. |
P30044 | PRDX5 | T103 | ochoa | Peroxiredoxin-5, mitochondrial (EC 1.11.1.24) (Alu corepressor 1) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 71B) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (TPx type VI) (Thioredoxin peroxidase PMP20) (Thioredoxin-dependent peroxiredoxin 5) | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:31740833}. |
P30260 | CDC27 | T430 | ochoa | Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (APC3) (CDC27 homolog) (CDC27Hs) (H-NUC) | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:29033132}. |
P30533 | LRPAP1 | T141 | ochoa | Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) | Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway. {ECO:0000269|PubMed:32296178, ECO:0000269|PubMed:7774585}. |
P32298 | GRK4 | T256 | 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}. |
P33981 | TTK | T46 | ochoa|psp | Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) | Involved in mitotic spindle assembly checkpoint signaling, a process that delays anaphase until chromosomes are bioriented on the spindle, and in the repair of incorrect mitotic kinetochore-spindle microtubule attachments (PubMed:18243099, PubMed:28441529, PubMed:29162720). Phosphorylates MAD1L1 to promote the mitotic spindle assembly checkpoint (PubMed:18243099, PubMed:29162720). Phosphorylates CDCA8/Borealin leading to enhanced AURKB activity at the kinetochore (PubMed:18243099). Phosphorylates SKA3 at 'Ser-34' leading to dissociation of the SKA complex from microtubules and destabilization of microtubule-kinetochore attachments (PubMed:28441529). Phosphorylates KNL1, KNTC1 and autophosphorylates (PubMed:28441529). Phosphorylates MCRS1 which enhances recruitment of KIF2A to the minus end of spindle microtubules and promotes chromosome alignment (PubMed:30785839). {ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:28441529, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:30785839}. |
P35251 | RFC1 | T171 | ochoa | Replication factor C subunit 1 (Activator 1 140 kDa subunit) (A1 140 kDa subunit) (Activator 1 large subunit) (Activator 1 subunit 1) (DNA-binding protein PO-GA) (Replication factor C 140 kDa subunit) (RF-C 140 kDa subunit) (RFC140) (Replication factor C large subunit) | 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 (PubMed:9488738). This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Can bind single- or double-stranded DNA. {ECO:0000269|PubMed:8999859, ECO:0000269|PubMed:9488738}. |
P35869 | AHR | T583 | ochoa | Aryl hydrocarbon receptor (Ah receptor) (AhR) (Class E basic helix-loop-helix protein 76) (bHLHe76) | Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:23275542, PubMed:30373764, PubMed:32818467, PubMed:7961644). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed:23275542, PubMed:30373764, PubMed:7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:12213388). Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed:7961644, PubMed:33193710). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (PubMed:34521881, PubMed:7961644). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (PubMed:18076143). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (PubMed:32818467, PubMed:32866000). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (PubMed:28602820). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed:28602820). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820). {ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:30373764, ECO:0000269|PubMed:32818467, ECO:0000269|PubMed:32866000, ECO:0000269|PubMed:33193710, ECO:0000269|PubMed:34521881, ECO:0000269|PubMed:7961644, ECO:0000303|PubMed:12213388, ECO:0000303|PubMed:18076143}. |
P36952 | SERPINB5 | T157 | psp | Serpin B5 (Maspin) (Peptidase inhibitor 5) (PI-5) | Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. |
P41208 | CETN2 | T26 | ochoa | Centrin-2 (Caltractin isoform 1) | Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; FUNCTION: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}. |
P42166 | TMPO | T164 | ochoa | Lamina-associated polypeptide 2, isoform alpha (Thymopoietin isoform alpha) (TP alpha) (Thymopoietin-related peptide isoform alpha) (TPRP isoform alpha) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)] | May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide. |
P42574 | CASP3 | T174 | ochoa | Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12] | Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:35338844, PubMed:35446120, PubMed:7596430). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:7596430). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed:10497198, PubMed:16374543, PubMed:7596430, PubMed:7774019). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed:7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed:37993714, PubMed:9334240). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed:35338844, PubMed:35446120). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758104, PubMed:36758106). {ECO:0000250|UniProtKB:Q60431, ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:16374543, ECO:0000269|PubMed:18723680, ECO:0000269|PubMed:20566630, ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:23152800, ECO:0000269|PubMed:23650375, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:30878284, ECO:0000269|PubMed:33725486, ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36758104, ECO:0000269|PubMed:36758106, ECO:0000269|PubMed:37993714, ECO:0000269|PubMed:7596430, ECO:0000269|PubMed:7774019, ECO:0000269|PubMed:8696339, ECO:0000269|PubMed:9334240}. |
P42858 | HTT | T269 | psp | Huntingtin (Huntington disease protein) (HD protein) [Cleaved into: Huntingtin, myristoylated N-terminal fragment] | [Huntingtin]: May play a role in microtubule-mediated transport or vesicle function.; FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the formation of autophagic vesicles. {ECO:0000269|PubMed:24459296}. |
P46013 | MKI67 | T1237 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
P46013 | MKI67 | T1967 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
P46013 | MKI67 | T2931 | ochoa | Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67) | Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636). {ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:28935370, ECO:0000269|PubMed:32879492, ECO:0000269|PubMed:35513709, ECO:0000269|PubMed:39153474}. |
P46087 | NOP2 | T663 | ochoa | 28S rRNA (cytosine(4447)-C(5))-methyltransferase (EC 2.1.1.-) (Nucleolar protein 1) (Nucleolar protein 2 homolog) (Proliferating-cell nucleolar antigen p120) (Proliferation-associated nucleolar protein p120) | S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA (PubMed:26196125). Required for efficient rRNA processing and 60S ribosomal subunit biogenesis (PubMed:24120868, PubMed:36161484). Regulates pre-rRNA processing through non-catalytic complex formation with box C/D snoRNAs and facilitates the recruitment of U3 and U8 snoRNAs to pre-90S ribosomal particles and their stable assembly into snoRNP complexes (PubMed:36161484). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (PubMed:24120868). {ECO:0000269|PubMed:24120868, ECO:0000269|PubMed:26196125, ECO:0000269|PubMed:36161484}. |
P47712 | PLA2G4A | T447 | ochoa | Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] | Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:18451993, PubMed:27642067, PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:8619991, PubMed:9425121). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:10358058, PubMed:17472963, PubMed:18451993, PubMed:7794891, PubMed:9425121). In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891). Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891). {ECO:0000250|UniProtKB:P47713, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602, ECO:0000269|PubMed:9425121}. |
P48730 | CSNK1D | T161 | psp | Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26) | Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}. |
P49792 | RANBP2 | T2005 | ochoa | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270) | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}. |
P50851 | LRBA | T2194 | 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}. |
P51587 | BRCA2 | T363 | ochoa | Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein) | Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180). {ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:20729832, ECO:0000269|PubMed:20729858, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21719596, ECO:0000269|PubMed:24485656, ECO:0000269|PubMed:24896180}. |
P54132 | BLM | T150 | ochoa | RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein) (DNA 3'-5' helicase BLM) (DNA helicase, RecQ-like type 2) (RecQ2) (RecQ protein-like 3) | ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity). {ECO:0000250|UniProtKB:O88700, ECO:0000269|PubMed:12019152, ECO:0000269|PubMed:18426915, ECO:0000269|PubMed:20639533, ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:24257077, ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0000269|PubMed:34606619, ECO:0000269|PubMed:9388193, ECO:0000269|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269|PubMed:32690953}. |
P54278 | PMS2 | T597 | ochoa | Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2) | Component of the post-replicative DNA mismatch repair system (MMR) (PubMed:30653781, PubMed:35189042). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (PubMed:35189042). {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974, ECO:0000269|PubMed:23709753, ECO:0000269|PubMed:30653781, ECO:0000269|PubMed:35189042}. |
P54296 | MYOM2 | T901 | ochoa | Myomesin-2 (165 kDa connectin-associated protein) (165 kDa titin-associated protein) (M-protein) (Myomesin family member 2) | Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent. |
P60763 | RAC3 | T167 | ochoa | Ras-related C3 botulinum toxin substrate 3 (EC 3.6.5.2) (p21-Rac3) | Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}. |
P60900 | PSMA6 | T173 | ochoa | Proteasome subunit alpha type-6 (27 kDa prosomal protein) (PROS-27) (p27K) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain) (Proteasome subunit alpha-1) (alpha-1) | 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}. |
P61160 | ACTR2 | T117 | ochoa | Actin-related protein 2 (Actin-like protein 2) | ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9000076). Seems to contact the pointed end of the daughter actin filament (PubMed:9000076). In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:17220302, PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29058690, ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9000076}. |
P61160 | ACTR2 | T237 | psp | Actin-related protein 2 (Actin-like protein 2) | ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9000076). Seems to contact the pointed end of the daughter actin filament (PubMed:9000076). In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:17220302, PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29058690, ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9000076}. |
P61981 | YWHAG | T70 | ochoa | 14-3-3 protein gamma (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein gamma, N-terminally processed] | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binding generally results in the modulation of the activity of the binding partner (PubMed:16511572). Promotes inactivation of WDR24 component of the GATOR2 complex by binding to phosphorylated WDR24 (PubMed:36732624). Participates in the positive regulation of NMDA glutamate receptor activity by promoting the L-glutamate secretion through interaction with BEST1 (PubMed:29121962). Reduces keratinocyte intercellular adhesion, via interacting with PKP1 and sequestering it in the cytoplasm, thereby reducing its incorporation into desmosomes (PubMed:29678907). Plays a role in mitochondrial protein catabolic process (also named MALM) that promotes the degradation of damaged proteins inside mitochondria (PubMed:22532927). {ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:22532927, ECO:0000269|PubMed:29121962, ECO:0000269|PubMed:29678907, ECO:0000269|PubMed:36732624}. |
P63000 | RAC1 | T167 | ochoa | Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (Cell migration-inducing gene 5 protein) (Ras-like protein TC25) (p21-Rac1) | Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles (PubMed:1643658, PubMed:22843693, PubMed:23512198, PubMed:28886345). Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity (PubMed:9121475). In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts (PubMed:1643658). In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In neurons, is involved in dendritic spine formation and synaptic plasticity (By similarity). In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX (PubMed:12695502). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization (By similarity). Required for DSG3 translocation to cell-cell junctions, DSG3-mediated organization of cortical F-actin bundles and anchoring of actin at cell junctions; via interaction with DSG3 (PubMed:22796473). Subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:38355798). {ECO:0000250|UniProtKB:P63001, ECO:0000250|UniProtKB:Q6RUV5, ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:1643658, ECO:0000269|PubMed:22796473, ECO:0000269|PubMed:22843693, ECO:0000269|PubMed:23512198, ECO:0000269|PubMed:28886345, ECO:0000269|PubMed:38355798, ECO:0000269|PubMed:9121475}.; FUNCTION: [Isoform B]: Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins (PubMed:14625275). It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction (PubMed:14625275). {ECO:0000269|PubMed:14625275}. |
P63244 | RACK1 | T192 | psp | 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}. |
P68104 | EEF1A1 | T23 | ochoa | Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (Leukocyte receptor cluster member 7) | Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity). {ECO:0000250|UniProtKB:P68105, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:26593721, ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.; FUNCTION: (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. {ECO:0000269|PubMed:33495306}. |
P68363 | TUBA1B | T381 | ochoa | Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] | Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661}. |
P68366 | TUBA4A | T381 | ochoa | Tubulin alpha-4A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Testis-specific alpha-tubulin) (Tubulin H2-alpha) (Tubulin alpha-1 chain) | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
P98082 | DAB2 | T730 | ochoa | Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2) | Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:16267015, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19306879, ECO:0000269|PubMed:21995445, ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22491013}. |
P98172 | EFNB1 | T309 | ochoa | Ephrin-B1 (EFL-3) (ELK ligand) (ELK-L) (EPH-related receptor tyrosine kinase ligand 2) (LERK-2) [Cleaved into: Ephrin-B1 C-terminal fragment (Ephrin-B1 CTF); Ephrin-B1 intracellular domain (Ephrin-B1 ICD)] | Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:7973638, PubMed:8070404). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:7973638, PubMed:8070404). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:7973638, PubMed:8070404). Can also bind EPHB2 and EPHB3 (PubMed:8070404). Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity). {ECO:0000250|UniProtKB:P52795, ECO:0000269|PubMed:7973638, ECO:0000269|PubMed:8070404}. |
Q03393 | PTS | T58 | psp | 6-pyruvoyl tetrahydrobiopterin synthase (PTP synthase) (PTPS) (EC 4.2.3.12) | Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. {ECO:0000269|PubMed:1282802}. |
Q04759 | PRKCQ | T219 | ochoa|psp | Protein kinase C theta type (EC 2.7.11.13) (nPKC-theta) | Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation (PubMed:21964608). Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange factor activity (PubMed:23509302). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). {ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:14988727, ECO:0000269|PubMed:15364919, ECO:0000269|PubMed:16252004, ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16709830, ECO:0000269|PubMed:19549985, ECO:0000269|PubMed:21964608, ECO:0000269|PubMed:23509302, ECO:0000269|PubMed:36040231, ECO:0000269|PubMed:8657160}. |
Q05639 | EEF1A2 | T23 | ochoa | Elongation factor 1-alpha 2 (EF-1-alpha-2) (EC 3.6.5.-) (Eukaryotic elongation factor 1 A-2) (eEF1A-2) (Statin-S1) | Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (By similarity). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (By similarity). {ECO:0000250|UniProtKB:P68104, ECO:0000250|UniProtKB:Q71V39}. |
Q05655 | PRKCD | T218 | ochoa|psp | Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)] | Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses (PubMed:21406692, PubMed:21810427). Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (By similarity). Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis (PubMed:21406692, PubMed:21810427). In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53 (PubMed:21406692, PubMed:21810427). In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53 (PubMed:21406692, PubMed:21810427). In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation (By similarity). Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1 (PubMed:15774464). Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways (PubMed:19801500). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA (PubMed:11748588). In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation (PubMed:16940418). Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release (PubMed:19587372). Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (PubMed:11877440). The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (PubMed:12649167). Phosphorylates SMPD1 which induces SMPD1 secretion (PubMed:17303575). {ECO:0000250|UniProtKB:P28867, ECO:0000269|PubMed:11748588, ECO:0000269|PubMed:11877440, ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:16940418, ECO:0000269|PubMed:17303575, ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19587372, ECO:0000269|PubMed:19801500, ECO:0000303|PubMed:21406692, ECO:0000303|PubMed:21810427}. |
Q05682 | CALD1 | T217 | ochoa | Caldesmon (CDM) | Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250, ECO:0000269|PubMed:8227296}. |
Q06546 | GABPA | T23 | ochoa | GA-binding protein alpha chain (GABP subunit alpha) (Nuclear respiratory factor 2 subunit alpha) (Transcription factor E4TF1-60) | Transcription factor capable of interacting with purine rich repeats (GA repeats). Positively regulates transcription of transcriptional repressor RHIT/ZNF205 (PubMed:22306510). {ECO:0000269|PubMed:22306510}.; FUNCTION: (Microbial infection) Necessary for the expression of the Adenovirus E4 gene. |
Q08357 | SLC20A2 | T390 | ochoa | Sodium-dependent phosphate transporter 2 (Gibbon ape leukemia virus receptor 2) (GLVR-2) (Phosphate transporter 2) (PiT-2) (Pit2) (hPit2) (Solute carrier family 20 member 2) | Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:12205090, PubMed:15955065, PubMed:16790504, PubMed:17494632, PubMed:22327515, PubMed:28722801, PubMed:30704756). Plays a critical role in the determination of bone quality and strength by providing phosphate for bone mineralization (By similarity). Required to maintain normal cerebrospinal fluid phosphate levels (By similarity). Mediates phosphate-induced calcification of vascular smooth muscle cells (VCMCs) and can functionally compensate for loss of SLC20A1 in VCMCs (By similarity). {ECO:0000250|UniProtKB:Q80UP8, ECO:0000269|PubMed:12205090, ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:17494632, ECO:0000269|PubMed:22327515, ECO:0000269|PubMed:28722801, ECO:0000269|PubMed:30704756}.; FUNCTION: (Microbial infection) Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. {ECO:0000269|PubMed:11435563, ECO:0000269|PubMed:12205090, ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:8302848}. |
Q09666 | AHNAK | T4999 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q09666 | AHNAK | T5839 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q12830 | BPTF | T2684 | ochoa | Nucleosome-remodeling factor subunit BPTF (Bromodomain and PHD finger-containing transcription factor) (Fetal Alz-50 clone 1 protein) (Fetal Alzheimer antigen) | Regulatory subunit of the ATP-dependent NURF-1 and NURF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:14609955, PubMed:28801535). The NURF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NURF-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NURF-1 ISWI chromatin-remodeling complex, binds to the promoters of En1 and En2 to positively regulate their expression and promote brain development (PubMed:14609955). Histone-binding protein which binds to H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of active genes (PubMed:16728976, PubMed:16728978). Binds to histone H3 tails dimethylated on 'Lys-4' (H3K4Me2) to a lesser extent (PubMed:16728976, PubMed:16728978, PubMed:18042461). May also regulate transcription through direct binding to DNA or transcription factors (PubMed:10575013). {ECO:0000269|PubMed:10575013, ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:16728976, ECO:0000269|PubMed:16728978, ECO:0000269|PubMed:18042461, ECO:0000269|PubMed:28801535}. |
Q12888 | TP53BP1 | T1156 | ochoa | TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1) | Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}. |
Q12893 | TMEM115 | T269 | ochoa | Transmembrane protein 115 (Placental protein 6) (Protein PL6) | May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi. {ECO:0000269|PubMed:24806965}. |
Q13033 | STRN3 | T293 | ochoa | Striatin-3 (Cell cycle autoantigen SG2NA) (S/G2 antigen) | Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:30622739, 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. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). {ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:30622739, ECO:0000269|PubMed:33633399, ECO:0000305|PubMed:26876214}. |
Q13043 | STK4 | T440 | ochoa | Serine/threonine-protein kinase 4 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 1) (MST-1) (STE20-like kinase MST1) (Serine/threonine-protein kinase Krs-2) [Cleaved into: Serine/threonine-protein kinase 4 37kDa subunit (MST1/N); Serine/threonine-protein kinase 4 18kDa subunit (MST1/C)] | Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of 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 LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q9JI11, ECO:0000269|PubMed:11278283, ECO:0000269|PubMed:11517310, ECO:0000269|PubMed:12757711, ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:16510573, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:17932490, ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:19525978, ECO:0000269|PubMed:21212262, ECO:0000269|PubMed:21245099, ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:8702870, ECO:0000269|PubMed:8816758}. |
Q13155 | AIMP2 | T90 | ochoa | Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) | Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. {ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:19131329}. |
Q13315 | ATM | T86 | psp | Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated) (A-T mutated) | Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15064416, PubMed:15448695, PubMed:15456891, PubMed:15790808, PubMed:15916964, PubMed:17923702, PubMed:21757780, PubMed:24534091, PubMed:35076389, PubMed:9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15448695, PubMed:15456891, PubMed:15916964, PubMed:17923702, PubMed:24534091, PubMed:9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, FBXO46, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:10550055, PubMed:10766245, PubMed:10802669, PubMed:10839545, PubMed:10910365, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:21757780, PubMed:24534091, PubMed:26240375, PubMed:26774286, PubMed:30171069, PubMed:30612738, PubMed:30886146, PubMed:30952868, PubMed:38128537, PubMed:9733515, PubMed:9843217). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (PubMed:19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed:15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed:15448695). Also involved in pexophagy by mediating phosphorylation of PEX5: translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed:26344566). {ECO:0000250|UniProtKB:Q62388, ECO:0000269|PubMed:10550055, ECO:0000269|PubMed:10766245, ECO:0000269|PubMed:10802669, ECO:0000269|PubMed:10839545, ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:11375976, ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:19965871, ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26240375, ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:26774286, ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:30171069, ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:30952868, ECO:0000269|PubMed:35076389, ECO:0000269|PubMed:38128537, ECO:0000269|PubMed:9733514, ECO:0000269|PubMed:9733515, ECO:0000269|PubMed:9843217}. |
Q13362 | PPP2R5C | T385 | ochoa | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29) | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and might also direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation. {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:17245430}. |
Q13428 | TCOF1 | T1382 | ochoa | Treacle protein (Treacher Collins syndrome protein) | Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:26399832}. |
Q13428 | TCOF1 | T1384 | ochoa | Treacle protein (Treacher Collins syndrome protein) | Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:26399832}. |
Q13428 | TCOF1 | T1385 | ochoa | Treacle protein (Treacher Collins syndrome protein) | Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:12777385, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:26399832}. |
Q13464 | ROCK1 | T1334 | psp | Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK) | Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}. |
Q13469 | NFATC2 | T116 | ochoa | Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1) | Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF (PubMed:15790681). Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (PubMed:21871017). Is involved in the negative regulation of chondrogenesis (PubMed:35789258). Recruited by AKAP5 to ORAI1 pore-forming subunit of CRAC channels in Ca(2+) signaling microdomains where store-operated Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT-dependent transcriptional responses. {ECO:0000250|UniProtKB:Q60591, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:21871017, ECO:0000269|PubMed:35789258}. |
Q13642 | FHL1 | T120 | 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. |
Q13905 | RAPGEF1 | T247 | ochoa | Rap guanine nucleotide exchange factor 1 (CRK SH3-binding GNRP) (Guanine nucleotide-releasing factor 2) (Protein C3G) | Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1 (PubMed:12432078). Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269|PubMed:12432078, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:7806500}. |
Q14151 | SAFB2 | T81 | 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. |
Q14191 | WRN | T1100 | ochoa | Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN (DNA helicase, RecQ-like type 3) (RecQ protein-like 2) (Werner syndrome protein) [Includes: 3'-5' exonuclease (EC 3.1.-.-); ATP-dependent helicase (EC 5.6.2.4) (DNA 3'-5' helicase WRN)] | Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates (PubMed:9224595, PubMed:9288107, PubMed:9611231). Also has 3'->5' exonuclease activity towards double-stranded (ds)DNA with a 5'-overhang (PubMed:11863428). Has no nuclease activity towards single-stranded (ss)DNA or blunt-ended dsDNA (PubMed:11863428). Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding-protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3) (PubMed:9611231). Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation (PubMed:9224595, PubMed:9288107, PubMed:9611231). Unwinds some G-quadruplex DNA (d(CGG)n tracts); unwinding seems to occur in both 5'-3' and 3'-5' direction and requires a short single-stranded tail (PubMed:10212265). d(CGG)n tracts have a propensity to assemble into tetraplex structures; other G-rich substrates from a telomeric or IgG switch sequence are not unwound (PubMed:10212265). Depletion leads to chromosomal breaks and genome instability (PubMed:33199508). {ECO:0000250|UniProtKB:O09053, ECO:0000269|PubMed:10212265, ECO:0000269|PubMed:11863428, ECO:0000269|PubMed:17563354, ECO:0000269|PubMed:18596042, ECO:0000269|PubMed:19283071, ECO:0000269|PubMed:19652551, ECO:0000269|PubMed:21639834, ECO:0000269|PubMed:27063109, ECO:0000269|PubMed:33199508, ECO:0000269|PubMed:9224595, ECO:0000269|PubMed:9288107, ECO:0000269|PubMed:9611231}. |
Q14653 | IRF3 | T333 | ochoa | Interferon regulatory factor 3 (IRF-3) | Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:22394562, PubMed:25636800, PubMed:27302953, PubMed:36603579). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16154084, PubMed:27302953, PubMed:33440148, PubMed:36603579). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591). In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis (PubMed:25609812). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). {ECO:0000269|PubMed:16154084, ECO:0000269|PubMed:22394562, ECO:0000269|PubMed:24049179, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:27302953, ECO:0000269|PubMed:31340999, ECO:0000269|PubMed:31413131, ECO:0000269|PubMed:32972995, ECO:0000269|PubMed:33440148, ECO:0000269|PubMed:36603579, ECO:0000269|PubMed:8524823, ECO:0000303|PubMed:11846977, ECO:0000303|PubMed:16846591, ECO:0000303|PubMed:16979567, ECO:0000303|PubMed:20049431}. |
Q14686 | NCOA6 | T935 | ochoa | Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC RAP250) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein) | Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins. |
Q15042 | RAB3GAP1 | T386 | 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}. |
Q15208 | STK38 | T243 | 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}. |
Q15560 | TCEA2 | T260 | ochoa | Transcription elongation factor A protein 2 (Testis-specific S-II) (Transcription elongation factor S-II protein 2) (Transcription elongation factor TFIIS.l) | Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. {ECO:0000269|PubMed:12034815}. |
Q15910 | EZH2 | T261 | psp | Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6) | Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2 (PubMed:22323599, PubMed:30923826). Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. {ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16179254, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:16717091, ECO:0000269|PubMed:16936726, ECO:0000269|PubMed:17210787, ECO:0000269|PubMed:17344414, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:22323599, ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:24474760, ECO:0000269|PubMed:30026490, ECO:0000269|PubMed:30923826}. |
Q16181 | SEPTIN7 | T318 | ochoa | Septin-7 (CDC10 protein homolog) | Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). {ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18460473, ECO:0000305|PubMed:25588830}. |
Q16666 | IFI16 | T117 | ochoa | Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator) | Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:24198334, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9642285}.; FUNCTION: [Isoform IFI16-beta]: Isoform that specifically inhibits the AIM2 inflammasome (PubMed:30104205). Binds double-stranded DNA (dsDNA) in the cytoplasm, impeding its detection by AIM2 (PubMed:30104205). Also prevents the interaction between AIM2 and PYCARD/ASC via its interaction with AIM2, thereby inhibiting assembly of the AIM2 inflammasome (PubMed:30104205). This isoform also weakly induce production of type I interferon-beta (IFNB1) via its interaction with STING1 (PubMed:30104205). {ECO:0000269|PubMed:30104205}. |
Q2TB10 | ZNF800 | T319 | ochoa | Zinc finger protein 800 | May be involved in transcriptional regulation. |
Q4G0J3 | LARP7 | T338 | ochoa | La-related protein 7 (La ribonucleoprotein domain family member 7) (hLARP7) (P-TEFb-interaction protein for 7SK stability) (PIP7S) | RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function (PubMed:18249148, PubMed:32017898). Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (PubMed:18249148, PubMed:18483487). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:18249148, PubMed:18483487). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (PubMed:18281698, PubMed:18483487). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing (PubMed:32017898). Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes (PubMed:32017898). U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity (PubMed:32017898). Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (PubMed:32017898). U6 snRNA processing is required for spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q05CL8, ECO:0000269|PubMed:18249148, ECO:0000269|PubMed:18281698, ECO:0000269|PubMed:18483487, ECO:0000269|PubMed:28254838, ECO:0000269|PubMed:32017898}. |
Q56NI9 | ESCO2 | T62 | ochoa | N-acetyltransferase ESCO2 (EC 2.3.1.-) (Establishment factor-like protein 2) (EFO2) (EFO2p) (hEFO2) (Establishment of cohesion 1 homolog 2) (ECO1 homolog 2) | Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:15821733, PubMed:15958495). Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3 (PubMed:21111234). {ECO:0000269|PubMed:15821733, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234}. |
Q5S007 | LRRK2 | T1491 | psp | Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (EC 3.6.5.-) (Dardarin) | Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:17114044, PubMed:20949042, PubMed:21850687, PubMed:22012985, PubMed:23395371, PubMed:24687852, PubMed:25201882, PubMed:26014385, PubMed:26824392, PubMed:27830463, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43 (PubMed:23395371, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421, PubMed:38127736). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29212815). Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins (PubMed:30209220, PubMed:38227290). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421, ECO:0000269|PubMed:38127736, ECO:0000269|PubMed:38227290}. |
Q5T011 | SZT2 | T1196 | ochoa | KICSTOR complex protein SZT2 (Seizure threshold 2 protein homolog) | As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose (PubMed:28199306, PubMed:28199315). May play a role in the cellular response to oxidative stress (By similarity). {ECO:0000250|UniProtKB:A2A9C3, ECO:0000269|PubMed:28199306, ECO:0000269|PubMed:28199315}. |
Q5T200 | ZC3H13 | T985 | ochoa | Zinc finger CCCH domain-containing protein 13 | Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity). {ECO:0000250|UniProtKB:E9Q784}. |
Q5T3I0 | GPATCH4 | T271 | ochoa | G patch domain-containing protein 4 | None |
Q5T7W0 | ZNF618 | T175 | ochoa | Zinc finger protein 618 | Regulates UHRF2 function as a specific 5-hydroxymethylcytosine (5hmC) reader by regulating its chromatin localization. {ECO:0000269|PubMed:27129234}. |
Q5VTE0 | EEF1A1P5 | T23 | ochoa | Putative elongation factor 1-alpha-like 3 (EF-1-alpha-like 3) (Eukaryotic elongation factor 1 A-like 3) (eEF1A-like 3) (Eukaryotic translation elongation factor 1 alpha-1 pseudogene 5) | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000250}. |
Q5VUJ6 | LRCH2 | T361 | ochoa | Leucine-rich repeat and calponin homology domain-containing protein 2 | May play a role in the organization of the cytoskeleton. {ECO:0000250|UniProtKB:Q960C5, ECO:0000250|UniProtKB:Q96II8}. |
Q5VWN6 | TASOR2 | T612 | ochoa | Protein TASOR 2 | None |
Q69YH5 | CDCA2 | T673 | ochoa | Cell division cycle-associated protein 2 (Recruits PP1 onto mitotic chromatin at anaphase protein) (Repo-Man) | Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates. {ECO:0000269|PubMed:16492807, ECO:0000269|PubMed:16998479}. |
Q6NUK4 | REEP3 | T157 | ochoa | Receptor expression-enhancing protein 3 | Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes. {ECO:0000269|PubMed:23911198}. |
Q6P4R8 | NFRKB | T340 | ochoa | Nuclear factor related to kappa-B-binding protein (DNA-binding protein R kappa-B) (INO80 complex subunit G) | Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. {ECO:0000269|PubMed:18922472}.; FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Modulates the deubiquitinase activity of UCHL5 in the INO80 complex. {ECO:0000269|PubMed:18922472}. |
Q6SJ93 | FAM111B | T290 | ochoa | Serine protease FAM111B (EC 3.4.21.-) (Cancer-associated nucleoprotein) | Serine protease. {ECO:0000250|UniProtKB:Q96PZ2}. |
Q6UB98 | ANKRD12 | T565 | ochoa | Ankyrin repeat domain-containing protein 12 (Ankyrin repeat-containing cofactor 2) (GAC-1 protein) | May recruit HDACs to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation. |
Q6WKZ4 | RAB11FIP1 | T154 | ochoa | Rab11 family-interacting protein 1 (Rab11-FIP1) (Rab-coupling protein) | A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Interaction with RAB14 may function in the process of neurite formation (PubMed:26032412). {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206, ECO:0000269|PubMed:26032412}. |
Q6WKZ4 | RAB11FIP1 | T196 | ochoa | Rab11 family-interacting protein 1 (Rab11-FIP1) (Rab-coupling protein) | A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Interaction with RAB14 may function in the process of neurite formation (PubMed:26032412). {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206, ECO:0000269|PubMed:26032412}. |
Q6WKZ4 | RAB11FIP1 | T229 | ochoa | Rab11 family-interacting protein 1 (Rab11-FIP1) (Rab-coupling protein) | A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Interaction with RAB14 may function in the process of neurite formation (PubMed:26032412). {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206, ECO:0000269|PubMed:26032412}. |
Q6ZNB7 | AGMO | T22 | ochoa | Alkylglycerol monooxygenase (EC 1.14.16.5) (Transmembrane protein 195) | Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes. {ECO:0000269|PubMed:20643956}. |
Q6ZRI8 | ARHGAP36 | T478 | ochoa | Rho GTPase-activating protein 36 | GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}. |
Q70CQ2 | USP34 | T3364 | ochoa | Ubiquitin carboxyl-terminal hydrolase 34 (EC 3.4.19.12) (Deubiquitinating enzyme 34) (Ubiquitin thioesterase 34) (Ubiquitin-specific-processing protease 34) | Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000269|PubMed:21383061}. |
Q71F23 | CENPU | T231 | ochoa | Centromere protein U (CENP-U) (Centromere protein of 50 kDa) (CENP-50) (Interphase centromere complex protein 24) (KSHV latent nuclear antigen-interacting protein 1) (MLF1-interacting protein) (Polo-box-interacting protein 1) | Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:17081991}. |
Q71U36 | TUBA1A | T381 | ochoa | Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
Q7L804 | RAB11FIP2 | T148 | ochoa | Rab11 family-interacting protein 2 (Rab11-FIP2) (NRip11) | A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. Plays an essential role in phagocytosis through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for controlling actin-dynamics. {ECO:0000269|PubMed:12364336, ECO:0000269|PubMed:15304524, ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:19542231, ECO:0000269|PubMed:30883606}. |
Q7Z2Z1 | TICRR | T1877 | ochoa | Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein) | Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation. {ECO:0000269|PubMed:20116089}. |
Q7Z3J3 | RGPD4 | T1030 | ochoa | RanBP2-like and GRIP domain-containing protein 4 | None |
Q86U86 | PBRM1 | T174 | 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}. |
Q86V48 | LUZP1 | T676 | ochoa | Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin) | F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250|UniProtKB:Q8R4U7, ECO:0000269|PubMed:30990684, ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:38009294, ECO:0000269|PubMed:38832964}. |
Q8IVL0 | NAV3 | T355 | ochoa | Neuron navigator 3 (Pore membrane and/or filament-interacting-like protein 1) (Steerin-3) (Unc-53 homolog 3) (unc53H3) | Plays a role in cell migration (PubMed:21471154). May be involved in neuron regeneration. May regulate IL2 production by T-cells. {ECO:0000269|PubMed:16166283, ECO:0000269|PubMed:21471154}. |
Q8IX01 | SUGP2 | T284 | ochoa | SURP and G-patch domain-containing protein 2 (Arginine/serine-rich-splicing factor 14) (Splicing factor, arginine/serine-rich 14) | May play a role in mRNA splicing. {ECO:0000305}. |
Q8IXS8 | HYCC2 | T319 | ochoa | Hyccin 2 | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. {ECO:0000305|PubMed:26571211}. |
Q8N302 | AGGF1 | T337 | ochoa | Angiogenic factor with G patch and FHA domains 1 (Angiogenic factor VG5Q) (hVG5Q) (G patch domain-containing protein 7) (Vasculogenesis gene on 5q protein) | Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. {ECO:0000269|PubMed:14961121}. |
Q8N302 | AGGF1 | T341 | ochoa | Angiogenic factor with G patch and FHA domains 1 (Angiogenic factor VG5Q) (hVG5Q) (G patch domain-containing protein 7) (Vasculogenesis gene on 5q protein) | Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion. {ECO:0000269|PubMed:14961121}. |
Q8N4C9 | C17orf78 | T148 | ochoa | Uncharacterized protein C17orf78 | None |
Q8N4S9 | MARVELD2 | T168 | ochoa | MARVEL domain-containing protein 2 (Tricellulin) | Plays a role in the formation of tricellular tight junctions and of epithelial barriers (By similarity). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti (PubMed:17186462). {ECO:0000250|UniProtKB:Q3UZP0, ECO:0000269|PubMed:17186462}. |
Q8N8Z6 | DCBLD1 | T517 | psp | Discoidin, CUB and LCCL domain-containing protein 1 | None |
Q8NCN4 | RNF169 | T643 | ochoa | E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169) | Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}. |
Q8TAF3 | WDR48 | T343 | ochoa | WD repeat-containing protein 48 (USP1-associated factor 1) (WD repeat endosomal protein) (p80) | Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46 (PubMed:18082604, PubMed:19075014, PubMed:26388029, PubMed:31253762). Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself (PubMed:18082604, PubMed:31253762). Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (PubMed:19075014, PubMed:27373336). Also activates deubiquitinating activity of complexes containing USP12 (PubMed:19075014, PubMed:27373336, PubMed:27650958). In complex with USP12, acts as a potential tumor suppressor by positively regulating PHLPP1 stability (PubMed:24145035). Docks at the distal end of the USP12 fingers domain and induces a cascade of structural changes leading to the activation of the enzyme (PubMed:27373336, PubMed:27650958). Together with RAD51AP1, promotes DNA repair by stimulating RAD51-mediated homologous recombination (PubMed:27239033, PubMed:27463890, PubMed:32350107). Binds single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) (PubMed:27239033, PubMed:31253762, PubMed:32350107). DNA-binding is required both for USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during these processes (PubMed:31253762, PubMed:32350107). Together with ATAD5 and by regulating USP1 activity, has a role in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA (PubMed:20147293). Together with ATAD5, has a role in recruiting RAD51 to stalled forks during replication stress (PubMed:31844045). {ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:27239033, ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27463890, ECO:0000269|PubMed:27650958, ECO:0000269|PubMed:31253762, ECO:0000269|PubMed:31844045, ECO:0000269|PubMed:32350107}.; FUNCTION: (Microbial infection) In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP (PubMed:12196293). In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1 (PubMed:18032488). {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488}. |
Q8TB72 | PUM2 | T175 | ochoa | Pumilio homolog 2 (Pumilio-2) | Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26724866, ECO:0000269|PubMed:28431233}. |
Q8WWQ0 | PHIP | T1570 | ochoa | PH-interacting protein (PHIP) (DDB1- and CUL4-associated factor 14) (IRS-1 PH domain-binding protein) (WD repeat-containing protein 11) | Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:12242307, ECO:0000269|PubMed:21834987}. |
Q8WYL5 | SSH1 | T590 | 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}. |
Q92823 | NRCAM | T1221 | ochoa | Neuronal cell adhesion molecule (Nr-CAM) (Neuronal surface protein Bravo) (hBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related) | Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. Plays a role in mediating cell-cell contacts between Schwann cells and axons. Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier. {ECO:0000250|UniProtKB:Q810U4}. |
Q92945 | KHSRP | T277 | ochoa | Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (p75) | Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs. {ECO:0000250, ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:8940189, ECO:0000269|PubMed:9136930}. |
Q969S3 | ZNF622 | T318 | psp | Cytoplasmic 60S subunit biogenesis factor ZNF622 (Zinc finger protein 622) (Zinc finger-like protein 9) | Pre-60S-associated cytoplasmic factor involved in the cytoplasmic maturation of the 60S subunit. {ECO:0000269|PubMed:33711283}. |
Q96A65 | EXOC4 | T233 | ochoa | Exocyst complex component 4 (Exocyst complex component Sec8) | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250|UniProtKB:Q62824}. |
Q96AE4 | FUBP1 | T229 | ochoa | Far upstream element-binding protein 1 (FBP) (FUSE-binding protein 1) (DNA helicase V) (hDH V) | Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. {ECO:0000269|PubMed:8125259}. |
Q96B01 | RAD51AP1 | T29 | ochoa | RAD51-associated protein 1 (HsRAD51AP1) (RAD51-interacting protein) | Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination (PubMed:17996710, PubMed:17996711, PubMed:20871616, PubMed:25288561, PubMed:26323318). Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51 (PubMed:17996710, PubMed:17996711). Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation (PubMed:17996710, PubMed:17996711, PubMed:22375013, PubMed:9396801). Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair (PubMed:27239033, PubMed:27463890, PubMed:32350107). WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2 (PubMed:31253762). Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination (PubMed:21307306). Key mediator of alternative lengthening of telomeres (ALT) pathway, a homology-directed repair mechanism of telomere elongation that controls proliferation in aggressive cancers, by stimulating homologous recombination (PubMed:31400850). May also bind RNA; additional evidences are however required to confirm RNA-binding in vivo (PubMed:9396801). {ECO:0000269|PubMed:17996710, ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:22375013, ECO:0000269|PubMed:25288561, ECO:0000269|PubMed:26323318, ECO:0000269|PubMed:27239033, ECO:0000269|PubMed:27463890, ECO:0000269|PubMed:31253762, ECO:0000269|PubMed:31400850, ECO:0000269|PubMed:32350107, ECO:0000269|PubMed:9396801}. |
Q96GN5 | CDCA7L | T196 | ochoa | Cell division cycle-associated 7-like protein (Protein JPO2) (Transcription factor RAM2) | Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1. {ECO:0000269|PubMed:15654081, ECO:0000269|PubMed:15994933, ECO:0000269|PubMed:16829576}. |
Q96J84 | KIRREL1 | T549 | ochoa | Kin of IRRE-like protein 1 (Kin of irregular chiasm-like protein 1) (Nephrin-like protein 1) | Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (PubMed:31472902). It is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:31472902}. |
Q96K21 | ZFYVE19 | T291 | ochoa | Abscission/NoCut checkpoint regulator (ANCHR) (MLL partner containing FYVE domain) (Zinc finger FYVE domain-containing protein 19) | Key regulator of abscission step in cytokinesis: part of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Together with CHMP4C, required to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ZFYVE19/ANCHR and VPS4 and subsequent abscission. {ECO:0000269|PubMed:24814515}. |
Q96M96 | FGD4 | T60 | ochoa | FYVE, RhoGEF and PH domain-containing protein 4 (Actin filament-binding protein frabin) (FGD1-related F-actin-binding protein) (Zinc finger FYVE domain-containing protein 6) | Activates 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. Activates MAPK8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:15133042}. |
Q96RS0 | TGS1 | T309 | ochoa | Trimethylguanosine synthase (EC 2.1.1.-) (CLL-associated antigen KW-2) (Cap-specific guanine-N(2) methyltransferase) (Hepatocellular carcinoma-associated antigen 137) (Nuclear receptor coactivator 6-interacting protein) (PRIP-interacting protein with methyltransferase motif) (PIMT) (PIPMT) | Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation. {ECO:0000269|PubMed:11517327, ECO:0000269|PubMed:11912212, ECO:0000269|PubMed:16687569, ECO:0000269|PubMed:18775984}. |
Q96S66 | CLCC1 | T434 | ochoa | Chloride channel CLIC-like protein 1 (ER anion channel 1) (ERAC1) (Mid-1-related chloride channel protein) | Anion-selective channel with Ca(2+)-dependent and voltage-independent gating. Permeable to small monovalent anions with selectivity for bromide > chloride > nitrate > fluoride (By similarity). Operates in the endoplasmic reticulum (ER) membrane where it mediates chloride efflux to compensate for the loss of positive charges from the ER lumen upon Ca(2+) release. Contributes to the maintenance of ER Ca(2+) pools and activation of unfolded protein response to prevent accumulation of misfolded proteins in the ER lumen. Particularly involved in ER homeostasis mechanisms underlying motor neurons and retinal photoreceptors survival (By similarity) (PubMed:25698737, PubMed:30157172, PubMed:37142673). {ECO:0000250|UniProtKB:Q99LI2, ECO:0000269|PubMed:25698737, ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:37142673}. |
Q99442 | SEC62 | T332 | ochoa | Translocation protein SEC62 (Translocation protein 1) (TP-1) (hTP-1) | Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. {ECO:0000269|PubMed:22375059, ECO:0000269|PubMed:29719251}. |
Q99549 | MPHOSPH8 | T502 | ochoa | M-phase phosphoprotein 8 (Two hybrid-associated protein 3 with RanBPM) (Twa3) | Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:20871592, PubMed:26022416). Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene (PubMed:20871592). Mediates down-regulation of CDH1 expression (PubMed:20871592). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). {ECO:0000269|PubMed:20871592, ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:29211708, ECO:0000269|PubMed:30487602}. |
Q99567 | NUP88 | T443 | ochoa | Nuclear pore complex protein Nup88 (88 kDa nucleoporin) (Nucleoporin Nup88) | Component of nuclear pore complex. {ECO:0000269|PubMed:30543681}. |
Q99666 | RGPD5 | T1029 | ochoa | RANBP2-like and GRIP domain-containing protein 5/6 (Ran-binding protein 2-like 1/2) (RanBP2-like 1/2) (RanBP2L1) (RanBP2L2) (Sperm membrane protein BS-63) | None |
Q9BQG0 | MYBBP1A | T1190 | ochoa | Myb-binding protein 1A | May activate or repress transcription via interactions with sequence specific DNA-binding proteins (By similarity). Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) (By similarity). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2 (By similarity). Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter (By similarity). Has a role in rRNA biogenesis together with PWP1 (PubMed:29065309). {ECO:0000250|UniProtKB:Q7TPV4, ECO:0000269|PubMed:29065309}. |
Q9BRP8 | PYM1 | T112 | ochoa | Partner of Y14 and mago (PYM homolog 1 exon junction complex-associated factor) (Protein wibg homolog) | Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC. {ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19410547}. |
Q9BV36 | MLPH | T205 | ochoa | Melanophilin (Exophilin-3) (Slp homolog lacking C2 domains a) (SlaC2-a) (Synaptotagmin-like protein 2a) | Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. {ECO:0000269|PubMed:12062444}. |
Q9BW27 | NUP85 | T90 | 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}. |
Q9BY89 | KIAA1671 | T1106 | ochoa | Uncharacterized protein KIAA1671 | None |
Q9BZ95 | NSD3 | T547 | ochoa | Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.370) (EC 2.1.1.371) (Nuclear SET domain-containing protein 3) (Protein whistle) (WHSC1-like 1 isoform 9 with methyltransferase activity to lysine) (Wolf-Hirschhorn syndrome candidate 1-like protein 1) (WHSC1-like protein 1) | Histone methyltransferase. Preferentially dimethylates 'Lys-4' and 'Lys-27' of histone H3 forming H3K4me2 and H3K27me2. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression. {ECO:0000269|PubMed:16682010}. |
Q9C0C9 | UBE2O | T404 | ochoa | (E3-independent) E2 ubiquitin-conjugating enzyme (EC 2.3.2.24) (E2/E3 hybrid ubiquitin-protein ligase UBE2O) (Ubiquitin carrier protein O) (Ubiquitin-conjugating enzyme E2 O) (Ubiquitin-conjugating enzyme E2 of 230 kDa) (Ubiquitin-conjugating enzyme E2-230K) (Ubiquitin-protein ligase O) | E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853). {ECO:0000269|PubMed:23381138, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950}. |
Q9C0D5 | TANC1 | T1713 | ochoa | Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1) | May be a scaffold component in the postsynaptic density. {ECO:0000250}. |
Q9H2K8 | TAOK3 | T573 | ochoa | Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Cutaneous T-cell lymphoma-associated antigen HD-CL-09) (CTCL-associated antigen HD-CL-09) (Dendritic cell-derived protein kinase) (JNK/SAPK-inhibitory kinase) (Jun kinase-inhibitory kinase) (Kinase from chicken homolog A) (hKFC-A) (Thousand and one amino acid protein 3) | Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. 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. Inhibits basal activity of the MAPK8/JNK cascade and diminishes its activation in response to epidermal growth factor (EGF). Positively regulates canonical T cell receptor (TCR) signaling by preventing early PTPN6/SHP1-mediated inactivation of LCK, ensuring sustained TCR signaling that is required for optimal activation and differentiation of T cells (PubMed:30373850). Phosphorylates PTPN6/SHP1 on 'Thr-394', leading to its polyubiquitination and subsequent proteasomal degradation (PubMed:38166031). Required for cell surface expression of metalloprotease ADAM10 on type 1 transitional B cells which is necessary for their NOTCH-mediated development into marginal zone B cells (By similarity). Also required for the NOTCH-mediated terminal differentiation of splenic conventional type 2 dendritic cells (By similarity). Positively regulates osteoblast differentiation by acting as an upstream activator of the JNK pathway (PubMed:32807497). Promotes JNK signaling in hepatocytes and positively regulates hepatocyte lipid storage by inhibiting beta-oxidation and triacylglycerol secretion while enhancing lipid synthesis (PubMed:34634521). Restricts age-associated inflammation by negatively regulating differentiation of macrophages and their production of pro-inflammatory cytokines (By similarity). Plays a role in negatively regulating the abundance of regulatory T cells in white adipose tissue (By similarity). {ECO:0000250|UniProtKB:Q8BYC6, ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:10924369, ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:30373850, ECO:0000269|PubMed:32807497, ECO:0000269|PubMed:34634521, ECO:0000269|PubMed:38166031}. |
Q9H2M9 | RAB3GAP2 | T566 | ochoa | Rab3 GTPase-activating protein non-catalytic subunit (RGAP-iso) (Rab3 GTPase-activating protein 150 kDa subunit) (Rab3-GAP p150) (Rab3-GAP150) (Rab3-GAP regulatory subunit) | Regulatory subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18 (PubMed:24891604, PubMed:9733780). As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (By similarity). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (By similarity). The Rab3GAP complex acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604). Recruits and stabilizes RAB18 at the cis-Golgi membrane in human fibroblasts where RAB18 is most likely activated (PubMed:26063829). Also involved in RAB18 recruitment at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604). Required for normal eye and brain development (By similarity). May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity). {ECO:0000250|UniProtKB:Q15042, ECO:0000269|PubMed:24891604, ECO:0000269|PubMed:26063829, ECO:0000269|PubMed:9733780}. |
Q9H2Y7 | ZNF106 | T397 | ochoa | Zinc finger protein 106 (Zfp-106) (Zinc finger protein 474) | RNA-binding protein. Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA. Essential for maintenance of peripheral motor neuron and skeletal muscle function. Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism. {ECO:0000250|UniProtKB:O88466}. |
Q9H2Y7 | ZNF106 | T1245 | ochoa | Zinc finger protein 106 (Zfp-106) (Zinc finger protein 474) | RNA-binding protein. Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA. Essential for maintenance of peripheral motor neuron and skeletal muscle function. Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism. {ECO:0000250|UniProtKB:O88466}. |
Q9H4A3 | WNK1 | T601 | 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}. |
Q9H7P6 | MVB12B | T122 | ochoa|psp | Multivesicular body subunit 12B (ESCRT-I complex subunit MVB12B) (Protein FAM125B) | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. |
Q9HAW4 | CLSPN | T1161 | ochoa | Claspin (hClaspin) | Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation (PubMed:12766152, PubMed:15190204, PubMed:15707391, PubMed:16123041). Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins (PubMed:12766152, PubMed:15096610, PubMed:15707391, PubMed:16123041). Also required to maintain normal rates of replication fork progression during unperturbed DNA replication. Binds directly to DNA, with particular affinity for branched or forked molecules and interacts with multiple protein components of the replisome such as the MCM2-7 complex and TIMELESS (PubMed:15226314, PubMed:34694004, PubMed:35585232). Important for initiation of DNA replication, recruits kinase CDC7 to phosphorylate MCM2-7 components (PubMed:27401717). {ECO:0000269|PubMed:12766152, ECO:0000269|PubMed:15096610, ECO:0000269|PubMed:15190204, ECO:0000269|PubMed:15226314, ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:16123041, ECO:0000269|PubMed:27401717, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:35585232}. |
Q9HC62 | SENP2 | T369 | psp | Sentrin-specific protease 2 (EC 3.4.22.-) (Axam2) (SMT3-specific isopeptidase 2) (Smt3ip2) (Sentrin/SUMO-specific protease SENP2) | Protease that catalyzes two essential functions in the SUMO pathway (PubMed:11896061, PubMed:12192048, PubMed:15296745, PubMed:20194620, PubMed:21965678). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed:15296745). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:15296745, PubMed:20194620, PubMed:21965678). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000269|PubMed:11896061, ECO:0000269|PubMed:12192048, ECO:0000269|PubMed:15296745, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:21965678}. |
Q9HCK8 | CHD8 | T548 | ochoa | Chromodomain-helicase-DNA-binding protein 8 (CHD-8) (EC 3.6.4.-) (ATP-dependent helicase CHD8) (Helicase with SNF2 domain 1) | ATP-dependent chromatin-remodeling factor, it slides nucleosomes along DNA; nucleosome sliding requires ATP (PubMed:28533432). Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. Regulates alternative splicing of a core group of genes involved in neuronal differentiation, cell cycle and DNA repair. Enables H3K36me3-coupled transcription elongation and co-transcriptional RNA processing likely via interaction with HNRNPL. {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:28533432, ECO:0000269|PubMed:36537238}. |
Q9NP74 | PALMD | T527 | ochoa | Palmdelphin (Paralemmin-like protein) | None |
Q9NQV6 | PRDM10 | T826 | ochoa | PR domain zinc finger protein 10 (PR domain-containing protein 10) (Tristanin) | Transcriptional activator, essential for early embryonic development and survival of embryonic stem cells (ESCs) (By similarity). Supports cell growth and survival during early development by transcriptionally activating the expression of the translation initiation factor EIF3B, to sustain global translation (By similarity). Activates the transcription of FLNC (PubMed:36440963). {ECO:0000250|UniProtKB:Q3UTQ7, ECO:0000269|PubMed:36440963}. |
Q9NQZ2 | UTP3 | T362 | ochoa | Something about silencing protein 10 (Charged amino acid-rich leucine zipper 1) (CRL1) (Disrupter of silencing SAS10) (UTP3 homolog) | Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250|UniProtKB:Q12136, ECO:0000250|UniProtKB:Q9JI13, ECO:0000269|PubMed:34516797}. |
Q9NQZ2 | UTP3 | T397 | ochoa | Something about silencing protein 10 (Charged amino acid-rich leucine zipper 1) (CRL1) (Disrupter of silencing SAS10) (UTP3 homolog) | Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250|UniProtKB:Q12136, ECO:0000250|UniProtKB:Q9JI13, ECO:0000269|PubMed:34516797}. |
Q9NY65 | TUBA8 | T381 | ochoa | Tubulin alpha-8 chain (EC 3.6.5.-) (Alpha-tubulin 8) (Tubulin alpha chain-like 2) [Cleaved into: Dephenylalaninated tubulin alpha-8 chain] | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
Q9NYF8 | BCLAF1 | T355 | ochoa | Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1) | Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:18794151}. |
Q9P0M6 | MACROH2A2 | T170 | ochoa | Core histone macro-H2A.2 (Histone macroH2A2) (mH2A2) | Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in stable X chromosome inactivation. {ECO:0000269|PubMed:15621527}. |
Q9P266 | JCAD | T691 | ochoa | Junctional cadherin 5-associated protein (Junctional protein associated with coronary artery disease) (JCAD) | None |
Q9P2G1 | ANKIB1 | T440 | ochoa | Ankyrin repeat and IBR domain-containing protein 1 (EC 2.3.2.31) | Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. {ECO:0000250}. |
Q9UIF8 | BAZ2B | T2011 | ochoa | Bromodomain adjacent to zinc finger domain protein 2B (hWALp4) | Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535). Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By similarity) (PubMed:10662543). Involved in positively modulating the rate of age-related behavioral deterioration (By similarity). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with histone methyltransferase EHMT1 (By similarity). {ECO:0000250|UniProtKB:A2AUY4, ECO:0000269|PubMed:28801535, ECO:0000303|PubMed:10662543}. |
Q9UIF9 | BAZ2A | T688 | ochoa | Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5) (hWALp3) | Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (By similarity). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By similarity). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity). {ECO:0000250|UniProtKB:Q91YE5, ECO:0000269|PubMed:28801535}. |
Q9UJX2 | CDC23 | T542 | ochoa | Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Cyclosome subunit 8) | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132). {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:29033132}. |
Q9UKJ3 | GPATCH8 | T327 | ochoa | G patch domain-containing protein 8 | None |
Q9UKL3 | CASP8AP2 | T1828 | ochoa | CASP8-associated protein 2 (FLICE-associated huge protein) | Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase. {ECO:0000269|PubMed:12477726, ECO:0000269|PubMed:15698540, ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17245429}. |
Q9UKN8 | GTF3C4 | T649 | ochoa | General transcription factor 3C polypeptide 4 (EC 2.3.1.48) (TF3C-delta) (Transcription factor IIIC 90 kDa subunit) (TFIIIC 90 kDa subunit) (TFIIIC90) (Transcription factor IIIC subunit delta) | Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin (PubMed:10523658). Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3 (PubMed:10523658). May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F (PubMed:10523658). May be localized close to the A box (PubMed:10523658). {ECO:0000269|PubMed:10523658}. |
Q9UKT9 | IKZF3 | T389 | ochoa | Zinc finger protein Aiolos (Ikaros family zinc finger protein 3) | Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner. {ECO:0000269|PubMed:10369681, ECO:0000269|PubMed:34155405}. |
Q9UKX2 | MYH2 | T64 | ochoa | Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) | Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. {ECO:0000250|UniProtKB:P12883}. |
Q9ULF5 | SLC39A10 | T553 | ochoa | Zinc transporter ZIP10 (Solute carrier family 39 member 10) (Zrt- and Irt-like protein 10) (ZIP-10) | Zinc-influx transporter (PubMed:17359283, PubMed:27274087, PubMed:30520657). When associated with SLC39A6, the heterodimer formed by SLC39A10 and SLC39A6 mediates cellular zinc uptake to trigger cells to undergo epithelial-to-mesenchymal transition (EMT) (PubMed:23186163). SLC39A10-SLC39A6 heterodimers play also an essentiel role in initiating mitosis by importing zinc into cells to initiate a pathway resulting in the onset of mitosis (PubMed:32797246). Plays an important for both mature B-cell maintenance and humoral immune responses (By similarity). When associated with SLC39A10, the heterodimer controls NCAM1 phosphorylation and integration into focal adhesion complexes during EMT (By similarity). {ECO:0000250|UniProtKB:Q6P5F6, ECO:0000269|PubMed:17359283, ECO:0000269|PubMed:23186163, ECO:0000269|PubMed:27274087, ECO:0000269|PubMed:30520657, ECO:0000269|PubMed:32797246}. |
Q9ULH0 | KIDINS220 | T1528 | ochoa | Kinase D-interacting substrate of 220 kDa (Ankyrin repeat-rich membrane-spanning protein) | Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269|PubMed:18089783}. |
Q9UQ13 | SHOC2 | T71 | ochoa|psp | Leucine-rich repeat protein SHOC-2 (Protein soc-2 homolog) (Protein sur-8 homolog) | Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates activation of the MAPK pathway (PubMed:10783161, PubMed:16630891, PubMed:25137548, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). Acts as a scaffolding protein in the SMP complex (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:10783161, PubMed:16630891, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670). {ECO:0000269|PubMed:10783161, ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:25137548, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35830882, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670}. |
Q9UQL6 | HDAC5 | T292 | psp | Histone deacetylase 5 (HD5) (EC 3.5.1.98) (Antigen NY-CO-9) | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Serves as a corepressor of RARA and causes its deacetylation (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). {ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:28167758}. |
Q9UQM7 | CAMK2A | T337 | ochoa | Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17) | Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (PubMed:14722083). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (By similarity). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (PubMed:11972023). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (PubMed:35568036). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (By similarity). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:P11798, ECO:0000269|PubMed:11972023, ECO:0000269|PubMed:23805378, ECO:0000269|PubMed:28130356, ECO:0000269|PubMed:29100089}. |
Q9Y2X7 | GIT1 | T537 | ochoa|psp | ARF GTPase-activating protein GIT1 (ARF GAP GIT1) (Cool-associated and tyrosine-phosphorylated protein 1) (CAT-1) (CAT1) (G protein-coupled receptor kinase-interactor 1) (GRK-interacting protein 1) (p95-APP1) | GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase (PubMed:27012601). Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (PubMed:23108400). May promote cell motility both by regulating focal complex dynamics and by local activation of RAC1 (PubMed:10938112, PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (PubMed:15923189). Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (PubMed:25284783). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity). Required for successful bone regeneration during fracture healing (By similarity). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity). May play a role in angiogenesis during fracture healing (By similarity). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (PubMed:31502302). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). {ECO:0000250|UniProtKB:Q68FF6, ECO:0000250|UniProtKB:Q9Z272, ECO:0000269|PubMed:10938112, ECO:0000269|PubMed:11896197, ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:15800193, ECO:0000269|PubMed:15923189, ECO:0000269|PubMed:19273721, ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:25284783, ECO:0000269|PubMed:27012601, ECO:0000269|PubMed:31502302}. |
Q9Y426 | C2CD2 | T521 | ochoa | C2 domain-containing protein 2 (Transmembrane protein 24-like) | None |
Q9Y450 | HBS1L | T151 | ochoa | HBS1-like protein (EC 3.6.5.-) (ERFS) | GTPase component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:21448132, PubMed:23667253, PubMed:27863242). The Pelota-HBS1L complex recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (PubMed:27863242). Following mRNA extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L complex promotes recruitment of ABCE1, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132, PubMed:32006463). {ECO:0000269|PubMed:21448132, ECO:0000269|PubMed:23667253, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:32006463}. |
Q9Y485 | DMXL1 | T468 | ochoa | DmX-like protein 1 (X-like 1 protein) | None |
Q9Y5B9 | SUPT16H | T903 | ochoa | FACT complex subunit SPT16 (Chromatin-specific transcription elongation factor 140 kDa subunit) (FACT 140 kDa subunit) (FACTp140) (Facilitates chromatin transcription complex subunit SPT16) (hSPT16) | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9836642}. |
P07237 | P4HB | T85 | Sugiyama | Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (p55) | This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:32149426}. |
P08195 | SLC3A2 | T275 | Sugiyama | Amino acid transporter heavy chain SLC3A2 (4F2 cell-surface antigen heavy chain) (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98) | Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:11557028, PubMed:30867591, PubMed:33298890, PubMed:33758168, PubMed:34880232, PubMed:9751058, PubMed:9829974, PubMed:9878049). Heterodimers function as amino acids exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids (PubMed:10903140, PubMed:9829974). Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:34880232). SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, thyroid hormones and L-DOPA (PubMed:10574970, PubMed:11389679, PubMed:11557028, PubMed:11564694, PubMed:11742812, PubMed:12117417, PubMed:12225859, PubMed:12716892, PubMed:15980244, PubMed:30867591, PubMed:33298890, PubMed:33758168). SLC3A2 is essential for plasma membrane localization, stability, and the transport activity of SLC7A5 and SLC7A8 (PubMed:10391915, PubMed:10574970, PubMed:11311135, PubMed:15769744, PubMed:33066406). When associated with LAPTM4B, the heterodimer SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression (PubMed:11121428, PubMed:15625115). {ECO:0000250|UniProtKB:P63115, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:15625115, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33066406, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:9751058, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.; FUNCTION: (Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis. {ECO:0000269|PubMed:30341327}.; FUNCTION: (Microbial infection) Acts as a receptor for malaria parasite Plasmodium vivax (Thai isolate) in immature red blood cells. {ECO:0000269|PubMed:34294905}. |
P30101 | PDIA3 | T485 | Sugiyama | Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) | Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323). {ECO:0000269|PubMed:11825568, ECO:0000269|PubMed:16193070, ECO:0000269|PubMed:27897272, ECO:0000269|PubMed:35948544, ECO:0000269|PubMed:36104323, ECO:0000269|PubMed:7487104}. |
P31948 | STIP1 | T243 | Sugiyama | Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop) (Renal carcinoma antigen NY-REN-11) (Transformation-sensitive protein IEF SSP 3521) | Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000303|PubMed:27353360}. |
P50914 | RPL14 | T43 | Sugiyama | Large ribosomal subunit protein eL14 (60S ribosomal protein L14) (CAG-ISL 7) | 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}. |
A0MZ66 | SHTN1 | T455 | Sugiyama | Shootin-1 (Shootin1) | Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons. {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}. |
P04040 | CAT | T43 | Sugiyama | Catalase (EC 1.11.1.6) | Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369). {ECO:0000269|PubMed:7882369}. |
P62899 | RPL31 | T26 | Sugiyama | Large ribosomal subunit protein eL31 (60S ribosomal protein L31) | 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}. |
Q92522 | H1-10 | T55 | Sugiyama | Histone H1.10 (Histone H1x) | Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. |
O94779 | CNTN5 | T494 | Sugiyama | Contactin-5 (Neural recognition molecule NB-2) (hNB-2) | Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons. Probably involved in neuronal activity in the auditory system (By similarity). {ECO:0000250}. |
Q15056 | EIF4H | T100 | Sugiyama | Eukaryotic translation initiation factor 4H (eIF-4H) (Williams-Beuren syndrome chromosomal region 1 protein) | Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}. |
Q15293 | RCN1 | T101 | Sugiyama | Reticulocalbin-1 | May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. |
P04406 | GAPDH | T104 | Sugiyama | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) | Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. |
P07900 | HSP90AA1 | T298 | Sugiyama | Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Heat shock protein family C member 1) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. {ECO:0000305|PubMed:22066472}. |
P08238 | HSP90AB1 | T290 | Sugiyama | Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84) (Heat shock protein family C member 3) | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269|PubMed:21949862, ECO:0000305|PubMed:22066472}. |
P63173 | RPL38 | T44 | Sugiyama | Large ribosomal subunit protein eL38 (60S ribosomal protein L38) | 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}. |
O43707 | ACTN4 | T612 | Sugiyama | Alpha-actinin-4 (Non-muscle alpha-actinin 4) | F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:22689882, ECO:0000305|PubMed:9508771}. |
P04075 | ALDOA | T119 | Sugiyama | 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}. |
P35080 | PFN2 | T85 | Sugiyama | Profilin-2 (Profilin II) | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. |
A6NDS4 | TBC1D3B | T152 | Sugiyama | TBC1 domain family member 3B | Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}. |
B9A6J9 | TBC1D3L | T152 | Sugiyama | TBC1 domain family member 3L | Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250|UniProtKB:Q8IZP1}. |
Q6DHY5 | TBC1D3G | T152 | Sugiyama | TBC1 domain family member 3G | Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}. |
Q6IPX1 | TBC1D3C | T152 | Sugiyama | TBC1 domain family member 3C | Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity). {ECO:0000250}. |
Q13442 | PDAP1 | T93 | Sugiyama | 28 kDa heat- and acid-stable phosphoprotein (PDGF-associated protein) (PAP) (PDGFA-associated protein 1) (PAP1) | Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. {ECO:0000250}. |
P19338 | NCL | T464 | Sugiyama | Nucleolin (Protein C23) | Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. {ECO:0000269|PubMed:10393184}. |
O60739 | EIF1B | T45 | Sugiyama | Eukaryotic translation initiation factor 1b (eIF1b) (Protein translation factor SUI1 homolog GC20) | Probably involved in translation. |
P41567 | EIF1 | T45 | Sugiyama | 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}. |
P46779 | RPL28 | T81 | Sugiyama | Large ribosomal subunit protein eL28 (60S ribosomal protein L28) | 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}. |
O94804 | STK10 | T544 | Sugiyama | Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase) | Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:11903060, ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:19255442}. |
P08708 | RPS17 | T30 | Sugiyama | Small ribosomal subunit protein eS17 (40S ribosomal protein S17) | 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}. |
P62847 | RPS24 | T69 | Sugiyama | Small ribosomal subunit protein eS24 (40S ribosomal protein S24) | Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Required for processing of pre-rRNA and maturation of 40S ribosomal subunits (PubMed:18230666). 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:18230666, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. |
P62249 | RPS16 | T118 | Sugiyama | 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}. |
P24666 | ACP1 | T85 | Sugiyama | Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Adipocyte acid phosphatase) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) (Red cell acid phosphatase 1) | Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates with differences in substrate specificity between isoform 1 and isoform 2. {ECO:0000269|PubMed:10336608, ECO:0000269|PubMed:9705307}.; FUNCTION: [Isoform 3]: Does not possess phosphatase activity. {ECO:0000269|PubMed:10336608}. |
P31327 | CPS1 | T771 | Sugiyama | Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) | Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. |
P27824 | CANX | T186 | Sugiyama | Calnexin (IP90) (Major histocompatibility complex class I antigen-binding protein p88) (p90) | Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse. |
P31948 | STIP1 | T257 | Sugiyama | Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop) (Renal carcinoma antigen NY-REN-11) (Transformation-sensitive protein IEF SSP 3521) | Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000303|PubMed:27353360}. |
Q12904 | AIMP1 | T287 | Sugiyama | Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (Multisynthase complex auxiliary component p43) [Cleaved into: Endothelial monocyte-activating polypeptide 2 (EMAP-2) (Endothelial monocyte-activating polypeptide II) (EMAP-II) (Small inducible cytokine subfamily E member 1)] | Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase (PubMed:10358004). Binds tRNA. Possesses inflammatory cytokine activity (PubMed:11306575). Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation (By similarity). Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels (By similarity). Promotes dermal fibroblast proliferation and wound repair (PubMed:16472771). Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum (By similarity). Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations (PubMed:12237313). Induces maturation of dendritic cells and monocyte cell adhesion (PubMed:11818442). Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (PubMed:19362550). {ECO:0000250|UniProtKB:P31230, ECO:0000269|PubMed:10358004, ECO:0000269|PubMed:11157763, ECO:0000269|PubMed:11306575, ECO:0000269|PubMed:11818442, ECO:0000269|PubMed:12237313, ECO:0000269|PubMed:19362550}. |
P16234 | PDGFRA | T740 | Sugiyama | Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a) | Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:10947961, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:17087943, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664, ECO:0000269|PubMed:8760137, ECO:0000269|PubMed:8943348}. |
Q8WUA2 | PPIL4 | T361 | Sugiyama | Peptidyl-prolyl cis-trans isomerase-like 4 (PPIase) (EC 5.2.1.8) (Cyclophilin-like protein PPIL4) (Rotamase PPIL4) | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. |
P14314 | PRKCSH | T103 | Sugiyama | Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH) | Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (By similarity). {ECO:0000250|UniProtKB:O08795, ECO:0000269|PubMed:10929008}. |
Q99714 | HSD17B10 | T73 | Sugiyama | 3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-estradiol 17-dehydrogenase) (EC 1.1.1.62) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))) (EC 1.1.1.239) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (3alpha(or 20beta)-hydroxysteroid dehydrogenase) (EC 1.1.1.53) (7-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.159) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH) | Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PubMed:10600649, PubMed:12917011, PubMed:18996107, PubMed:19706438, PubMed:20077426, PubMed:25925575, PubMed:26950678, PubMed:28888424, PubMed:9553139). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678, PubMed:9553139). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PubMed:18996107, PubMed:19706438, PubMed:20077426). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PubMed:10600649, PubMed:12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PubMed:19706438, PubMed:28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PubMed:26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426). {ECO:0000269|PubMed:10600649, ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18996107, ECO:0000269|PubMed:19706438, ECO:0000269|PubMed:20077426, ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26338420, ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:9553139}.; FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424). Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23042678, ECO:0000269|PubMed:24549042, ECO:0000269|PubMed:24703694, ECO:0000269|PubMed:25925575, ECO:0000269|PubMed:26950678, ECO:0000269|PubMed:28888424, ECO:0000269|PubMed:29040705}. |
Q05209 | PTPN12 | T81 | Sugiyama | Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (PTP-PEST) (Protein-tyrosine phosphatase G1) (PTPG1) | Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). {ECO:0000269|PubMed:17329398, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:27134172}. |
P36894 | BMPR1A | T391 | Sugiyama | Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292) | On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6. May promote the expression of HAMP, potentially via its interaction with BMP2 (By similarity). {ECO:0000250|UniProtKB:P36895}. |
P36896 | ACVR1B | T364 | Sugiyama | Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2) | Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:12639945, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:20226172, ECO:0000269|PubMed:8196624, ECO:0000269|PubMed:9032295, ECO:0000269|PubMed:9892009}. |
Q9UBU7 | DBF4 | T308 | Sugiyama | 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}. |
P51813 | BMX | T72 | Sugiyama | Cytoplasmic tyrosine-protein kinase BMX (EC 2.7.10.2) (Bone marrow tyrosine kinase gene in chromosome X protein) (Epithelial and endothelial tyrosine kinase) (ETK) (NTK38) | Non-receptor tyrosine kinase that plays central but diverse modulatory roles in various signaling processes involved in the regulation of actin reorganization, cell migration, cell proliferation and survival, cell adhesion, and apoptosis. Participates in signal transduction stimulated by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen receptors and integrins. Induces tyrosine phosphorylation of BCAR1 in response to integrin regulation. Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator of integrin signaling events leading to the regulation of actin cytoskeleton and cell motility. Plays a critical role in TNF-induced angiogenesis, and implicated in the signaling of TEK and FLT1 receptors, 2 important receptor families essential for angiogenesis. Required for the phosphorylation and activation of STAT3, a transcription factor involved in cell differentiation. Also involved in interleukin-6 (IL6) induced differentiation. Also plays a role in programming adaptive cytoprotection against extracellular stress in different cell systems, salivary epithelial cells, brain endothelial cells, and dermal fibroblasts. May be involved in regulation of endocytosis through its interaction with an endosomal protein RUFY1. May also play a role in the growth and differentiation of hematopoietic cells; as well as in signal transduction in endocardial and arterial endothelial cells. {ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:12370298, ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:15788485, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:9520419}. |
Q00839 | HNRNPU | T530 | Sugiyama | Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (GRIP120) (Nuclear p120 ribonucleoprotein) (Scaffold-attachment factor A) (SAF-A) (p120) (pp120) | DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression (PubMed:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991, PubMed:25986610, PubMed:28622508). Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability (PubMed:1324173, PubMed:28622508, PubMed:8174554). Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:10490622, PubMed:15711563, PubMed:19617346, PubMed:23811339, PubMed:8174554, PubMed:9353307). Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner (PubMed:10490622, PubMed:15711563). Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation (PubMed:10490622). Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus (PubMed:19617346). Negatively regulates glucocorticoid-mediated transcriptional activation (PubMed:9353307). Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (PubMed:23811339). Participates in the circadian regulation of the core clock component BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length (PubMed:18082603). Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a role in mRNA stability (PubMed:17174306, PubMed:17289661, PubMed:19029303). Component of the CRD-mediated complex that promotes MYC mRNA stabilization (PubMed:19029303). Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR) (PubMed:17174306). Plays a role in mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610). Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression (PubMed:21242313). Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis (PubMed:25986610). Also contributes to the targeting of AURKA to mitotic spindle MTs (PubMed:21242313). Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365). Binds to chromatin-associated RNAs (caRNAs) (PubMed:28622508). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:10671544, PubMed:11003645, PubMed:11909954, PubMed:1324173, PubMed:28622508, PubMed:7509195, PubMed:9204873, PubMed:9405365). Binds to the Xist RNA (PubMed:26244333). Binds the long non-coding H19 RNA (PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions (PubMed:22325991). Binds to small nuclear RNAs (snRNAs) (PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306). Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). Required for embryonic development (By similarity). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:10490622, ECO:0000269|PubMed:10671544, ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:11909954, ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:15711563, ECO:0000269|PubMed:1628625, ECO:0000269|PubMed:17174306, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:22325991, ECO:0000269|PubMed:23811339, ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:26244333, ECO:0000269|PubMed:28622508, ECO:0000269|PubMed:7509195, ECO:0000269|PubMed:8068679, ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9204873, ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.; FUNCTION: (Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm. {ECO:0000269|PubMed:16916646}. |
Q14697 | GANAB | T492 | Sugiyama | Neutral alpha-glucosidase AB (EC 3.2.1.207) (Alpha-glucosidase 2) (Glucosidase II subunit alpha) | Catalytic subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia (PubMed:27259053). {ECO:0000269|PubMed:10929008, ECO:0000269|PubMed:27259053}. |
Q9Y3F4 | STRAP | T165 | Sugiyama | Serine-threonine kinase receptor-associated protein (MAP activator with WD repeats) (UNR-interacting protein) (WD-40 repeat protein PT-WD) | The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. {ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}. |
P62280 | RPS11 | T127 | 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}. |
P10768 | ESD | T205 | Sugiyama | S-formylglutathione hydrolase (FGH) (EC 3.1.2.12) (Esterase D) (Methylumbelliferyl-acetate deacetylase) (EC 3.1.1.56) | Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}. |
P62258 | YWHAE | T114 | Sugiyama | 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}. |
Q13347 | EIF3I | T205 | Sugiyama | Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36) | 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_03008, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. |
P52272 | HNRNPM | T68 | Sugiyama | Heterogeneous nuclear ribonucleoprotein M (hnRNP M) | Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines. |
Q99615 | DNAJC7 | T280 | Sugiyama | DnaJ homolog subfamily C member 7 (Tetratricopeptide repeat protein 2) (TPR repeat protein 2) | Acts as a co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}. |
Q9H6T3 | RPAP3 | T157 | Sugiyama | RNA polymerase II-associated protein 3 | Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. {ECO:0000269|PubMed:17643375}. |
O15226 | NKRF | T623 | Sugiyama | NF-kappa-B-repressing factor (NFkB-repressing factor) (NRF) (Protein ITBA4) | Enhances the ATPase activity of DHX15 by acting like a brace that tethers mobile sections of DHX15 together, stabilizing a functional conformation with high RNA affinity of DHX15 (PubMed:12381793). Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity (PubMed:12381793). Also involved in the regulation of IL-8 transcription (PubMed:12381793). May also act as a DNA-binding transcription regulator: interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes (PubMed:10562553). {ECO:0000269|PubMed:10562553, ECO:0000269|PubMed:12381793}. |
O75534 | CSDE1 | T431 | Sugiyama | Cold shock domain-containing protein E1 (N-ras upstream gene protein) (Protein UNR) | RNA-binding protein involved in translationally coupled mRNA turnover (PubMed:11051545, PubMed:15314026). Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (PubMed:11051545, PubMed:15314026). Required for efficient formation of stress granules (PubMed:29395067). {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:29395067}.; FUNCTION: (Microbial infection) Required for internal initiation of translation of human rhinovirus RNA. {ECO:0000269|PubMed:10049359}. |
Q99615 | DNAJC7 | T52 | Sugiyama | DnaJ homolog subfamily C member 7 (Tetratricopeptide repeat protein 2) (TPR repeat protein 2) | Acts as a co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}. |
P31948 | STIP1 | T143 | Sugiyama | Stress-induced-phosphoprotein 1 (STI1) (Hsc70/Hsp90-organizing protein) (Hop) (Renal carcinoma antigen NY-REN-11) (Transformation-sensitive protein IEF SSP 3521) | Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000303|PubMed:27353360}. |
Q9H2G2 | SLK | T809 | Sugiyama | STE20-like serine/threonine-protein kinase (STE20-like kinase) (hSLK) (EC 2.7.11.1) (CTCL tumor antigen se20-9) (STE20-related serine/threonine-protein kinase) (STE20-related kinase) (Serine/threonine-protein kinase 2) | Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}. |
P49792 | RANBP2 | T2703 | Sugiyama | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270) | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}. |
Q15652 | JMJD1C | T516 | Sugiyama | Probable JmjC domain-containing histone demethylation protein 2C (EC 1.14.11.-) (Jumonji domain-containing protein 1C) (Thyroid receptor-interacting protein 8) (TR-interacting protein 8) (TRIP-8) | Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). {ECO:0000250}. |
P41223 | BUD31 | T111 | Sugiyama | Protein BUD31 homolog (Protein EDG-2) (Protein G10 homolog) | Involved in the pre-mRNA splicing process (PubMed:28076346, PubMed:28502770). May play a role as regulator of AR transcriptional activity; may increase AR transcriptional activity (PubMed:25091737). {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000305|PubMed:25091737}. |
Q99575 | POP1 | T103 | Sugiyama | Ribonucleases P/MRP protein subunit POP1 (hPOP1) | Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:8918471). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:8918471}. |
Download
reactome_id | name | p | -log10_p |
---|---|---|---|
R-HSA-2262752 | Cellular responses to stress | 8.910325e-10 | 9.050 |
R-HSA-8953897 | Cellular responses to stimuli | 2.014868e-09 | 8.696 |
R-HSA-156842 | Eukaryotic Translation Elongation | 1.879051e-08 | 7.726 |
R-HSA-168255 | Influenza Infection | 1.713509e-08 | 7.766 |
R-HSA-422475 | Axon guidance | 2.476952e-07 | 6.606 |
R-HSA-1640170 | Cell Cycle | 3.027882e-07 | 6.519 |
R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 5.655263e-07 | 6.248 |
R-HSA-9675108 | Nervous system development | 9.351656e-07 | 6.029 |
R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 1.919401e-06 | 5.717 |
R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 3.889390e-06 | 5.410 |
R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 5.168760e-06 | 5.287 |
R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 5.038783e-06 | 5.298 |
R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 2.966297e-06 | 5.528 |
R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 5.502575e-06 | 5.259 |
R-HSA-156902 | Peptide chain elongation | 3.889390e-06 | 5.410 |
R-HSA-9646399 | Aggrephagy | 4.659923e-06 | 5.332 |
R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 5.038783e-06 | 5.298 |
R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 3.732759e-06 | 5.428 |
R-HSA-190840 | Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane | 5.354045e-06 | 5.271 |
R-HSA-69278 | Cell Cycle, Mitotic | 4.572300e-06 | 5.340 |
R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 5.157514e-06 | 5.288 |
R-HSA-190872 | Transport of connexons to the plasma membrane | 6.879108e-06 | 5.162 |
R-HSA-9709603 | Impaired BRCA2 binding to PALB2 | 8.738842e-06 | 5.059 |
R-HSA-9701193 | Defective homologous recombination repair (HRR) due to PALB2 loss of function | 1.098626e-05 | 4.959 |
R-HSA-9704646 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.098626e-05 | 4.959 |
R-HSA-9704331 | Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of... | 1.098626e-05 | 4.959 |
R-HSA-9701192 | Defective homologous recombination repair (HRR) due to BRCA1 loss of function | 1.098626e-05 | 4.959 |
R-HSA-72689 | Formation of a pool of free 40S subunits | 8.866618e-06 | 5.052 |
R-HSA-389977 | Post-chaperonin tubulin folding pathway | 1.098626e-05 | 4.959 |
R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 8.543092e-06 | 5.068 |
R-HSA-72613 | Eukaryotic Translation Initiation | 1.111343e-05 | 4.954 |
R-HSA-72737 | Cap-dependent Translation Initiation | 1.111343e-05 | 4.954 |
R-HSA-8852276 | The role of GTSE1 in G2/M progression after G2 checkpoint | 1.112046e-05 | 4.954 |
R-HSA-72312 | rRNA processing | 1.083206e-05 | 4.965 |
R-HSA-69275 | G2/M Transition | 1.416421e-05 | 4.849 |
R-HSA-453274 | Mitotic G2-G2/M phases | 1.583439e-05 | 4.800 |
R-HSA-68877 | Mitotic Prometaphase | 2.079669e-05 | 4.682 |
R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 3.027527e-05 | 4.519 |
R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 3.350209e-05 | 4.475 |
R-HSA-5693554 | Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SD... | 3.627166e-05 | 4.440 |
R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 3.674626e-05 | 4.435 |
R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 3.674626e-05 | 4.435 |
R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 4.620074e-05 | 4.335 |
R-HSA-72764 | Eukaryotic Translation Termination | 4.995069e-05 | 4.301 |
R-HSA-9609736 | Assembly and cell surface presentation of NMDA receptors | 5.521007e-05 | 4.258 |
R-HSA-9948299 | Ribosome-associated quality control | 6.007899e-05 | 4.221 |
R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 6.017202e-05 | 4.221 |
R-HSA-2467813 | Separation of Sister Chromatids | 6.690267e-05 | 4.175 |
R-HSA-2408522 | Selenoamino acid metabolism | 6.690267e-05 | 4.175 |
R-HSA-2408557 | Selenocysteine synthesis | 7.835096e-05 | 4.106 |
R-HSA-190828 | Gap junction trafficking | 7.970118e-05 | 4.099 |
R-HSA-192823 | Viral mRNA Translation | 9.044422e-05 | 4.044 |
R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 9.525234e-05 | 4.021 |
R-HSA-9675135 | Diseases of DNA repair | 1.004779e-04 | 3.998 |
R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 9.706135e-05 | 4.013 |
R-HSA-8955332 | Carboxyterminal post-translational modifications of tubulin | 1.124066e-04 | 3.949 |
R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.100068e-04 | 3.959 |
R-HSA-437239 | Recycling pathway of L1 | 1.124066e-04 | 3.949 |
R-HSA-9824446 | Viral Infection Pathways | 1.089889e-04 | 3.963 |
R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 1.277880e-04 | 3.894 |
R-HSA-5685942 | HDR through Homologous Recombination (HRR) | 1.234541e-04 | 3.908 |
R-HSA-5693568 | Resolution of D-loop Structures through Holliday Junction Intermediates | 1.265204e-04 | 3.898 |
R-HSA-69620 | Cell Cycle Checkpoints | 1.240933e-04 | 3.906 |
R-HSA-438064 | Post NMDA receptor activation events | 1.238371e-04 | 3.907 |
R-HSA-9668328 | Sealing of the nuclear envelope (NE) by ESCRT-III | 1.265204e-04 | 3.898 |
R-HSA-376176 | Signaling by ROBO receptors | 1.298345e-04 | 3.887 |
R-HSA-9663891 | Selective autophagy | 1.337048e-04 | 3.874 |
R-HSA-157858 | Gap junction trafficking and regulation | 1.397207e-04 | 3.855 |
R-HSA-68886 | M Phase | 1.347310e-04 | 3.871 |
R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 1.412723e-04 | 3.850 |
R-HSA-5693537 | Resolution of D-Loop Structures | 1.449406e-04 | 3.839 |
R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 1.460011e-04 | 3.836 |
R-HSA-9701190 | Defective homologous recombination repair (HRR) due to BRCA2 loss of function | 1.654218e-04 | 3.781 |
R-HSA-9675136 | Diseases of DNA Double-Strand Break Repair | 1.654218e-04 | 3.781 |
R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 1.654218e-04 | 3.781 |
R-HSA-190861 | Gap junction assembly | 1.654218e-04 | 3.781 |
R-HSA-9612973 | Autophagy | 1.745562e-04 | 3.758 |
R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 2.013406e-04 | 3.696 |
R-HSA-72766 | Translation | 2.107533e-04 | 3.676 |
R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 2.264348e-04 | 3.645 |
R-HSA-72649 | Translation initiation complex formation | 2.320705e-04 | 3.634 |
R-HSA-68882 | Mitotic Anaphase | 2.409334e-04 | 3.618 |
R-HSA-2555396 | Mitotic Metaphase and Anaphase | 2.513216e-04 | 3.600 |
R-HSA-72702 | Ribosomal scanning and start codon recognition | 2.805741e-04 | 3.552 |
R-HSA-5693538 | Homology Directed Repair | 2.900466e-04 | 3.538 |
R-HSA-5693579 | Homologous DNA Pairing and Strand Exchange | 2.712853e-04 | 3.567 |
R-HSA-8953854 | Metabolism of RNA | 2.987058e-04 | 3.525 |
R-HSA-9833482 | PKR-mediated signaling | 3.582091e-04 | 3.446 |
R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 3.369089e-04 | 3.472 |
R-HSA-3371556 | Cellular response to heat stress | 3.454073e-04 | 3.462 |
R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 3.582091e-04 | 3.446 |
R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 3.454073e-04 | 3.462 |
R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 3.624901e-04 | 3.441 |
R-HSA-913531 | Interferon Signaling | 3.819352e-04 | 3.418 |
R-HSA-1852241 | Organelle biogenesis and maintenance | 3.907414e-04 | 3.408 |
R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 4.052678e-04 | 3.392 |
R-HSA-9678108 | SARS-CoV-1 Infection | 4.597425e-04 | 3.337 |
R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 4.787344e-04 | 3.320 |
R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 5.180116e-04 | 3.286 |
R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 5.180116e-04 | 3.286 |
R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 5.488498e-04 | 3.261 |
R-HSA-69481 | G2/M Checkpoints | 5.095669e-04 | 3.293 |
R-HSA-9692914 | SARS-CoV-1-host interactions | 5.508738e-04 | 3.259 |
R-HSA-9709570 | Impaired BRCA2 binding to RAD51 | 6.474176e-04 | 3.189 |
R-HSA-8854518 | AURKA Activation by TPX2 | 6.592831e-04 | 3.181 |
R-HSA-8856688 | Golgi-to-ER retrograde transport | 6.974950e-04 | 3.156 |
R-HSA-75153 | Apoptotic execution phase | 7.018452e-04 | 3.154 |
R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 7.018452e-04 | 3.154 |
R-HSA-9711097 | Cellular response to starvation | 7.225987e-04 | 3.141 |
R-HSA-5617833 | Cilium Assembly | 8.730057e-04 | 3.059 |
R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 9.610446e-04 | 3.017 |
R-HSA-373760 | L1CAM interactions | 1.080257e-03 | 2.966 |
R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 1.108472e-03 | 2.955 |
R-HSA-9613829 | Chaperone Mediated Autophagy | 1.109884e-03 | 2.955 |
R-HSA-3928664 | Ephrin signaling | 1.109884e-03 | 2.955 |
R-HSA-69473 | G2/M DNA damage checkpoint | 1.188549e-03 | 2.925 |
R-HSA-9705683 | SARS-CoV-2-host interactions | 1.222978e-03 | 2.913 |
R-HSA-6807878 | COPI-mediated anterograde transport | 1.253943e-03 | 2.902 |
R-HSA-380287 | Centrosome maturation | 1.273091e-03 | 2.895 |
R-HSA-1169408 | ISG15 antiviral mechanism | 1.273091e-03 | 2.895 |
R-HSA-901042 | Calnexin/calreticulin cycle | 1.301080e-03 | 2.886 |
R-HSA-5693616 | Presynaptic phase of homologous DNA pairing and strand exchange | 1.445103e-03 | 2.840 |
R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 1.555223e-03 | 2.808 |
R-HSA-70171 | Glycolysis | 1.575547e-03 | 2.803 |
R-HSA-9636667 | Manipulation of host energy metabolism | 1.600090e-03 | 2.796 |
R-HSA-5693532 | DNA Double-Strand Break Repair | 2.018025e-03 | 2.695 |
R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 2.140646e-03 | 2.669 |
R-HSA-8875555 | MET activates RAP1 and RAC1 | 2.150718e-03 | 2.667 |
R-HSA-9683686 | Maturation of spike protein | 2.150718e-03 | 2.667 |
R-HSA-392499 | Metabolism of proteins | 2.196294e-03 | 2.658 |
R-HSA-983189 | Kinesins | 2.241092e-03 | 2.650 |
R-HSA-9694516 | SARS-CoV-2 Infection | 2.444193e-03 | 2.612 |
R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 2.564334e-03 | 2.591 |
R-HSA-373755 | Semaphorin interactions | 2.769161e-03 | 2.558 |
R-HSA-390466 | Chaperonin-mediated protein folding | 2.859595e-03 | 2.544 |
R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 3.380056e-03 | 2.471 |
R-HSA-9609690 | HCMV Early Events | 3.406217e-03 | 2.468 |
R-HSA-1632852 | Macroautophagy | 3.943588e-03 | 2.404 |
R-HSA-391251 | Protein folding | 3.969811e-03 | 2.401 |
R-HSA-70326 | Glucose metabolism | 4.281852e-03 | 2.368 |
R-HSA-5620924 | Intraflagellar transport | 4.905498e-03 | 2.309 |
R-HSA-70263 | Gluconeogenesis | 4.905498e-03 | 2.309 |
R-HSA-199977 | ER to Golgi Anterograde Transport | 5.193990e-03 | 2.284 |
R-HSA-532668 | N-glycan trimming in the ER and Calnexin/Calreticulin cycle | 5.277573e-03 | 2.278 |
R-HSA-5663205 | Infectious disease | 5.307476e-03 | 2.275 |
R-HSA-9008059 | Interleukin-37 signaling | 5.486642e-03 | 2.261 |
R-HSA-2132295 | MHC class II antigen presentation | 5.558395e-03 | 2.255 |
R-HSA-205025 | NADE modulates death signalling | 6.161798e-03 | 2.210 |
R-HSA-5610787 | Hedgehog 'off' state | 6.211845e-03 | 2.207 |
R-HSA-9609646 | HCMV Infection | 6.789638e-03 | 2.168 |
R-HSA-5685938 | HDR through Single Strand Annealing (SSA) | 7.227904e-03 | 2.141 |
R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 7.441399e-03 | 2.128 |
R-HSA-5693607 | Processing of DNA double-strand break ends | 8.090791e-03 | 2.092 |
R-HSA-109581 | Apoptosis | 8.893570e-03 | 2.051 |
R-HSA-2028269 | Signaling by Hippo | 9.184293e-03 | 2.037 |
R-HSA-1643685 | Disease | 8.374813e-03 | 2.077 |
R-HSA-168316 | Assembly of Viral Components at the Budding Site | 8.281699e-03 | 2.082 |
R-HSA-597592 | Post-translational protein modification | 9.583335e-03 | 2.018 |
R-HSA-5687128 | MAPK6/MAPK4 signaling | 9.892424e-03 | 2.005 |
R-HSA-3371511 | HSF1 activation | 1.006699e-02 | 1.997 |
R-HSA-8937144 | Aryl hydrocarbon receptor signalling | 1.068146e-02 | 1.971 |
R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 1.084474e-02 | 1.965 |
R-HSA-180910 | Vpr-mediated nuclear import of PICs | 1.087466e-02 | 1.964 |
R-HSA-5358351 | Signaling by Hedgehog | 1.115364e-02 | 1.953 |
R-HSA-5683057 | MAPK family signaling cascades | 1.275669e-02 | 1.894 |
R-HSA-1280215 | Cytokine Signaling in Immune system | 1.283428e-02 | 1.892 |
R-HSA-5357801 | Programmed Cell Death | 1.287671e-02 | 1.890 |
R-HSA-9764265 | Regulation of CDH1 Expression and Function | 1.307326e-02 | 1.884 |
R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 1.307326e-02 | 1.884 |
R-HSA-8869496 | TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif... | 1.334970e-02 | 1.875 |
R-HSA-176033 | Interactions of Vpr with host cellular proteins | 1.354445e-02 | 1.868 |
R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 1.389166e-02 | 1.857 |
R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 1.770132e-02 | 1.752 |
R-HSA-2682334 | EPH-Ephrin signaling | 1.495783e-02 | 1.825 |
R-HSA-174417 | Telomere C-strand (Lagging Strand) Synthesis | 1.553651e-02 | 1.809 |
R-HSA-73894 | DNA Repair | 1.670243e-02 | 1.777 |
R-HSA-111996 | Ca-dependent events | 1.659800e-02 | 1.780 |
R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 1.707532e-02 | 1.768 |
R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 1.559541e-02 | 1.807 |
R-HSA-5336415 | Uptake and function of diphtheria toxin | 1.627538e-02 | 1.788 |
R-HSA-8949275 | RUNX3 Regulates Immune Response and Cell Migration | 1.627538e-02 | 1.788 |
R-HSA-1266738 | Developmental Biology | 1.716127e-02 | 1.765 |
R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 1.843768e-02 | 1.734 |
R-HSA-3928662 | EPHB-mediated forward signaling | 1.885454e-02 | 1.725 |
R-HSA-9674415 | Drug resistance of PDGFR mutants | 1.906754e-02 | 1.720 |
R-HSA-9674428 | PDGFR mutants bind TKIs | 1.906754e-02 | 1.720 |
R-HSA-9674403 | Regorafenib-resistant PDGFR mutants | 1.906754e-02 | 1.720 |
R-HSA-9674396 | Imatinib-resistant PDGFR mutants | 1.906754e-02 | 1.720 |
R-HSA-9674401 | Sunitinib-resistant PDGFR mutants | 1.906754e-02 | 1.720 |
R-HSA-9674404 | Sorafenib-resistant PDGFR mutants | 1.906754e-02 | 1.720 |
R-HSA-199991 | Membrane Trafficking | 2.051606e-02 | 1.688 |
R-HSA-110314 | Recognition of DNA damage by PCNA-containing replication complex | 2.082982e-02 | 1.681 |
R-HSA-69618 | Mitotic Spindle Checkpoint | 2.159253e-02 | 1.666 |
R-HSA-400685 | Sema4D in semaphorin signaling | 2.266615e-02 | 1.645 |
R-HSA-2025928 | Calcineurin activates NFAT | 2.285648e-02 | 1.641 |
R-HSA-9619229 | Activation of RAC1 downstream of NMDARs | 2.285648e-02 | 1.641 |
R-HSA-9834752 | Respiratory syncytial virus genome replication | 2.285648e-02 | 1.641 |
R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 2.329889e-02 | 1.633 |
R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 2.491731e-02 | 1.603 |
R-HSA-9820962 | Assembly and release of respiratory syncytial virus (RSV) virions | 2.649140e-02 | 1.577 |
R-HSA-174414 | Processive synthesis on the C-strand of the telomere | 2.659468e-02 | 1.575 |
R-HSA-912446 | Meiotic recombination | 2.820019e-02 | 1.550 |
R-HSA-948021 | Transport to the Golgi and subsequent modification | 2.897032e-02 | 1.538 |
R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 3.006130e-02 | 1.522 |
R-HSA-9734091 | Drug-mediated inhibition of MET activation | 3.777266e-02 | 1.423 |
R-HSA-9709275 | Impaired BRCA2 translocation to the nucleus | 3.777266e-02 | 1.423 |
R-HSA-5632987 | Defective Mismatch Repair Associated With PMS2 | 3.777266e-02 | 1.423 |
R-HSA-5545483 | Defective Mismatch Repair Associated With MLH1 | 3.777266e-02 | 1.423 |
R-HSA-9763198 | Impaired BRCA2 binding to SEM1 (DSS1) | 3.777266e-02 | 1.423 |
R-HSA-416550 | Sema4D mediated inhibition of cell attachment and migration | 3.440089e-02 | 1.463 |
R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 3.312441e-02 | 1.480 |
R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 3.546945e-02 | 1.450 |
R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 3.546945e-02 | 1.450 |
R-HSA-5693548 | Sensing of DNA Double Strand Breaks | 3.440089e-02 | 1.463 |
R-HSA-6802957 | Oncogenic MAPK signaling | 3.525624e-02 | 1.453 |
R-HSA-9933387 | RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression | 3.312441e-02 | 1.480 |
R-HSA-169131 | Inhibition of PKR | 3.777266e-02 | 1.423 |
R-HSA-192905 | vRNP Assembly | 3.034270e-02 | 1.518 |
R-HSA-112315 | Transmission across Chemical Synapses | 3.574090e-02 | 1.447 |
R-HSA-5653656 | Vesicle-mediated transport | 3.197026e-02 | 1.495 |
R-HSA-3299685 | Detoxification of Reactive Oxygen Species | 3.629767e-02 | 1.440 |
R-HSA-9679506 | SARS-CoV Infections | 3.170940e-02 | 1.499 |
R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 3.804907e-02 | 1.420 |
R-HSA-2980766 | Nuclear Envelope Breakdown | 3.806184e-02 | 1.420 |
R-HSA-69109 | Leading Strand Synthesis | 3.865672e-02 | 1.413 |
R-HSA-69091 | Polymerase switching | 3.865672e-02 | 1.413 |
R-HSA-3000484 | Scavenging by Class F Receptors | 3.865672e-02 | 1.413 |
R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 3.865672e-02 | 1.413 |
R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 3.865672e-02 | 1.413 |
R-HSA-1855170 | IPs transport between nucleus and cytosol | 4.040911e-02 | 1.394 |
R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 4.040911e-02 | 1.394 |
R-HSA-9022692 | Regulation of MECP2 expression and activity | 4.040911e-02 | 1.394 |
R-HSA-194441 | Metabolism of non-coding RNA | 4.173544e-02 | 1.379 |
R-HSA-191859 | snRNP Assembly | 4.173544e-02 | 1.379 |
R-HSA-180786 | Extension of Telomeres | 4.173544e-02 | 1.379 |
R-HSA-418990 | Adherens junctions interactions | 4.291599e-02 | 1.367 |
R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 4.300244e-02 | 1.367 |
R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 4.300244e-02 | 1.367 |
R-HSA-9768727 | Regulation of CDH1 posttranslational processing and trafficking to plasma membra... | 4.300244e-02 | 1.367 |
R-HSA-5685939 | HDR through MMEJ (alt-NHEJ) | 4.310124e-02 | 1.366 |
R-HSA-75035 | Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex | 4.310124e-02 | 1.366 |
R-HSA-5619111 | Defective SLC20A2 causes idiopathic basal ganglia calcification 1 (IBGC1) | 5.612222e-02 | 1.251 |
R-HSA-3270619 | IRF3-mediated induction of type I IFN | 5.252181e-02 | 1.280 |
R-HSA-176412 | Phosphorylation of the APC/C | 5.748126e-02 | 1.240 |
R-HSA-9687136 | Aberrant regulation of mitotic exit in cancer due to RB1 defects | 5.748126e-02 | 1.240 |
R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 4.843237e-02 | 1.315 |
R-HSA-8875878 | MET promotes cell motility | 5.717235e-02 | 1.243 |
R-HSA-186797 | Signaling by PDGF | 4.760897e-02 | 1.322 |
R-HSA-9673324 | WNT5:FZD7-mediated leishmania damping | 5.748126e-02 | 1.240 |
R-HSA-9664420 | Killing mechanisms | 5.748126e-02 | 1.240 |
R-HSA-169893 | Prolonged ERK activation events | 5.748126e-02 | 1.240 |
R-HSA-111447 | Activation of BAD and translocation to mitochondria | 5.252181e-02 | 1.280 |
R-HSA-983170 | Antigen Presentation: Folding, assembly and peptide loading of class I MHC | 4.567714e-02 | 1.340 |
R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 4.966344e-02 | 1.304 |
R-HSA-5607763 | CLEC7A (Dectin-1) induces NFAT activation | 4.772574e-02 | 1.321 |
R-HSA-5673000 | RAF activation | 4.567714e-02 | 1.340 |
R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 4.843237e-02 | 1.315 |
R-HSA-180746 | Nuclear import of Rev protein | 4.567714e-02 | 1.340 |
R-HSA-6784531 | tRNA processing in the nucleus | 4.760897e-02 | 1.322 |
R-HSA-112043 | PLC beta mediated events | 4.560276e-02 | 1.341 |
R-HSA-111933 | Calmodulin induced events | 5.126728e-02 | 1.290 |
R-HSA-111997 | CaM pathway | 5.126728e-02 | 1.290 |
R-HSA-9755779 | SARS-CoV-2 targets host intracellular signalling and regulatory pathways | 5.252181e-02 | 1.280 |
R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 5.717235e-02 | 1.243 |
R-HSA-162909 | Host Interactions of HIV factors | 5.253206e-02 | 1.280 |
R-HSA-9006925 | Intracellular signaling by second messengers | 4.993373e-02 | 1.302 |
R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 5.252181e-02 | 1.280 |
R-HSA-3700989 | Transcriptional Regulation by TP53 | 5.140899e-02 | 1.289 |
R-HSA-8986944 | Transcriptional Regulation by MECP2 | 4.560955e-02 | 1.341 |
R-HSA-446203 | Asparagine N-linked glycosylation | 5.005038e-02 | 1.301 |
R-HSA-168268 | Virus Assembly and Release | 5.748126e-02 | 1.240 |
R-HSA-112040 | G-protein mediated events | 5.836137e-02 | 1.234 |
R-HSA-74160 | Gene expression (Transcription) | 5.969661e-02 | 1.224 |
R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 6.024049e-02 | 1.220 |
R-HSA-9931509 | Expression of BMAL (ARNTL), CLOCK, and NPAS2 | 6.024049e-02 | 1.220 |
R-HSA-8957275 | Post-translational protein phosphorylation | 6.132403e-02 | 1.212 |
R-HSA-141430 | Inactivation of APC/C via direct inhibition of the APC/C complex | 6.259617e-02 | 1.203 |
R-HSA-141405 | Inhibition of the proteolytic activity of APC/C required for the onset of anapha... | 6.259617e-02 | 1.203 |
R-HSA-1500931 | Cell-Cell communication | 6.305256e-02 | 1.200 |
R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 6.338430e-02 | 1.198 |
R-HSA-177243 | Interactions of Rev with host cellular proteins | 6.338430e-02 | 1.198 |
R-HSA-5218920 | VEGFR2 mediated vascular permeability | 6.660265e-02 | 1.177 |
R-HSA-9694548 | Maturation of spike protein | 6.660265e-02 | 1.177 |
R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 6.660265e-02 | 1.177 |
R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 6.781817e-02 | 1.169 |
R-HSA-174437 | Removal of the Flap Intermediate from the C-strand | 6.785884e-02 | 1.168 |
R-HSA-176407 | Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase | 6.785884e-02 | 1.168 |
R-HSA-5358565 | Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) | 6.785884e-02 | 1.168 |
R-HSA-5358606 | Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) | 6.785884e-02 | 1.168 |
R-HSA-9683701 | Translation of Structural Proteins | 6.989438e-02 | 1.156 |
R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 7.412297e-02 | 1.130 |
R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 7.412297e-02 | 1.130 |
R-HSA-3560796 | Defective PAPSS2 causes SEMD-PA | 7.412297e-02 | 1.130 |
R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 7.412297e-02 | 1.130 |
R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 7.412297e-02 | 1.130 |
R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 7.412297e-02 | 1.130 |
R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 7.412297e-02 | 1.130 |
R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 7.412297e-02 | 1.130 |
R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 7.412297e-02 | 1.130 |
R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 7.412297e-02 | 1.130 |
R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 7.412297e-02 | 1.130 |
R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 7.412297e-02 | 1.130 |
R-HSA-8875513 | MET interacts with TNS proteins | 9.178151e-02 | 1.037 |
R-HSA-9673766 | Signaling by cytosolic PDGFRA and PDGFRB fusion proteins | 9.178151e-02 | 1.037 |
R-HSA-8865999 | MET activates PTPN11 | 9.178151e-02 | 1.037 |
R-HSA-5660862 | Defective SLC7A7 causes lysinuric protein intolerance (LPI) | 9.178151e-02 | 1.037 |
R-HSA-5651801 | PCNA-Dependent Long Patch Base Excision Repair | 7.326182e-02 | 1.135 |
R-HSA-174048 | APC/C:Cdc20 mediated degradation of Cyclin B | 7.879789e-02 | 1.103 |
R-HSA-6807004 | Negative regulation of MET activity | 8.446005e-02 | 1.073 |
R-HSA-179409 | APC-Cdc20 mediated degradation of Nek2A | 9.024151e-02 | 1.045 |
R-HSA-5696397 | Gap-filling DNA repair synthesis and ligation in GG-NER | 9.613570e-02 | 1.017 |
R-HSA-174084 | Autodegradation of Cdh1 by Cdh1:APC/C | 8.741099e-02 | 1.058 |
R-HSA-174154 | APC/C:Cdc20 mediated degradation of Securin | 9.111691e-02 | 1.040 |
R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 7.282606e-02 | 1.138 |
R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 9.758048e-02 | 1.011 |
R-HSA-6806834 | Signaling by MET | 9.177436e-02 | 1.037 |
R-HSA-9671555 | Signaling by PDGFR in disease | 9.613570e-02 | 1.017 |
R-HSA-69186 | Lagging Strand Synthesis | 9.024151e-02 | 1.045 |
R-HSA-73893 | DNA Damage Bypass | 9.872066e-02 | 1.006 |
R-HSA-373753 | Nephrin family interactions | 8.446005e-02 | 1.073 |
R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 1.035542e-01 | 0.985 |
R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 7.541707e-02 | 1.123 |
R-HSA-5619507 | Activation of HOX genes during differentiation | 7.541707e-02 | 1.123 |
R-HSA-5626978 | TNFR1-mediated ceramide production | 1.091043e-01 | 0.962 |
R-HSA-5358508 | Mismatch Repair | 7.326182e-02 | 1.135 |
R-HSA-8875791 | MET activates STAT3 | 9.178151e-02 | 1.037 |
R-HSA-350054 | Notch-HLH transcription pathway | 1.021363e-01 | 0.991 |
R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 8.377084e-02 | 1.077 |
R-HSA-69239 | Synthesis of DNA | 8.195099e-02 | 1.086 |
R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 1.058054e-01 | 0.975 |
R-HSA-3371571 | HSF1-dependent transactivation | 1.065710e-01 | 0.972 |
R-HSA-1500620 | Meiosis | 1.066026e-01 | 0.972 |
R-HSA-5423599 | Diseases of Mismatch Repair (MMR) | 9.178151e-02 | 1.037 |
R-HSA-9960525 | CASP5-mediated substrate cleavage | 9.178151e-02 | 1.037 |
R-HSA-1834941 | STING mediated induction of host immune responses | 7.879789e-02 | 1.103 |
R-HSA-69242 | S Phase | 1.038511e-01 | 0.984 |
R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 9.488726e-02 | 1.023 |
R-HSA-2559583 | Cellular Senescence | 9.252904e-02 | 1.034 |
R-HSA-211736 | Stimulation of the cell death response by PAK-2p34 | 7.412297e-02 | 1.130 |
R-HSA-9960519 | CASP4-mediated substrate cleavage | 9.178151e-02 | 1.037 |
R-HSA-162906 | HIV Infection | 1.074339e-01 | 0.969 |
R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 7.282606e-02 | 1.138 |
R-HSA-432142 | Platelet sensitization by LDL | 7.326182e-02 | 1.135 |
R-HSA-1489509 | DAG and IP3 signaling | 8.377084e-02 | 1.077 |
R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 8.741099e-02 | 1.058 |
R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 8.446005e-02 | 1.073 |
R-HSA-162582 | Signal Transduction | 1.024299e-01 | 0.990 |
R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 9.119658e-02 | 1.040 |
R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 9.613570e-02 | 1.017 |
R-HSA-421270 | Cell-cell junction organization | 8.144353e-02 | 1.089 |
R-HSA-4086400 | PCP/CE pathway | 8.613966e-02 | 1.065 |
R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 1.007850e-01 | 0.997 |
R-HSA-9711123 | Cellular response to chemical stress | 1.075194e-01 | 0.969 |
R-HSA-381119 | Unfolded Protein Response (UPR) | 8.325455e-02 | 1.080 |
R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 1.096913e-01 | 0.960 |
R-HSA-141424 | Amplification of signal from the kinetochores | 1.096913e-01 | 0.960 |
R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 1.096913e-01 | 0.960 |
R-HSA-174184 | Cdc20:Phospho-APC/C mediated degradation of Cyclin A | 1.105852e-01 | 0.956 |
R-HSA-1592230 | Mitochondrial biogenesis | 1.109469e-01 | 0.955 |
R-HSA-71291 | Metabolism of amino acids and derivatives | 1.139959e-01 | 0.943 |
R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 1.144320e-01 | 0.941 |
R-HSA-8863678 | Neurodegenerative Diseases | 1.144320e-01 | 0.941 |
R-HSA-179419 | APC:Cdc20 mediated degradation of cell cycle proteins prior to satisfation of th... | 1.146567e-01 | 0.941 |
R-HSA-174178 | APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins ... | 1.146567e-01 | 0.941 |
R-HSA-69306 | DNA Replication | 1.150602e-01 | 0.939 |
R-HSA-76002 | Platelet activation, signaling and aggregation | 1.177296e-01 | 0.929 |
R-HSA-69017 | CDK-mediated phosphorylation and removal of Cdc6 | 1.187842e-01 | 0.925 |
R-HSA-174411 | Polymerase switching on the C-strand of the telomere | 1.207154e-01 | 0.918 |
R-HSA-73886 | Chromosome Maintenance | 1.215846e-01 | 0.915 |
R-HSA-176409 | APC/C:Cdc20 mediated degradation of mitotic proteins | 1.229662e-01 | 0.910 |
R-HSA-418597 | G alpha (z) signalling events | 1.229662e-01 | 0.910 |
R-HSA-162587 | HIV Life Cycle | 1.244489e-01 | 0.905 |
R-HSA-446728 | Cell junction organization | 1.248221e-01 | 0.904 |
R-HSA-447038 | NrCAM interactions | 1.260978e-01 | 0.899 |
R-HSA-9022537 | Loss of MECP2 binding ability to the NCoR/SMRT complex | 1.427681e-01 | 0.845 |
R-HSA-177539 | Autointegration results in viral DNA circles | 1.591215e-01 | 0.798 |
R-HSA-6802953 | RAS signaling downstream of NF1 loss-of-function variants | 1.591215e-01 | 0.798 |
R-HSA-8851907 | MET activates PI3K/AKT signaling | 1.751638e-01 | 0.757 |
R-HSA-9726840 | SHOC2 M1731 mutant abolishes MRAS complex function | 1.751638e-01 | 0.757 |
R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 1.909011e-01 | 0.719 |
R-HSA-111995 | phospho-PLA2 pathway | 1.909011e-01 | 0.719 |
R-HSA-8875656 | MET receptor recycling | 1.909011e-01 | 0.719 |
R-HSA-196025 | Formation of annular gap junctions | 1.909011e-01 | 0.719 |
R-HSA-9660537 | Signaling by MRAS-complex mutants | 1.909011e-01 | 0.719 |
R-HSA-9726842 | Gain-of-function MRAS complexes activate RAF signaling | 1.909011e-01 | 0.719 |
R-HSA-170984 | ARMS-mediated activation | 2.063391e-01 | 0.685 |
R-HSA-190873 | Gap junction degradation | 2.063391e-01 | 0.685 |
R-HSA-5467348 | Truncations of AMER1 destabilize the destruction complex | 2.363397e-01 | 0.626 |
R-HSA-5467340 | AXIN missense mutants destabilize the destruction complex | 2.363397e-01 | 0.626 |
R-HSA-5467337 | APC truncation mutants have impaired AXIN binding | 2.363397e-01 | 0.626 |
R-HSA-5339716 | Signaling by GSK3beta mutants | 2.509134e-01 | 0.600 |
R-HSA-9615710 | Late endosomal microautophagy | 1.466242e-01 | 0.834 |
R-HSA-5696394 | DNA Damage Recognition in GG-NER | 1.803799e-01 | 0.744 |
R-HSA-176814 | Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins | 1.272013e-01 | 0.896 |
R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 1.674632e-01 | 0.776 |
R-HSA-1989781 | PPARA activates gene expression | 2.423071e-01 | 0.616 |
R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 2.494214e-01 | 0.603 |
R-HSA-186763 | Downstream signal transduction | 1.599721e-01 | 0.796 |
R-HSA-5656169 | Termination of translesion DNA synthesis | 1.466242e-01 | 0.834 |
R-HSA-110313 | Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA templa... | 2.362872e-01 | 0.627 |
R-HSA-9664873 | Pexophagy | 2.214834e-01 | 0.655 |
R-HSA-6798695 | Neutrophil degranulation | 1.361318e-01 | 0.866 |
R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 2.216320e-01 | 0.654 |
R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 1.402102e-01 | 0.853 |
R-HSA-5693606 | DNA Double Strand Break Response | 1.768708e-01 | 0.752 |
R-HSA-9843745 | Adipogenesis | 1.561623e-01 | 0.806 |
R-HSA-453276 | Regulation of mitotic cell cycle | 1.961022e-01 | 0.708 |
R-HSA-174143 | APC/C-mediated degradation of cell cycle proteins | 1.961022e-01 | 0.708 |
R-HSA-162592 | Integration of provirus | 2.509134e-01 | 0.600 |
R-HSA-9656223 | Signaling by RAF1 mutants | 2.433627e-01 | 0.614 |
R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 1.270763e-01 | 0.896 |
R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 2.063391e-01 | 0.685 |
R-HSA-381340 | Transcriptional regulation of white adipocyte differentiation | 1.532537e-01 | 0.815 |
R-HSA-1606341 | IRF3 mediated activation of type 1 IFN | 1.260978e-01 | 0.899 |
R-HSA-8857538 | PTK6 promotes HIF1A stabilization | 1.591215e-01 | 0.798 |
R-HSA-69190 | DNA strand elongation | 1.667277e-01 | 0.778 |
R-HSA-5696400 | Dual Incision in GG-NER | 1.872681e-01 | 0.728 |
R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 1.909783e-01 | 0.719 |
R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 2.387709e-01 | 0.622 |
R-HSA-6806942 | MET Receptor Activation | 1.591215e-01 | 0.798 |
R-HSA-450341 | Activation of the AP-1 family of transcription factors | 2.063391e-01 | 0.685 |
R-HSA-9820841 | M-decay: degradation of maternal mRNAs by maternally stored factors | 2.362872e-01 | 0.627 |
R-HSA-5696398 | Nucleotide Excision Repair | 1.904945e-01 | 0.720 |
R-HSA-9032759 | NTRK2 activates RAC1 | 1.260978e-01 | 0.899 |
R-HSA-111459 | Activation of caspases through apoptosome-mediated cleavage | 1.427681e-01 | 0.845 |
R-HSA-418889 | Caspase activation via Dependence Receptors in the absence of ligand | 2.063391e-01 | 0.685 |
R-HSA-2468052 | Establishment of Sister Chromatid Cohesion | 2.214834e-01 | 0.655 |
R-HSA-4839744 | Signaling by APC mutants | 2.363397e-01 | 0.626 |
R-HSA-177135 | Conjugation of benzoate with glycine | 2.363397e-01 | 0.626 |
R-HSA-4839748 | Signaling by AMER1 mutants | 2.509134e-01 | 0.600 |
R-HSA-4839735 | Signaling by AXIN mutants | 2.509134e-01 | 0.600 |
R-HSA-1250196 | SHC1 events in ERBB2 signaling | 1.532694e-01 | 0.815 |
R-HSA-9929491 | SPOP-mediated proteasomal degradation of PD-L1(CD274) | 2.362872e-01 | 0.627 |
R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 1.426722e-01 | 0.846 |
R-HSA-199418 | Negative regulation of the PI3K/AKT network | 1.501371e-01 | 0.824 |
R-HSA-212165 | Epigenetic regulation of gene expression | 2.189804e-01 | 0.660 |
R-HSA-379716 | Cytosolic tRNA aminoacylation | 2.504469e-01 | 0.601 |
R-HSA-1227990 | Signaling by ERBB2 in Cancer | 1.532694e-01 | 0.815 |
R-HSA-8963888 | Chylomicron assembly | 2.363397e-01 | 0.626 |
R-HSA-349425 | Autodegradation of the E3 ubiquitin ligase COP1 | 1.872681e-01 | 0.728 |
R-HSA-69541 | Stabilization of p53 | 2.221743e-01 | 0.653 |
R-HSA-9707616 | Heme signaling | 1.536440e-01 | 0.813 |
R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 1.710090e-01 | 0.767 |
R-HSA-5689603 | UCH proteinases | 2.208064e-01 | 0.656 |
R-HSA-194138 | Signaling by VEGF | 1.355230e-01 | 0.868 |
R-HSA-176408 | Regulation of APC/C activators between G1/S and early anaphase | 1.536440e-01 | 0.813 |
R-HSA-157579 | Telomere Maintenance | 1.568455e-01 | 0.805 |
R-HSA-111464 | SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes | 1.260978e-01 | 0.899 |
R-HSA-175567 | Integration of viral DNA into host genomic DNA | 1.591215e-01 | 0.798 |
R-HSA-1296052 | Ca2+ activated K+ channels | 1.751638e-01 | 0.757 |
R-HSA-8964041 | LDL remodeling | 1.751638e-01 | 0.757 |
R-HSA-1433617 | Regulation of signaling by NODAL | 2.063391e-01 | 0.685 |
R-HSA-164843 | 2-LTR circle formation | 2.214834e-01 | 0.655 |
R-HSA-9623433 | NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis | 2.509134e-01 | 0.600 |
R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 2.509134e-01 | 0.600 |
R-HSA-9687139 | Aberrant regulation of mitotic cell cycle due to RB1 defects | 1.532694e-01 | 0.815 |
R-HSA-168325 | Viral Messenger RNA Synthesis | 1.491213e-01 | 0.826 |
R-HSA-110373 | Resolution of AP sites via the multiple-nucleotide patch replacement pathway | 1.270817e-01 | 0.896 |
R-HSA-111469 | SMAC, XIAP-regulated apoptotic response | 1.427681e-01 | 0.845 |
R-HSA-69052 | Switching of origins to a post-replicative state | 2.059034e-01 | 0.686 |
R-HSA-111885 | Opioid Signalling | 1.828237e-01 | 0.738 |
R-HSA-9909396 | Circadian clock | 1.592120e-01 | 0.798 |
R-HSA-3214841 | PKMTs methylate histone lysines | 2.362872e-01 | 0.627 |
R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 2.009885e-01 | 0.697 |
R-HSA-162599 | Late Phase of HIV Life Cycle | 1.975882e-01 | 0.704 |
R-HSA-9013973 | TICAM1-dependent activation of IRF3/IRF7 | 2.509134e-01 | 0.600 |
R-HSA-8943724 | Regulation of PTEN gene transcription | 1.446429e-01 | 0.840 |
R-HSA-5673001 | RAF/MAP kinase cascade | 1.454740e-01 | 0.837 |
R-HSA-111463 | SMAC (DIABLO) binds to IAPs | 1.260978e-01 | 0.899 |
R-HSA-427652 | Sodium-coupled phosphate cotransporters | 1.427681e-01 | 0.845 |
R-HSA-428543 | Inactivation of CDC42 and RAC1 | 2.063391e-01 | 0.685 |
R-HSA-140342 | Apoptosis induced DNA fragmentation | 2.214834e-01 | 0.655 |
R-HSA-428540 | Activation of RAC1 | 2.509134e-01 | 0.600 |
R-HSA-1474151 | Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation | 1.532694e-01 | 0.815 |
R-HSA-9833109 | Evasion by RSV of host interferon responses | 1.599721e-01 | 0.796 |
R-HSA-187687 | Signalling to ERKs | 1.941923e-01 | 0.712 |
R-HSA-9764561 | Regulation of CDH1 Function | 1.314879e-01 | 0.881 |
R-HSA-69002 | DNA Replication Pre-Initiation | 2.061316e-01 | 0.686 |
R-HSA-5684996 | MAPK1/MAPK3 signaling | 1.594618e-01 | 0.797 |
R-HSA-1227986 | Signaling by ERBB2 | 1.446429e-01 | 0.840 |
R-HSA-176187 | Activation of ATR in response to replication stress | 1.735317e-01 | 0.761 |
R-HSA-8863795 | Downregulation of ERBB2 signaling | 1.532694e-01 | 0.815 |
R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 1.260978e-01 | 0.899 |
R-HSA-164944 | Nef and signal transduction | 1.591215e-01 | 0.798 |
R-HSA-8866423 | VLDL assembly | 1.591215e-01 | 0.798 |
R-HSA-9614399 | Regulation of localization of FOXO transcription factors | 2.363397e-01 | 0.626 |
R-HSA-9675126 | Diseases of mitotic cell cycle | 1.667277e-01 | 0.778 |
R-HSA-3371568 | Attenuation phase | 2.292234e-01 | 0.640 |
R-HSA-3000480 | Scavenging by Class A Receptors | 2.433627e-01 | 0.614 |
R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 1.912459e-01 | 0.718 |
R-HSA-5578749 | Transcriptional regulation by small RNAs | 2.009885e-01 | 0.697 |
R-HSA-112316 | Neuronal System | 1.530647e-01 | 0.815 |
R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 2.434407e-01 | 0.614 |
R-HSA-264876 | Insulin processing | 1.335254e-01 | 0.874 |
R-HSA-9032845 | Activated NTRK2 signals through CDK5 | 1.751638e-01 | 0.757 |
R-HSA-442380 | Zinc influx into cells by the SLC39 gene family | 2.063391e-01 | 0.685 |
R-HSA-6804757 | Regulation of TP53 Degradation | 2.011487e-01 | 0.696 |
R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 1.532537e-01 | 0.815 |
R-HSA-111932 | CaMK IV-mediated phosphorylation of CREB | 2.214834e-01 | 0.655 |
R-HSA-9020956 | Interleukin-27 signaling | 2.214834e-01 | 0.655 |
R-HSA-447043 | Neurofascin interactions | 1.591215e-01 | 0.798 |
R-HSA-9032500 | Activated NTRK2 signals through FYN | 1.909011e-01 | 0.719 |
R-HSA-450520 | HuR (ELAVL1) binds and stabilizes mRNA | 2.063391e-01 | 0.685 |
R-HSA-6806003 | Regulation of TP53 Expression and Degradation | 2.221743e-01 | 0.653 |
R-HSA-73933 | Resolution of Abasic Sites (AP sites) | 2.362872e-01 | 0.627 |
R-HSA-3858494 | Beta-catenin independent WNT signaling | 1.748163e-01 | 0.757 |
R-HSA-1257604 | PIP3 activates AKT signaling | 1.574246e-01 | 0.803 |
R-HSA-114604 | GPVI-mediated activation cascade | 2.011487e-01 | 0.696 |
R-HSA-168256 | Immune System | 2.364183e-01 | 0.626 |
R-HSA-9007101 | Rab regulation of trafficking | 2.466918e-01 | 0.608 |
R-HSA-5633007 | Regulation of TP53 Activity | 1.317294e-01 | 0.880 |
R-HSA-114508 | Effects of PIP2 hydrolysis | 1.803799e-01 | 0.744 |
R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 1.912459e-01 | 0.718 |
R-HSA-114452 | Activation of BH3-only proteins | 1.532694e-01 | 0.815 |
R-HSA-109606 | Intrinsic Pathway for Apoptosis | 1.272013e-01 | 0.896 |
R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 1.780057e-01 | 0.750 |
R-HSA-9020933 | Interleukin-23 signaling | 1.909011e-01 | 0.719 |
R-HSA-111461 | Cytochrome c-mediated apoptotic response | 2.509134e-01 | 0.600 |
R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 1.335254e-01 | 0.874 |
R-HSA-193704 | p75 NTR receptor-mediated signalling | 1.641219e-01 | 0.785 |
R-HSA-909733 | Interferon alpha/beta signaling | 2.384340e-01 | 0.623 |
R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 1.270817e-01 | 0.896 |
R-HSA-8853884 | Transcriptional Regulation by VENTX | 2.362872e-01 | 0.627 |
R-HSA-1538133 | G0 and Early G1 | 1.667277e-01 | 0.778 |
R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 2.214834e-01 | 0.655 |
R-HSA-73887 | Death Receptor Signaling | 2.387709e-01 | 0.622 |
R-HSA-9694635 | Translation of Structural Proteins | 2.258223e-01 | 0.646 |
R-HSA-212436 | Generic Transcription Pathway | 2.071903e-01 | 0.684 |
R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 2.433627e-01 | 0.614 |
R-HSA-1368108 | BMAL1:CLOCK,NPAS2 activates circadian expression | 1.872681e-01 | 0.728 |
R-HSA-211000 | Gene Silencing by RNA | 1.982656e-01 | 0.703 |
R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 1.335254e-01 | 0.874 |
R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 2.508444e-01 | 0.601 |
R-HSA-9730414 | MITF-M-regulated melanocyte development | 1.656828e-01 | 0.781 |
R-HSA-446652 | Interleukin-1 family signaling | 2.317425e-01 | 0.635 |
R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 2.221743e-01 | 0.653 |
R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 2.512053e-01 | 0.600 |
R-HSA-9707564 | Cytoprotection by HMOX1 | 2.563337e-01 | 0.591 |
R-HSA-877300 | Interferon gamma signaling | 2.565886e-01 | 0.591 |
R-HSA-5619115 | Disorders of transmembrane transporters | 2.574795e-01 | 0.589 |
R-HSA-9637690 | Response of Mtb to phagocytosis | 2.575369e-01 | 0.589 |
R-HSA-1433557 | Signaling by SCF-KIT | 2.575369e-01 | 0.589 |
R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 2.581414e-01 | 0.588 |
R-HSA-68875 | Mitotic Prophase | 2.591933e-01 | 0.586 |
R-HSA-373752 | Netrin-1 signaling | 2.646298e-01 | 0.577 |
R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 2.646298e-01 | 0.577 |
R-HSA-8851805 | MET activates RAS signaling | 2.652098e-01 | 0.576 |
R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 2.652098e-01 | 0.576 |
R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 2.652098e-01 | 0.576 |
R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 2.652098e-01 | 0.576 |
R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 2.652098e-01 | 0.576 |
R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 2.652098e-01 | 0.576 |
R-HSA-9931530 | Phosphorylation and nuclear translocation of the CRY:PER:kinase complex | 2.652098e-01 | 0.576 |
R-HSA-380615 | Serotonin clearance from the synaptic cleft | 2.652098e-01 | 0.576 |
R-HSA-177128 | Conjugation of salicylate with glycine | 2.652098e-01 | 0.576 |
R-HSA-1679131 | Trafficking and processing of endosomal TLR | 2.652098e-01 | 0.576 |
R-HSA-877312 | Regulation of IFNG signaling | 2.652098e-01 | 0.576 |
R-HSA-9005891 | Loss of function of MECP2 in Rett syndrome | 2.652098e-01 | 0.576 |
R-HSA-9005895 | Pervasive developmental disorders | 2.652098e-01 | 0.576 |
R-HSA-9697154 | Disorders of Nervous System Development | 2.652098e-01 | 0.576 |
R-HSA-8984722 | Interleukin-35 Signalling | 2.652098e-01 | 0.576 |
R-HSA-195721 | Signaling by WNT | 2.717186e-01 | 0.566 |
R-HSA-5678895 | Defective CFTR causes cystic fibrosis | 2.717230e-01 | 0.566 |
R-HSA-432040 | Vasopressin regulates renal water homeostasis via Aquaporins | 2.717230e-01 | 0.566 |
R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 2.788140e-01 | 0.555 |
R-HSA-9649948 | Signaling downstream of RAS mutants | 2.788140e-01 | 0.555 |
R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 2.788140e-01 | 0.555 |
R-HSA-6802949 | Signaling by RAS mutants | 2.788140e-01 | 0.555 |
R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 2.788140e-01 | 0.555 |
R-HSA-170660 | Adenylate cyclase activating pathway | 2.792342e-01 | 0.554 |
R-HSA-174490 | Membrane binding and targetting of GAG proteins | 2.792342e-01 | 0.554 |
R-HSA-389359 | CD28 dependent Vav1 pathway | 2.792342e-01 | 0.554 |
R-HSA-170968 | Frs2-mediated activation | 2.792342e-01 | 0.554 |
R-HSA-8877330 | RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) | 2.792342e-01 | 0.554 |
R-HSA-5688426 | Deubiquitination | 2.810098e-01 | 0.551 |
R-HSA-5619102 | SLC transporter disorders | 2.857198e-01 | 0.544 |
R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 2.859002e-01 | 0.544 |
R-HSA-9645723 | Diseases of programmed cell death | 2.873656e-01 | 0.542 |
R-HSA-109582 | Hemostasis | 2.910380e-01 | 0.536 |
R-HSA-1236974 | ER-Phagosome pathway | 2.925703e-01 | 0.534 |
R-HSA-389356 | Co-stimulation by CD28 | 2.929793e-01 | 0.533 |
R-HSA-69166 | Removal of the Flap Intermediate | 2.929919e-01 | 0.533 |
R-HSA-174495 | Synthesis And Processing Of GAG, GAGPOL Polyproteins | 2.929919e-01 | 0.533 |
R-HSA-1483115 | Hydrolysis of LPC | 2.929919e-01 | 0.533 |
R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 2.929919e-01 | 0.533 |
R-HSA-1433559 | Regulation of KIT signaling | 2.929919e-01 | 0.533 |
R-HSA-9686114 | Non-canonical inflammasome activation | 2.929919e-01 | 0.533 |
R-HSA-1482798 | Acyl chain remodeling of CL | 2.929919e-01 | 0.533 |
R-HSA-435354 | Zinc transporters | 2.929919e-01 | 0.533 |
R-HSA-114608 | Platelet degranulation | 2.930772e-01 | 0.533 |
R-HSA-69580 | p53-Dependent G1/S DNA damage checkpoint | 3.000489e-01 | 0.523 |
R-HSA-69563 | p53-Dependent G1 DNA Damage Response | 3.000489e-01 | 0.523 |
R-HSA-9766229 | Degradation of CDH1 | 3.000489e-01 | 0.523 |
R-HSA-2122947 | NOTCH1 Intracellular Domain Regulates Transcription | 3.000489e-01 | 0.523 |
R-HSA-72306 | tRNA processing | 3.005163e-01 | 0.522 |
R-HSA-8875360 | InlB-mediated entry of Listeria monocytogenes into host cell | 3.064877e-01 | 0.514 |
R-HSA-9027284 | Erythropoietin activates RAS | 3.064877e-01 | 0.514 |
R-HSA-9673767 | Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants | 3.064877e-01 | 0.514 |
R-HSA-9673770 | Signaling by PDGFRA extracellular domain mutants | 3.064877e-01 | 0.514 |
R-HSA-170670 | Adenylate cyclase inhibitory pathway | 3.064877e-01 | 0.514 |
R-HSA-196299 | Beta-catenin phosphorylation cascade | 3.064877e-01 | 0.514 |
R-HSA-69183 | Processive synthesis on the lagging strand | 3.064877e-01 | 0.514 |
R-HSA-110312 | Translesion synthesis by REV1 | 3.064877e-01 | 0.514 |
R-HSA-174362 | Transport and metabolism of PAPS | 3.064877e-01 | 0.514 |
R-HSA-1502540 | Signaling by Activin | 3.064877e-01 | 0.514 |
R-HSA-9857492 | Protein lipoylation | 3.064877e-01 | 0.514 |
R-HSA-8876725 | Protein methylation | 3.064877e-01 | 0.514 |
R-HSA-418885 | DCC mediated attractive signaling | 3.064877e-01 | 0.514 |
R-HSA-5658442 | Regulation of RAS by GAPs | 3.071069e-01 | 0.513 |
R-HSA-1474165 | Reproduction | 3.102403e-01 | 0.508 |
R-HSA-5689880 | Ub-specific processing proteases | 3.116930e-01 | 0.506 |
R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 3.134425e-01 | 0.504 |
R-HSA-5358346 | Hedgehog ligand biogenesis | 3.141511e-01 | 0.503 |
R-HSA-2514856 | The phototransduction cascade | 3.141511e-01 | 0.503 |
R-HSA-73857 | RNA Polymerase II Transcription | 3.168998e-01 | 0.499 |
R-HSA-68867 | Assembly of the pre-replicative complex | 3.186687e-01 | 0.497 |
R-HSA-450604 | KSRP (KHSRP) binds and destabilizes mRNA | 3.197267e-01 | 0.495 |
R-HSA-5656121 | Translesion synthesis by POLI | 3.197267e-01 | 0.495 |
R-HSA-399955 | SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion | 3.197267e-01 | 0.495 |
R-HSA-9706369 | Negative regulation of FLT3 | 3.197267e-01 | 0.495 |
R-HSA-6803207 | TP53 Regulates Transcription of Caspase Activators and Caspases | 3.197267e-01 | 0.495 |
R-HSA-5339562 | Uptake and actions of bacterial toxins | 3.211794e-01 | 0.493 |
R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 3.231767e-01 | 0.491 |
R-HSA-445355 | Smooth Muscle Contraction | 3.281900e-01 | 0.484 |
R-HSA-168928 | DDX58/IFIH1-mediated induction of interferon-alpha/beta | 3.291235e-01 | 0.483 |
R-HSA-5655862 | Translesion synthesis by POLK | 3.327139e-01 | 0.478 |
R-HSA-9912633 | Antigen processing: Ub, ATP-independent proteasomal degradation | 3.327139e-01 | 0.478 |
R-HSA-9931521 | The CRY:PER:kinase complex represses transactivation by the BMAL:CLOCK (ARNTL:CL... | 3.327139e-01 | 0.478 |
R-HSA-918233 | TRAF3-dependent IRF activation pathway | 3.327139e-01 | 0.478 |
R-HSA-936964 | Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) | 3.327139e-01 | 0.478 |
R-HSA-3134975 | Regulation of innate immune responses to cytosolic DNA | 3.327139e-01 | 0.478 |
R-HSA-6787450 | tRNA modification in the mitochondrion | 3.327139e-01 | 0.478 |
R-HSA-9675151 | Disorders of Developmental Biology | 3.327139e-01 | 0.478 |
R-HSA-9018519 | Estrogen-dependent gene expression | 3.404804e-01 | 0.468 |
R-HSA-8878159 | Transcriptional regulation by RUNX3 | 3.447980e-01 | 0.462 |
R-HSA-5637812 | Signaling by EGFRvIII in Cancer | 3.454538e-01 | 0.462 |
R-HSA-5637810 | Constitutive Signaling by EGFRvIII | 3.454538e-01 | 0.462 |
R-HSA-2408550 | Metabolism of ingested H2SeO4 and H2SeO3 into H2Se | 3.454538e-01 | 0.462 |
R-HSA-6782210 | Gap-filling DNA repair synthesis and ligation in TC-NER | 3.490969e-01 | 0.457 |
R-HSA-193648 | NRAGE signals death through JNK | 3.490969e-01 | 0.457 |
R-HSA-6807070 | PTEN Regulation | 3.534794e-01 | 0.452 |
R-HSA-9614085 | FOXO-mediated transcription | 3.552316e-01 | 0.449 |
R-HSA-181429 | Serotonin Neurotransmitter Release Cycle | 3.579513e-01 | 0.446 |
R-HSA-164378 | PKA activation in glucagon signalling | 3.579513e-01 | 0.446 |
R-HSA-1606322 | ZBP1(DAI) mediated induction of type I IFNs | 3.579513e-01 | 0.446 |
R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 3.579513e-01 | 0.446 |
R-HSA-163615 | PKA activation | 3.579513e-01 | 0.446 |
R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 3.579513e-01 | 0.446 |
R-HSA-111471 | Apoptotic factor-mediated response | 3.579513e-01 | 0.446 |
R-HSA-6804760 | Regulation of TP53 Activity through Methylation | 3.579513e-01 | 0.446 |
R-HSA-6782135 | Dual incision in TC-NER | 3.629137e-01 | 0.440 |
R-HSA-429914 | Deadenylation-dependent mRNA decay | 3.697810e-01 | 0.432 |
R-HSA-110320 | Translesion Synthesis by POLH | 3.702109e-01 | 0.432 |
R-HSA-156587 | Amino Acid conjugation | 3.702109e-01 | 0.432 |
R-HSA-159424 | Conjugation of carboxylic acids | 3.702109e-01 | 0.432 |
R-HSA-429958 | mRNA decay by 3' to 5' exoribonuclease | 3.702109e-01 | 0.432 |
R-HSA-844456 | The NLRP3 inflammasome | 3.702109e-01 | 0.432 |
R-HSA-912631 | Regulation of signaling by CBL | 3.702109e-01 | 0.432 |
R-HSA-9856532 | Mechanical load activates signaling by PIEZO1 and integrins in osteocytes | 3.702109e-01 | 0.432 |
R-HSA-449836 | Other interleukin signaling | 3.702109e-01 | 0.432 |
R-HSA-2559580 | Oxidative Stress Induced Senescence | 3.708402e-01 | 0.431 |
R-HSA-379724 | tRNA Aminoacylation | 3.766189e-01 | 0.424 |
R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 3.766189e-01 | 0.424 |
R-HSA-2644602 | Signaling by NOTCH1 PEST Domain Mutants in Cancer | 3.766189e-01 | 0.424 |
R-HSA-2894858 | Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer | 3.766189e-01 | 0.424 |
R-HSA-2894862 | Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants | 3.766189e-01 | 0.424 |
R-HSA-2644606 | Constitutive Signaling by NOTCH1 PEST Domain Mutants | 3.766189e-01 | 0.424 |
R-HSA-2644603 | Signaling by NOTCH1 in Cancer | 3.766189e-01 | 0.424 |
R-HSA-389513 | Co-inhibition by CTLA4 | 3.822372e-01 | 0.418 |
R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 3.822372e-01 | 0.418 |
R-HSA-1181150 | Signaling by NODAL | 3.822372e-01 | 0.418 |
R-HSA-5620916 | VxPx cargo-targeting to cilium | 3.822372e-01 | 0.418 |
R-HSA-445144 | Signal transduction by L1 | 3.822372e-01 | 0.418 |
R-HSA-1482922 | Acyl chain remodelling of PI | 3.822372e-01 | 0.418 |
R-HSA-9629569 | Protein hydroxylation | 3.822372e-01 | 0.418 |
R-HSA-445717 | Aquaporin-mediated transport | 3.834262e-01 | 0.416 |
R-HSA-163125 | Post-translational modification: synthesis of GPI-anchored proteins | 3.863789e-01 | 0.413 |
R-HSA-453279 | Mitotic G1 phase and G1/S transition | 3.881131e-01 | 0.411 |
R-HSA-2559586 | DNA Damage/Telomere Stress Induced Senescence | 3.902014e-01 | 0.409 |
R-HSA-1660499 | Synthesis of PIPs at the plasma membrane | 3.902014e-01 | 0.409 |
R-HSA-72163 | mRNA Splicing - Major Pathway | 3.909132e-01 | 0.408 |
R-HSA-5637815 | Signaling by Ligand-Responsive EGFR Variants in Cancer | 3.940346e-01 | 0.404 |
R-HSA-1236382 | Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants | 3.940346e-01 | 0.404 |
R-HSA-264642 | Acetylcholine Neurotransmitter Release Cycle | 3.940346e-01 | 0.404 |
R-HSA-162594 | Early Phase of HIV Life Cycle | 3.940346e-01 | 0.404 |
R-HSA-111931 | PKA-mediated phosphorylation of CREB | 3.940346e-01 | 0.404 |
R-HSA-1482925 | Acyl chain remodelling of PG | 3.940346e-01 | 0.404 |
R-HSA-210991 | Basigin interactions | 3.940346e-01 | 0.404 |
R-HSA-69615 | G1/S DNA Damage Checkpoints | 3.969433e-01 | 0.401 |
R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 3.969433e-01 | 0.401 |
R-HSA-8848021 | Signaling by PTK6 | 3.969433e-01 | 0.401 |
R-HSA-2426168 | Activation of gene expression by SREBF (SREBP) | 3.969433e-01 | 0.401 |
R-HSA-1280218 | Adaptive Immune System | 4.011556e-01 | 0.397 |
R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 4.018264e-01 | 0.396 |
R-HSA-9700206 | Signaling by ALK in cancer | 4.018264e-01 | 0.396 |
R-HSA-438066 | Unblocking of NMDA receptors, glutamate binding and activation | 4.056074e-01 | 0.392 |
R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 4.056074e-01 | 0.392 |
R-HSA-442982 | Ras activation upon Ca2+ influx through NMDA receptor | 4.056074e-01 | 0.392 |
R-HSA-8876384 | Listeria monocytogenes entry into host cells | 4.056074e-01 | 0.392 |
R-HSA-9617324 | Negative regulation of NMDA receptor-mediated neuronal transmission | 4.056074e-01 | 0.392 |
R-HSA-2995383 | Initiation of Nuclear Envelope (NE) Reformation | 4.056074e-01 | 0.392 |
R-HSA-175474 | Assembly Of The HIV Virion | 4.056074e-01 | 0.392 |
R-HSA-1236975 | Antigen processing-Cross presentation | 4.069519e-01 | 0.390 |
R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 4.169578e-01 | 0.380 |
R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 4.169598e-01 | 0.380 |
R-HSA-6803529 | FGFR2 alternative splicing | 4.169598e-01 | 0.380 |
R-HSA-212676 | Dopamine Neurotransmitter Release Cycle | 4.169598e-01 | 0.380 |
R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 4.169598e-01 | 0.380 |
R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 4.169598e-01 | 0.380 |
R-HSA-1483249 | Inositol phosphate metabolism | 4.273172e-01 | 0.369 |
R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 4.280961e-01 | 0.368 |
R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 4.301140e-01 | 0.366 |
R-HSA-5218859 | Regulated Necrosis | 4.301140e-01 | 0.366 |
R-HSA-8936459 | RUNX1 regulates genes involved in megakaryocyte differentiation and platelet fun... | 4.301140e-01 | 0.366 |
R-HSA-72172 | mRNA Splicing | 4.323475e-01 | 0.364 |
R-HSA-9610379 | HCMV Late Events | 4.352814e-01 | 0.361 |
R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 4.366331e-01 | 0.360 |
R-HSA-9855142 | Cellular responses to mechanical stimuli | 4.374088e-01 | 0.359 |
R-HSA-181430 | Norepinephrine Neurotransmitter Release Cycle | 4.390204e-01 | 0.358 |
R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 4.390204e-01 | 0.358 |
R-HSA-429947 | Deadenylation of mRNA | 4.390204e-01 | 0.358 |
R-HSA-8963898 | Plasma lipoprotein assembly | 4.390204e-01 | 0.358 |
R-HSA-418592 | ADP signalling through P2Y purinoceptor 1 | 4.390204e-01 | 0.358 |
R-HSA-388841 | Regulation of T cell activation by CD28 family | 4.393072e-01 | 0.357 |
R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 4.431117e-01 | 0.353 |
R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 4.431117e-01 | 0.353 |
R-HSA-5628897 | TP53 Regulates Metabolic Genes | 4.474332e-01 | 0.349 |
R-HSA-9006936 | Signaling by TGFB family members | 4.479848e-01 | 0.349 |
R-HSA-8978934 | Metabolism of cofactors | 4.495490e-01 | 0.347 |
R-HSA-9620244 | Long-term potentiation | 4.497367e-01 | 0.347 |
R-HSA-5218921 | VEGFR2 mediated cell proliferation | 4.497367e-01 | 0.347 |
R-HSA-1482801 | Acyl chain remodelling of PS | 4.497367e-01 | 0.347 |
R-HSA-3214842 | HDMs demethylate histones | 4.497367e-01 | 0.347 |
R-HSA-5601884 | PIWI-interacting RNA (piRNA) biogenesis | 4.497367e-01 | 0.347 |
R-HSA-9932444 | ATP-dependent chromatin remodelers | 4.497367e-01 | 0.347 |
R-HSA-9932451 | SWI/SNF chromatin remodelers | 4.497367e-01 | 0.347 |
R-HSA-8874081 | MET activates PTK2 signaling | 4.602489e-01 | 0.337 |
R-HSA-1643713 | Signaling by EGFR in Cancer | 4.602489e-01 | 0.337 |
R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 4.602489e-01 | 0.337 |
R-HSA-210500 | Glutamate Neurotransmitter Release Cycle | 4.602489e-01 | 0.337 |
R-HSA-525793 | Myogenesis | 4.602489e-01 | 0.337 |
R-HSA-5357769 | Caspase activation via extrinsic apoptotic signalling pathway | 4.602489e-01 | 0.337 |
R-HSA-400042 | Adrenaline,noradrenaline inhibits insulin secretion | 4.602489e-01 | 0.337 |
R-HSA-70635 | Urea cycle | 4.602489e-01 | 0.337 |
R-HSA-9845614 | Sphingolipid catabolism | 4.602489e-01 | 0.337 |
R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 4.705609e-01 | 0.327 |
R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 4.705609e-01 | 0.327 |
R-HSA-201451 | Signaling by BMP | 4.705609e-01 | 0.327 |
R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 4.705609e-01 | 0.327 |
R-HSA-445095 | Interaction between L1 and Ankyrins | 4.705609e-01 | 0.327 |
R-HSA-3928663 | EPHA-mediated growth cone collapse | 4.705609e-01 | 0.327 |
R-HSA-5357956 | TNFR1-induced NF-kappa-B signaling pathway | 4.705609e-01 | 0.327 |
R-HSA-75109 | Triglyceride biosynthesis | 4.705609e-01 | 0.327 |
R-HSA-9006115 | Signaling by NTRK2 (TRKB) | 4.705609e-01 | 0.327 |
R-HSA-6803204 | TP53 Regulates Transcription of Genes Involved in Cytochrome C Release | 4.705609e-01 | 0.327 |
R-HSA-449147 | Signaling by Interleukins | 4.748002e-01 | 0.323 |
R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 4.748700e-01 | 0.323 |
R-HSA-167287 | HIV elongation arrest and recovery | 4.806766e-01 | 0.318 |
R-HSA-167290 | Pausing and recovery of HIV elongation | 4.806766e-01 | 0.318 |
R-HSA-5576892 | Phase 0 - rapid depolarisation | 4.806766e-01 | 0.318 |
R-HSA-5620971 | Pyroptosis | 4.806766e-01 | 0.318 |
R-HSA-622312 | Inflammasomes | 4.806766e-01 | 0.318 |
R-HSA-380994 | ATF4 activates genes in response to endoplasmic reticulum stress | 4.806766e-01 | 0.318 |
R-HSA-1980143 | Signaling by NOTCH1 | 4.810899e-01 | 0.318 |
R-HSA-917729 | Endosomal Sorting Complex Required For Transport (ESCRT) | 4.905995e-01 | 0.309 |
R-HSA-9006335 | Signaling by Erythropoietin | 4.905995e-01 | 0.309 |
R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 4.905995e-01 | 0.309 |
R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 4.905995e-01 | 0.309 |
R-HSA-9816359 | Maternal to zygotic transition (MZT) | 4.915952e-01 | 0.308 |
R-HSA-5619084 | ABC transporter disorders | 4.933928e-01 | 0.307 |
R-HSA-416482 | G alpha (12/13) signalling events | 4.933928e-01 | 0.307 |
R-HSA-5621481 | C-type lectin receptors (CLRs) | 4.978048e-01 | 0.303 |
R-HSA-9659379 | Sensory processing of sound | 4.994750e-01 | 0.301 |
R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 4.994750e-01 | 0.301 |
R-HSA-68962 | Activation of the pre-replicative complex | 5.003335e-01 | 0.301 |
R-HSA-76046 | RNA Polymerase III Transcription Initiation | 5.003335e-01 | 0.301 |
R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 5.003335e-01 | 0.301 |
R-HSA-112311 | Neurotransmitter clearance | 5.003335e-01 | 0.301 |
R-HSA-2424491 | DAP12 signaling | 5.003335e-01 | 0.301 |
R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 5.018729e-01 | 0.299 |
R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 5.055102e-01 | 0.296 |
R-HSA-9841922 | MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesi... | 5.059311e-01 | 0.296 |
R-HSA-9851695 | Epigenetic regulation of adipogenesis genes by MLL3 and MLL4 complexes | 5.059311e-01 | 0.296 |
R-HSA-9818564 | Epigenetic regulation of gene expression by MLL3 and MLL4 complexes | 5.059311e-01 | 0.296 |
R-HSA-9820960 | Respiratory syncytial virus (RSV) attachment and entry | 5.098821e-01 | 0.293 |
R-HSA-162588 | Budding and maturation of HIV virion | 5.098821e-01 | 0.293 |
R-HSA-211733 | Regulation of activated PAK-2p34 by proteasome mediated degradation | 5.098821e-01 | 0.293 |
R-HSA-399719 | Trafficking of AMPA receptors | 5.098821e-01 | 0.293 |
R-HSA-936440 | Negative regulators of DDX58/IFIH1 signaling | 5.098821e-01 | 0.293 |
R-HSA-182971 | EGFR downregulation | 5.098821e-01 | 0.293 |
R-HSA-8878171 | Transcriptional regulation by RUNX1 | 5.130289e-01 | 0.290 |
R-HSA-4791275 | Signaling by WNT in cancer | 5.192487e-01 | 0.285 |
R-HSA-350562 | Regulation of ornithine decarboxylase (ODC) | 5.192487e-01 | 0.285 |
R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 5.192487e-01 | 0.285 |
R-HSA-9824443 | Parasitic Infection Pathways | 5.220292e-01 | 0.282 |
R-HSA-9658195 | Leishmania infection | 5.220292e-01 | 0.282 |
R-HSA-442742 | CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling | 5.284369e-01 | 0.277 |
R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 5.284369e-01 | 0.277 |
R-HSA-399721 | Glutamate binding, activation of AMPA receptors and synaptic plasticity | 5.284369e-01 | 0.277 |
R-HSA-5675482 | Regulation of necroptotic cell death | 5.284369e-01 | 0.277 |
R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 5.284369e-01 | 0.277 |
R-HSA-168249 | Innate Immune System | 5.286238e-01 | 0.277 |
R-HSA-163359 | Glucagon signaling in metabolic regulation | 5.374501e-01 | 0.270 |
R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 5.374501e-01 | 0.270 |
R-HSA-1482788 | Acyl chain remodelling of PC | 5.374501e-01 | 0.270 |
R-HSA-180534 | Vpu mediated degradation of CD4 | 5.374501e-01 | 0.270 |
R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 5.407157e-01 | 0.267 |
R-HSA-3247509 | Chromatin modifying enzymes | 5.412254e-01 | 0.267 |
R-HSA-201681 | TCF dependent signaling in response to WNT | 5.456182e-01 | 0.263 |
R-HSA-9843970 | Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex | 5.462915e-01 | 0.263 |
R-HSA-203615 | eNOS activation | 5.462915e-01 | 0.263 |
R-HSA-75815 | Ubiquitin-dependent degradation of Cyclin D | 5.462915e-01 | 0.263 |
R-HSA-392518 | Signal amplification | 5.462915e-01 | 0.263 |
R-HSA-447115 | Interleukin-12 family signaling | 5.520602e-01 | 0.258 |
R-HSA-8854050 | FBXL7 down-regulates AURKA during mitotic entry and in early mitosis | 5.549645e-01 | 0.256 |
R-HSA-174113 | SCF-beta-TrCP mediated degradation of Emi1 | 5.549645e-01 | 0.256 |
R-HSA-1482839 | Acyl chain remodelling of PE | 5.549645e-01 | 0.256 |
R-HSA-169911 | Regulation of Apoptosis | 5.549645e-01 | 0.256 |
R-HSA-381042 | PERK regulates gene expression | 5.549645e-01 | 0.256 |
R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 5.549645e-01 | 0.256 |
R-HSA-212300 | PRC2 methylates histones and DNA | 5.634722e-01 | 0.249 |
R-HSA-74158 | RNA Polymerase III Transcription | 5.634722e-01 | 0.249 |
R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 5.634722e-01 | 0.249 |
R-HSA-180585 | Vif-mediated degradation of APOBEC3G | 5.634722e-01 | 0.249 |
R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 5.634722e-01 | 0.249 |
R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 5.679478e-01 | 0.246 |
R-HSA-202424 | Downstream TCR signaling | 5.687045e-01 | 0.245 |
R-HSA-73884 | Base Excision Repair | 5.687045e-01 | 0.245 |
R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 5.718178e-01 | 0.243 |
R-HSA-4641258 | Degradation of DVL | 5.718178e-01 | 0.243 |
R-HSA-4641257 | Degradation of AXIN | 5.718178e-01 | 0.243 |
R-HSA-9762114 | GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 | 5.718178e-01 | 0.243 |
R-HSA-933541 | TRAF6 mediated IRF7 activation | 5.718178e-01 | 0.243 |
R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 5.718178e-01 | 0.243 |
R-HSA-196757 | Metabolism of folate and pterines | 5.718178e-01 | 0.243 |
R-HSA-6785470 | tRNA processing in the mitochondrion | 5.800043e-01 | 0.237 |
R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 5.800043e-01 | 0.237 |
R-HSA-5213460 | RIPK1-mediated regulated necrosis | 5.800043e-01 | 0.237 |
R-HSA-9958790 | SLC-mediated transport of inorganic anions | 5.800043e-01 | 0.237 |
R-HSA-9664407 | Parasite infection | 5.829277e-01 | 0.234 |
R-HSA-9664422 | FCGR3A-mediated phagocytosis | 5.829277e-01 | 0.234 |
R-HSA-9664417 | Leishmania phagocytosis | 5.829277e-01 | 0.234 |
R-HSA-1236978 | Cross-presentation of soluble exogenous antigens (endosomes) | 5.880349e-01 | 0.231 |
R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 5.880349e-01 | 0.231 |
R-HSA-9929356 | GSK3B-mediated proteasomal degradation of PD-L1(CD274) | 5.880349e-01 | 0.231 |
R-HSA-9648002 | RAS processing | 5.880349e-01 | 0.231 |
R-HSA-8953750 | Transcriptional Regulation by E2F6 | 5.880349e-01 | 0.231 |
R-HSA-4839726 | Chromatin organization | 5.919343e-01 | 0.228 |
R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 5.959123e-01 | 0.225 |
R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 5.959123e-01 | 0.225 |
R-HSA-5696395 | Formation of Incision Complex in GG-NER | 5.959123e-01 | 0.225 |
R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 5.959123e-01 | 0.225 |
R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 5.959123e-01 | 0.225 |
R-HSA-167169 | HIV Transcription Elongation | 5.959123e-01 | 0.225 |
R-HSA-1251985 | Nuclear signaling by ERBB4 | 5.959123e-01 | 0.225 |
R-HSA-9604323 | Negative regulation of NOTCH4 signaling | 5.959123e-01 | 0.225 |
R-HSA-8868766 | rRNA processing in the mitochondrion | 5.959123e-01 | 0.225 |
R-HSA-8941858 | Regulation of RUNX3 expression and activity | 5.959123e-01 | 0.225 |
R-HSA-71240 | Tryptophan catabolism | 5.959123e-01 | 0.225 |
R-HSA-8856828 | Clathrin-mediated endocytosis | 5.999081e-01 | 0.222 |
R-HSA-5362768 | Hh mutants are degraded by ERAD | 6.036396e-01 | 0.219 |
R-HSA-5676590 | NIK-->noncanonical NF-kB signaling | 6.036396e-01 | 0.219 |
R-HSA-9821002 | Chromatin modifications during the maternal to zygotic transition (MZT) | 6.036396e-01 | 0.219 |
R-HSA-9607240 | FLT3 Signaling | 6.036396e-01 | 0.219 |
R-HSA-389948 | Co-inhibition by PD-1 | 6.090850e-01 | 0.215 |
R-HSA-5674135 | MAP2K and MAPK activation | 6.112196e-01 | 0.214 |
R-HSA-9932298 | Degradation of CRY and PER proteins | 6.112196e-01 | 0.214 |
R-HSA-5610780 | Degradation of GLI1 by the proteasome | 6.112196e-01 | 0.214 |
R-HSA-5610783 | Degradation of GLI2 by the proteasome | 6.112196e-01 | 0.214 |
R-HSA-5610785 | GLI3 is processed to GLI3R by the proteasome | 6.112196e-01 | 0.214 |
R-HSA-442660 | SLC-mediated transport of neurotransmitters | 6.112196e-01 | 0.214 |
R-HSA-5675221 | Negative regulation of MAPK pathway | 6.112196e-01 | 0.214 |
R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 6.159290e-01 | 0.210 |
R-HSA-991365 | Activation of GABAB receptors | 6.186551e-01 | 0.209 |
R-HSA-977444 | GABA B receptor activation | 6.186551e-01 | 0.209 |
R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 6.186551e-01 | 0.209 |
R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 6.186551e-01 | 0.209 |
R-HSA-166520 | Signaling by NTRKs | 6.204887e-01 | 0.207 |
R-HSA-9710421 | Defective pyroptosis | 6.259488e-01 | 0.203 |
R-HSA-5387390 | Hh mutants abrogate ligand secretion | 6.259488e-01 | 0.203 |
R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 6.259488e-01 | 0.203 |
R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 6.285175e-01 | 0.202 |
R-HSA-9679191 | Potential therapeutics for SARS | 6.285175e-01 | 0.202 |
R-HSA-9856651 | MITF-M-dependent gene expression | 6.285175e-01 | 0.202 |
R-HSA-382556 | ABC-family proteins mediated transport | 6.307663e-01 | 0.200 |
R-HSA-9907900 | Proteasome assembly | 6.331035e-01 | 0.199 |
R-HSA-187577 | SCF(Skp2)-mediated degradation of p27/p21 | 6.331035e-01 | 0.199 |
R-HSA-3214858 | RMTs methylate histone arginines | 6.331035e-01 | 0.199 |
R-HSA-2172127 | DAP12 interactions | 6.331035e-01 | 0.199 |
R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 6.401218e-01 | 0.194 |
R-HSA-774815 | Nucleosome assembly | 6.401218e-01 | 0.194 |
R-HSA-9660821 | ADORA2B mediated anti-inflammatory cytokines production | 6.401218e-01 | 0.194 |
R-HSA-4608870 | Asymmetric localization of PCP proteins | 6.401218e-01 | 0.194 |
R-HSA-6783310 | Fanconi Anemia Pathway | 6.401218e-01 | 0.194 |
R-HSA-5607761 | Dectin-1 mediated noncanonical NF-kB signaling | 6.401218e-01 | 0.194 |
R-HSA-69613 | p53-Independent G1/S DNA Damage Checkpoint | 6.401218e-01 | 0.194 |
R-HSA-69601 | Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A | 6.401218e-01 | 0.194 |
R-HSA-3560782 | Diseases associated with glycosaminoglycan metabolism | 6.401218e-01 | 0.194 |
R-HSA-9824272 | Somitogenesis | 6.401218e-01 | 0.194 |
R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 6.401218e-01 | 0.194 |
R-HSA-1483255 | PI Metabolism | 6.404081e-01 | 0.194 |
R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | 6.470062e-01 | 0.189 |
R-HSA-9664424 | Cell recruitment (pro-inflammatory response) | 6.470062e-01 | 0.189 |
R-HSA-5357905 | Regulation of TNFR1 signaling | 6.470062e-01 | 0.189 |
R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 6.498511e-01 | 0.187 |
R-HSA-9860931 | Response of endothelial cells to shear stress | 6.498511e-01 | 0.187 |
R-HSA-9833110 | RSV-host interactions | 6.544985e-01 | 0.184 |
R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 6.590967e-01 | 0.181 |
R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 6.594548e-01 | 0.181 |
R-HSA-9634597 | GPER1 signaling | 6.603837e-01 | 0.180 |
R-HSA-425410 | Metal ion SLC transporters | 6.603837e-01 | 0.180 |
R-HSA-8963899 | Plasma lipoprotein remodeling | 6.603837e-01 | 0.180 |
R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 6.616066e-01 | 0.179 |
R-HSA-418346 | Platelet homeostasis | 6.636458e-01 | 0.178 |
R-HSA-9748787 | Azathioprine ADME | 6.732558e-01 | 0.172 |
R-HSA-1169091 | Activation of NF-kappaB in B cells | 6.795084e-01 | 0.168 |
R-HSA-1234176 | Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha | 6.795084e-01 | 0.168 |
R-HSA-70895 | Branched-chain amino acid catabolism | 6.795084e-01 | 0.168 |
R-HSA-202403 | TCR signaling | 6.813561e-01 | 0.167 |
R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 6.813561e-01 | 0.167 |
R-HSA-166166 | MyD88-independent TLR4 cascade | 6.813561e-01 | 0.167 |
R-HSA-72187 | mRNA 3'-end processing | 6.856416e-01 | 0.164 |
R-HSA-112382 | Formation of RNA Pol II elongation complex | 6.856416e-01 | 0.164 |
R-HSA-68949 | Orc1 removal from chromatin | 6.856416e-01 | 0.164 |
R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 6.856416e-01 | 0.164 |
R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 6.856416e-01 | 0.164 |
R-HSA-2871796 | FCERI mediated MAPK activation | 6.899226e-01 | 0.161 |
R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 6.916578e-01 | 0.160 |
R-HSA-75955 | RNA Polymerase II Transcription Elongation | 6.916578e-01 | 0.160 |
R-HSA-9639288 | Amino acids regulate mTORC1 | 6.916578e-01 | 0.160 |
R-HSA-8948751 | Regulation of PTEN stability and activity | 6.916578e-01 | 0.160 |
R-HSA-3214815 | HDACs deacetylate histones | 7.033482e-01 | 0.153 |
R-HSA-75893 | TNF signaling | 7.090266e-01 | 0.149 |
R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 7.090266e-01 | 0.149 |
R-HSA-5578775 | Ion homeostasis | 7.090266e-01 | 0.149 |
R-HSA-177929 | Signaling by EGFR | 7.090266e-01 | 0.149 |
R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 7.105123e-01 | 0.148 |
R-HSA-1483166 | Synthesis of PA | 7.145967e-01 | 0.146 |
R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 7.145967e-01 | 0.146 |
R-HSA-2980736 | Peptide hormone metabolism | 7.184233e-01 | 0.144 |
R-HSA-9029569 | NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflu... | 7.200605e-01 | 0.143 |
R-HSA-352230 | Amino acid transport across the plasma membrane | 7.254200e-01 | 0.139 |
R-HSA-9033241 | Peroxisomal protein import | 7.254200e-01 | 0.139 |
R-HSA-8979227 | Triglyceride metabolism | 7.254200e-01 | 0.139 |
R-HSA-8939211 | ESR-mediated signaling | 7.297750e-01 | 0.137 |
R-HSA-977443 | GABA receptor activation | 7.306772e-01 | 0.136 |
R-HSA-8873719 | RAB geranylgeranylation | 7.306772e-01 | 0.136 |
R-HSA-156590 | Glutathione conjugation | 7.306772e-01 | 0.136 |
R-HSA-351202 | Metabolism of polyamines | 7.306772e-01 | 0.136 |
R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 7.337012e-01 | 0.134 |
R-HSA-73856 | RNA Polymerase II Transcription Termination | 7.358341e-01 | 0.133 |
R-HSA-8939902 | Regulation of RUNX2 expression and activity | 7.358341e-01 | 0.133 |
R-HSA-450294 | MAP kinase activation | 7.358341e-01 | 0.133 |
R-HSA-211976 | Endogenous sterols | 7.358341e-01 | 0.133 |
R-HSA-9793380 | Formation of paraxial mesoderm | 7.358341e-01 | 0.133 |
R-HSA-157118 | Signaling by NOTCH | 7.379992e-01 | 0.132 |
R-HSA-6799198 | Complex I biogenesis | 7.458545e-01 | 0.127 |
R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 7.507216e-01 | 0.125 |
R-HSA-936837 | Ion transport by P-type ATPases | 7.507216e-01 | 0.125 |
R-HSA-211981 | Xenobiotics | 7.507216e-01 | 0.125 |
R-HSA-69206 | G1/S Transition | 7.518040e-01 | 0.124 |
R-HSA-1234174 | Cellular response to hypoxia | 7.554959e-01 | 0.122 |
R-HSA-187037 | Signaling by NTRK1 (TRKA) | 7.621509e-01 | 0.118 |
R-HSA-9958863 | SLC-mediated transport of amino acids | 7.647727e-01 | 0.116 |
R-HSA-167172 | Transcription of the HIV genome | 7.692787e-01 | 0.114 |
R-HSA-1650814 | Collagen biosynthesis and modifying enzymes | 7.692787e-01 | 0.114 |
R-HSA-168898 | Toll-like Receptor Cascades | 7.700108e-01 | 0.114 |
R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 7.727666e-01 | 0.112 |
R-HSA-448424 | Interleukin-17 signaling | 7.780342e-01 | 0.109 |
R-HSA-204005 | COPII-mediated vesicle transport | 7.780342e-01 | 0.109 |
R-HSA-69202 | Cyclin E associated events during G1/S transition | 7.780342e-01 | 0.109 |
R-HSA-1474228 | Degradation of the extracellular matrix | 7.785670e-01 | 0.109 |
R-HSA-427413 | NoRC negatively regulates rRNA expression | 7.822870e-01 | 0.107 |
R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 7.822870e-01 | 0.107 |
R-HSA-5632684 | Hedgehog 'on' state | 7.822870e-01 | 0.107 |
R-HSA-69656 | Cyclin A:Cdk2-associated events at S phase entry | 7.864585e-01 | 0.104 |
R-HSA-4086398 | Ca2+ pathway | 7.905503e-01 | 0.102 |
R-HSA-9749641 | Aspirin ADME | 7.905503e-01 | 0.102 |
R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 7.945640e-01 | 0.100 |
R-HSA-1236394 | Signaling by ERBB4 | 7.945640e-01 | 0.100 |
R-HSA-9013694 | Signaling by NOTCH4 | 7.945640e-01 | 0.100 |
R-HSA-1222556 | ROS and RNS production in phagocytes | 7.945640e-01 | 0.100 |
R-HSA-5633008 | TP53 Regulates Transcription of Cell Death Genes | 7.985010e-01 | 0.098 |
R-HSA-9020591 | Interleukin-12 signaling | 8.023628e-01 | 0.096 |
R-HSA-9024446 | NR1H2 and NR1H3-mediated signaling | 8.061509e-01 | 0.094 |
R-HSA-383280 | Nuclear Receptor transcription pathway | 8.098665e-01 | 0.092 |
R-HSA-216083 | Integrin cell surface interactions | 8.098665e-01 | 0.092 |
R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 8.170862e-01 | 0.088 |
R-HSA-5654738 | Signaling by FGFR2 | 8.170862e-01 | 0.088 |
R-HSA-2871837 | FCERI mediated NF-kB activation | 8.193638e-01 | 0.087 |
R-HSA-397014 | Muscle contraction | 8.246357e-01 | 0.084 |
R-HSA-2187338 | Visual phototransduction | 8.271815e-01 | 0.082 |
R-HSA-5668541 | TNFR2 non-canonical NF-kB pathway | 8.274065e-01 | 0.082 |
R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 8.297192e-01 | 0.081 |
R-HSA-8939236 | RUNX1 regulates transcription of genes involved in differentiation of HSCs | 8.307160e-01 | 0.081 |
R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 8.339904e-01 | 0.079 |
R-HSA-9755511 | KEAP1-NFE2L2 pathway | 8.371324e-01 | 0.077 |
R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 8.395381e-01 | 0.076 |
R-HSA-381038 | XBP1(S) activates chaperone genes | 8.402696e-01 | 0.076 |
R-HSA-163841 | Gamma carboxylation, hypusinylation, hydroxylation, and arylsulfatase activation | 8.402696e-01 | 0.076 |
R-HSA-8951664 | Neddylation | 8.435795e-01 | 0.074 |
R-HSA-112310 | Neurotransmitter release cycle | 8.521769e-01 | 0.069 |
R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 8.550127e-01 | 0.068 |
R-HSA-381070 | IRE1alpha activates chaperones | 8.577944e-01 | 0.067 |
R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 8.605229e-01 | 0.065 |
R-HSA-9006931 | Signaling by Nuclear Receptors | 8.615359e-01 | 0.065 |
R-HSA-9837999 | Mitochondrial protein degradation | 8.658242e-01 | 0.063 |
R-HSA-1474290 | Collagen formation | 8.658242e-01 | 0.063 |
R-HSA-77289 | Mitochondrial Fatty Acid Beta-Oxidation | 8.683991e-01 | 0.061 |
R-HSA-1296071 | Potassium Channels | 8.734020e-01 | 0.059 |
R-HSA-422356 | Regulation of insulin secretion | 8.782153e-01 | 0.056 |
R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 8.782153e-01 | 0.056 |
R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 8.782153e-01 | 0.056 |
R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 8.782153e-01 | 0.056 |
R-HSA-190236 | Signaling by FGFR | 8.782153e-01 | 0.056 |
R-HSA-9009391 | Extra-nuclear estrogen signaling | 8.850954e-01 | 0.053 |
R-HSA-9020702 | Interleukin-1 signaling | 8.850954e-01 | 0.053 |
R-HSA-9842860 | Regulation of endogenous retroelements | 8.873015e-01 | 0.052 |
R-HSA-9937383 | Mitochondrial ribosome-associated quality control | 8.894655e-01 | 0.051 |
R-HSA-9824439 | Bacterial Infection Pathways | 8.982301e-01 | 0.047 |
R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 9.016064e-01 | 0.045 |
R-HSA-2672351 | Stimuli-sensing channels | 9.016064e-01 | 0.045 |
R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 9.034964e-01 | 0.044 |
R-HSA-983712 | Ion channel transport | 9.101497e-01 | 0.041 |
R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 9.107017e-01 | 0.041 |
R-HSA-1912422 | Pre-NOTCH Expression and Processing | 9.107017e-01 | 0.041 |
R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 9.157514e-01 | 0.038 |
R-HSA-2029485 | Role of phospholipids in phagocytosis | 9.173705e-01 | 0.037 |
R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 9.235428e-01 | 0.035 |
R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 9.235428e-01 | 0.035 |
R-HSA-8878166 | Transcriptional regulation by RUNX2 | 9.235428e-01 | 0.035 |
R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 9.264544e-01 | 0.033 |
R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 9.278685e-01 | 0.033 |
R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 9.278685e-01 | 0.033 |
R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.345425e-01 | 0.029 |
R-HSA-5576891 | Cardiac conduction | 9.417437e-01 | 0.026 |
R-HSA-1483257 | Phospholipid metabolism | 9.425294e-01 | 0.026 |
R-HSA-9748784 | Drug ADME | 9.441010e-01 | 0.025 |
R-HSA-163685 | Integration of energy metabolism | 9.481550e-01 | 0.023 |
R-HSA-5368287 | Mitochondrial translation | 9.501317e-01 | 0.022 |
R-HSA-156580 | Phase II - Conjugation of compounds | 9.601888e-01 | 0.018 |
R-HSA-9758941 | Gastrulation | 9.605103e-01 | 0.017 |
R-HSA-425407 | SLC-mediated transmembrane transport | 9.607598e-01 | 0.017 |
R-HSA-2142753 | Arachidonate metabolism | 9.627491e-01 | 0.016 |
R-HSA-9609507 | Protein localization | 9.634669e-01 | 0.016 |
R-HSA-418594 | G alpha (i) signalling events | 9.656906e-01 | 0.015 |
R-HSA-1474244 | Extracellular matrix organization | 9.658124e-01 | 0.015 |
R-HSA-211897 | Cytochrome P450 - arranged by substrate type | 9.721818e-01 | 0.012 |
R-HSA-9734767 | Developmental Cell Lineages | 9.731561e-01 | 0.012 |
R-HSA-416476 | G alpha (q) signalling events | 9.735968e-01 | 0.012 |
R-HSA-418555 | G alpha (s) signalling events | 9.747632e-01 | 0.011 |
R-HSA-9664433 | Leishmania parasite growth and survival | 9.757277e-01 | 0.011 |
R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 9.757277e-01 | 0.011 |
R-HSA-611105 | Respiratory electron transport | 9.779810e-01 | 0.010 |
R-HSA-196854 | Metabolism of vitamins and cofactors | 9.790761e-01 | 0.009 |
R-HSA-211945 | Phase I - Functionalization of compounds | 9.790800e-01 | 0.009 |
R-HSA-3781865 | Diseases of glycosylation | 9.804114e-01 | 0.009 |
R-HSA-1630316 | Glycosaminoglycan metabolism | 9.835648e-01 | 0.007 |
R-HSA-428157 | Sphingolipid metabolism | 9.859402e-01 | 0.006 |
R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.864785e-01 | 0.006 |
R-HSA-382551 | Transport of small molecules | 9.865566e-01 | 0.006 |
R-HSA-8957322 | Metabolism of steroids | 9.903833e-01 | 0.004 |
R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.921757e-01 | 0.003 |
R-HSA-202733 | Cell surface interactions at the vascular wall | 9.931768e-01 | 0.003 |
R-HSA-211859 | Biological oxidations | 9.933742e-01 | 0.003 |
R-HSA-388396 | GPCR downstream signalling | 9.946062e-01 | 0.002 |
R-HSA-8978868 | Fatty acid metabolism | 9.977647e-01 | 0.001 |
R-HSA-372790 | Signaling by GPCR | 9.982117e-01 | 0.001 |
R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.991139e-01 | 0.000 |
R-HSA-5668914 | Diseases of metabolism | 9.998410e-01 | 0.000 |
R-HSA-556833 | Metabolism of lipids | 9.999777e-01 | 0.000 |
R-HSA-1430728 | Metabolism | 9.999894e-01 | 0.000 |
R-HSA-9709957 | Sensory Perception | 1.000000e+00 | 0.000 |
Download
kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
---|---|---|---|---|
GAK |
0.889 | 0.045 | 1 | 0.824 |
TAK1 |
0.882 | -0.001 | 1 | 0.823 |
PKR |
0.882 | 0.078 | 1 | 0.845 |
ALPHAK3 |
0.879 | 0.124 | -1 | 0.839 |
TTK |
0.879 | 0.123 | -2 | 0.896 |
ALK2 |
0.877 | 0.309 | -2 | 0.893 |
BRAF |
0.877 | 0.053 | -4 | 0.850 |
BMPR1B |
0.876 | 0.372 | 1 | 0.892 |
ALK4 |
0.874 | 0.170 | -2 | 0.903 |
VRK2 |
0.874 | -0.301 | 1 | 0.870 |
GCK |
0.873 | -0.016 | 1 | 0.792 |
EEF2K |
0.873 | 0.021 | 3 | 0.810 |
BMPR2 |
0.872 | 0.032 | -2 | 0.922 |
TNIK |
0.872 | -0.006 | 3 | 0.823 |
MST2 |
0.872 | -0.022 | 1 | 0.802 |
MINK |
0.871 | -0.064 | 1 | 0.775 |
MOS |
0.871 | 0.256 | 1 | 0.924 |
TGFBR1 |
0.869 | 0.235 | -2 | 0.883 |
ACVR2B |
0.869 | 0.286 | -2 | 0.898 |
MST1 |
0.869 | -0.066 | 1 | 0.778 |
MEK1 |
0.868 | -0.150 | 2 | 0.806 |
BMPR1A |
0.868 | 0.352 | 1 | 0.884 |
MEKK2 |
0.867 | -0.091 | 2 | 0.768 |
VRK1 |
0.867 | -0.262 | 2 | 0.780 |
LRRK2 |
0.867 | -0.219 | 2 | 0.820 |
ASK1 |
0.865 | -0.206 | 1 | 0.744 |
TAO3 |
0.865 | -0.009 | 1 | 0.785 |
NEK1 |
0.865 | -0.155 | 1 | 0.780 |
ACVR2A |
0.864 | 0.241 | -2 | 0.888 |
OSR1 |
0.864 | -0.039 | 2 | 0.766 |
CAMKK1 |
0.864 | -0.104 | -2 | 0.788 |
TAO2 |
0.864 | -0.121 | 2 | 0.831 |
NEK5 |
0.864 | -0.110 | 1 | 0.806 |
HGK |
0.863 | -0.084 | 3 | 0.825 |
NIK |
0.863 | -0.130 | -3 | 0.859 |
PRPK |
0.862 | -0.059 | -1 | 0.909 |
PASK |
0.862 | 0.059 | -3 | 0.816 |
DLK |
0.862 | -0.090 | 1 | 0.843 |
ANKRD3 |
0.862 | -0.068 | 1 | 0.844 |
MEK5 |
0.862 | -0.304 | 2 | 0.790 |
MYO3A |
0.861 | -0.075 | 1 | 0.779 |
KHS2 |
0.861 | -0.026 | 1 | 0.773 |
MST3 |
0.861 | -0.018 | 2 | 0.812 |
CAMKK2 |
0.861 | -0.137 | -2 | 0.771 |
DAPK2 |
0.860 | -0.100 | -3 | 0.840 |
LATS1 |
0.860 | 0.100 | -3 | 0.808 |
MEKK1 |
0.860 | -0.123 | 1 | 0.803 |
KHS1 |
0.860 | -0.087 | 1 | 0.760 |
LKB1 |
0.859 | -0.134 | -3 | 0.829 |
BIKE |
0.859 | -0.045 | 1 | 0.684 |
MEKK3 |
0.859 | -0.087 | 1 | 0.797 |
GRK7 |
0.858 | 0.220 | 1 | 0.794 |
HPK1 |
0.858 | -0.097 | 1 | 0.772 |
MAP3K15 |
0.858 | -0.198 | 1 | 0.751 |
NEK8 |
0.858 | -0.143 | 2 | 0.785 |
PDK1 |
0.857 | -0.208 | 1 | 0.779 |
CAMLCK |
0.857 | -0.101 | -2 | 0.826 |
MYO3B |
0.856 | -0.106 | 2 | 0.798 |
YSK4 |
0.854 | -0.107 | 1 | 0.763 |
GRK6 |
0.854 | 0.148 | 1 | 0.884 |
ZAK |
0.854 | -0.111 | 1 | 0.783 |
NEK4 |
0.854 | -0.188 | 1 | 0.766 |
MPSK1 |
0.854 | -0.023 | 1 | 0.772 |
NEK11 |
0.853 | -0.224 | 1 | 0.781 |
PLK1 |
0.853 | 0.097 | -2 | 0.890 |
STLK3 |
0.853 | -0.233 | 1 | 0.745 |
YSK1 |
0.853 | -0.137 | 2 | 0.787 |
CAMK1B |
0.852 | -0.087 | -3 | 0.834 |
MEK2 |
0.852 | -0.284 | 2 | 0.769 |
ATR |
0.852 | -0.061 | 1 | 0.810 |
COT |
0.852 | 0.265 | 2 | 0.845 |
CAMK2G |
0.851 | 0.098 | 2 | 0.836 |
NLK |
0.851 | -0.031 | 1 | 0.820 |
CDKL1 |
0.850 | -0.030 | -3 | 0.762 |
PERK |
0.850 | -0.057 | -2 | 0.905 |
JNK3 |
0.850 | 0.043 | 1 | 0.647 |
MEKK6 |
0.850 | -0.256 | 1 | 0.779 |
PRP4 |
0.850 | 0.002 | -3 | 0.764 |
JNK2 |
0.849 | 0.057 | 1 | 0.608 |
RAF1 |
0.849 | -0.061 | 1 | 0.844 |
DAPK3 |
0.848 | -0.049 | -3 | 0.743 |
DSTYK |
0.847 | 0.181 | 2 | 0.876 |
TLK2 |
0.847 | 0.001 | 1 | 0.800 |
GRK5 |
0.847 | 0.011 | -3 | 0.874 |
MLK1 |
0.846 | -0.038 | 2 | 0.791 |
SMMLCK |
0.846 | -0.113 | -3 | 0.779 |
CLK3 |
0.845 | 0.254 | 1 | 0.854 |
DMPK1 |
0.844 | -0.029 | -3 | 0.697 |
AAK1 |
0.844 | -0.011 | 1 | 0.570 |
HRI |
0.844 | -0.138 | -2 | 0.906 |
PBK |
0.844 | -0.130 | 1 | 0.729 |
CDC7 |
0.843 | 0.214 | 1 | 0.921 |
ICK |
0.842 | -0.063 | -3 | 0.796 |
SKMLCK |
0.842 | -0.035 | -2 | 0.818 |
LOK |
0.842 | -0.144 | -2 | 0.755 |
P38A |
0.842 | -0.004 | 1 | 0.685 |
MLK2 |
0.842 | -0.200 | 2 | 0.788 |
TLK1 |
0.841 | -0.065 | -2 | 0.905 |
ERK5 |
0.841 | 0.002 | 1 | 0.785 |
P38B |
0.841 | 0.031 | 1 | 0.620 |
NEK9 |
0.840 | -0.151 | 2 | 0.807 |
GRK2 |
0.840 | 0.053 | -2 | 0.789 |
GRK1 |
0.839 | 0.243 | -2 | 0.839 |
PLK3 |
0.839 | 0.055 | 2 | 0.764 |
ROCK2 |
0.838 | -0.054 | -3 | 0.724 |
MLK4 |
0.838 | -0.000 | 2 | 0.698 |
PDHK4 |
0.837 | -0.271 | 1 | 0.846 |
CHAK2 |
0.837 | -0.027 | -1 | 0.904 |
MLK3 |
0.836 | 0.017 | 2 | 0.731 |
SLK |
0.836 | -0.096 | -2 | 0.719 |
DAPK1 |
0.835 | -0.071 | -3 | 0.729 |
PIM3 |
0.834 | 0.033 | -3 | 0.784 |
CDK1 |
0.834 | 0.104 | 1 | 0.636 |
PIM1 |
0.834 | 0.036 | -3 | 0.717 |
TAO1 |
0.834 | -0.182 | 1 | 0.707 |
PINK1 |
0.833 | -0.130 | 1 | 0.828 |
PLK2 |
0.833 | 0.109 | -3 | 0.841 |
NEK7 |
0.833 | 0.004 | -3 | 0.874 |
RIPK3 |
0.833 | -0.094 | 3 | 0.750 |
MST4 |
0.832 | 0.037 | 2 | 0.851 |
PKN3 |
0.832 | -0.082 | -3 | 0.784 |
PDHK1 |
0.831 | -0.284 | 1 | 0.830 |
PKCD |
0.831 | 0.010 | 2 | 0.773 |
RIPK1 |
0.831 | -0.255 | 1 | 0.807 |
MASTL |
0.831 | -0.389 | -2 | 0.824 |
ERK2 |
0.831 | -0.026 | 1 | 0.651 |
TGFBR2 |
0.830 | 0.059 | -2 | 0.884 |
JNK1 |
0.830 | 0.025 | 1 | 0.603 |
NEK2 |
0.830 | -0.172 | 2 | 0.783 |
WNK1 |
0.830 | -0.097 | -2 | 0.831 |
ATM |
0.830 | 0.004 | 1 | 0.754 |
P38G |
0.830 | 0.022 | 1 | 0.540 |
NEK6 |
0.829 | 0.082 | -2 | 0.906 |
TSSK2 |
0.829 | -0.105 | -5 | 0.833 |
MTOR |
0.829 | -0.059 | 1 | 0.764 |
DNAPK |
0.829 | -0.002 | 1 | 0.645 |
CDK5 |
0.829 | 0.050 | 1 | 0.685 |
IRAK4 |
0.829 | -0.179 | 1 | 0.788 |
WNK4 |
0.828 | -0.256 | -2 | 0.823 |
HASPIN |
0.827 | -0.068 | -1 | 0.719 |
DRAK1 |
0.827 | -0.078 | 1 | 0.783 |
GSK3A |
0.827 | 0.065 | 4 | 0.475 |
GSK3B |
0.827 | 0.013 | 4 | 0.464 |
HIPK1 |
0.826 | -0.008 | 1 | 0.719 |
GRK4 |
0.826 | 0.028 | -2 | 0.888 |
ULK2 |
0.825 | -0.125 | 2 | 0.747 |
P70S6KB |
0.824 | -0.057 | -3 | 0.743 |
PKN2 |
0.824 | -0.084 | -3 | 0.798 |
BUB1 |
0.824 | -0.034 | -5 | 0.789 |
CDK2 |
0.823 | 0.061 | 1 | 0.716 |
P38D |
0.823 | 0.024 | 1 | 0.542 |
AMPKA1 |
0.823 | -0.127 | -3 | 0.803 |
ERK1 |
0.823 | 0.004 | 1 | 0.603 |
HUNK |
0.822 | -0.203 | 2 | 0.763 |
CAMK2B |
0.822 | 0.095 | 2 | 0.825 |
PIM2 |
0.822 | -0.048 | -3 | 0.686 |
CDKL5 |
0.822 | -0.050 | -3 | 0.747 |
NEK3 |
0.822 | -0.269 | 1 | 0.732 |
NUAK2 |
0.821 | -0.101 | -3 | 0.793 |
ERK7 |
0.821 | -0.009 | 2 | 0.533 |
TBK1 |
0.821 | -0.155 | 1 | 0.717 |
TTBK2 |
0.821 | -0.141 | 2 | 0.672 |
ROCK1 |
0.821 | -0.092 | -3 | 0.686 |
MRCKA |
0.820 | -0.059 | -3 | 0.689 |
CK2A2 |
0.820 | 0.230 | 1 | 0.800 |
CHK1 |
0.819 | -0.144 | -3 | 0.764 |
CHAK1 |
0.819 | -0.193 | 2 | 0.714 |
IKKB |
0.819 | -0.025 | -2 | 0.805 |
DCAMKL1 |
0.819 | -0.134 | -3 | 0.718 |
MAK |
0.819 | 0.014 | -2 | 0.696 |
CAMK2D |
0.819 | -0.069 | -3 | 0.794 |
MARK4 |
0.818 | -0.110 | 4 | 0.811 |
DYRK2 |
0.818 | -0.022 | 1 | 0.707 |
CDK3 |
0.817 | 0.118 | 1 | 0.567 |
IKKA |
0.817 | 0.093 | -2 | 0.805 |
SMG1 |
0.816 | -0.138 | 1 | 0.746 |
IRE1 |
0.816 | -0.140 | 1 | 0.793 |
IKKE |
0.816 | -0.140 | 1 | 0.717 |
MRCKB |
0.816 | -0.077 | -3 | 0.678 |
CLK4 |
0.816 | -0.008 | -3 | 0.712 |
IRE2 |
0.816 | -0.122 | 2 | 0.707 |
SRPK3 |
0.815 | -0.017 | -3 | 0.679 |
WNK3 |
0.815 | -0.339 | 1 | 0.798 |
RSK2 |
0.815 | 0.008 | -3 | 0.712 |
GRK3 |
0.815 | 0.054 | -2 | 0.752 |
IRAK1 |
0.814 | -0.322 | -1 | 0.795 |
PDHK3_TYR |
0.814 | 0.284 | 4 | 0.909 |
MYLK4 |
0.814 | -0.104 | -2 | 0.730 |
DCAMKL2 |
0.814 | -0.155 | -3 | 0.752 |
CRIK |
0.814 | -0.082 | -3 | 0.629 |
MOK |
0.814 | -0.026 | 1 | 0.730 |
CDK14 |
0.813 | -0.013 | 1 | 0.635 |
SRPK1 |
0.813 | 0.019 | -3 | 0.698 |
TSSK1 |
0.813 | -0.130 | -3 | 0.819 |
CAMK2A |
0.813 | 0.042 | 2 | 0.835 |
PKCA |
0.813 | -0.042 | 2 | 0.718 |
FAM20C |
0.812 | 0.264 | 2 | 0.687 |
CDK16 |
0.812 | 0.055 | 1 | 0.562 |
CDK17 |
0.811 | 0.021 | 1 | 0.546 |
CDK6 |
0.811 | -0.018 | 1 | 0.607 |
CK2A1 |
0.811 | 0.194 | 1 | 0.776 |
HIPK4 |
0.811 | -0.037 | 1 | 0.801 |
ULK1 |
0.811 | -0.144 | -3 | 0.849 |
GCN2 |
0.811 | -0.097 | 2 | 0.778 |
SGK3 |
0.810 | -0.097 | -3 | 0.699 |
PKCH |
0.810 | -0.105 | 2 | 0.702 |
HIPK3 |
0.809 | -0.088 | 1 | 0.702 |
PAK1 |
0.809 | -0.108 | -2 | 0.734 |
NDR1 |
0.809 | -0.063 | -3 | 0.782 |
PKCB |
0.808 | -0.034 | 2 | 0.725 |
PKCZ |
0.808 | -0.122 | 2 | 0.748 |
STK33 |
0.808 | -0.173 | 2 | 0.588 |
DYRK1A |
0.808 | -0.080 | 1 | 0.729 |
AKT2 |
0.808 | -0.071 | -3 | 0.623 |
PAK2 |
0.808 | -0.186 | -2 | 0.725 |
P90RSK |
0.807 | -0.074 | -3 | 0.718 |
CDK8 |
0.807 | -0.014 | 1 | 0.663 |
AMPKA2 |
0.807 | -0.140 | -3 | 0.762 |
PLK4 |
0.807 | -0.126 | 2 | 0.590 |
BMPR2_TYR |
0.806 | 0.128 | -1 | 0.926 |
CDK18 |
0.806 | 0.028 | 1 | 0.593 |
DYRK1B |
0.806 | -0.032 | 1 | 0.657 |
PDHK4_TYR |
0.806 | 0.148 | 2 | 0.859 |
MAP2K6_TYR |
0.805 | 0.113 | -1 | 0.927 |
RSK4 |
0.805 | 0.018 | -3 | 0.677 |
CDK4 |
0.805 | -0.044 | 1 | 0.597 |
CDK13 |
0.805 | -0.044 | 1 | 0.637 |
RIPK2 |
0.805 | -0.355 | 1 | 0.732 |
PKCG |
0.804 | -0.066 | 2 | 0.720 |
CAMK4 |
0.804 | -0.238 | -3 | 0.769 |
PDHK1_TYR |
0.803 | 0.081 | -1 | 0.939 |
CLK1 |
0.803 | -0.001 | -3 | 0.688 |
MAP2K4_TYR |
0.802 | 0.001 | -1 | 0.922 |
EPHA6 |
0.802 | 0.139 | -1 | 0.911 |
LATS2 |
0.802 | 0.001 | -5 | 0.784 |
SGK1 |
0.802 | -0.068 | -3 | 0.530 |
BCKDK |
0.801 | -0.182 | -1 | 0.862 |
NDR2 |
0.801 | 0.022 | -3 | 0.791 |
CK1D |
0.801 | -0.000 | -3 | 0.519 |
NIM1 |
0.801 | -0.172 | 3 | 0.742 |
AURB |
0.801 | -0.066 | -2 | 0.602 |
CLK2 |
0.801 | 0.097 | -3 | 0.683 |
MARK2 |
0.801 | -0.131 | 4 | 0.705 |
MSK1 |
0.800 | -0.053 | -3 | 0.685 |
MELK |
0.800 | -0.204 | -3 | 0.744 |
TESK1_TYR |
0.800 | -0.088 | 3 | 0.848 |
DYRK3 |
0.800 | -0.070 | 1 | 0.727 |
CAMK1G |
0.800 | -0.134 | -3 | 0.705 |
QIK |
0.799 | -0.232 | -3 | 0.801 |
CAMK1D |
0.799 | -0.124 | -3 | 0.606 |
HIPK2 |
0.799 | 0.008 | 1 | 0.616 |
DYRK4 |
0.799 | -0.006 | 1 | 0.629 |
CDK12 |
0.799 | -0.055 | 1 | 0.609 |
PAK3 |
0.799 | -0.188 | -2 | 0.735 |
PRKD1 |
0.799 | -0.057 | -3 | 0.765 |
CDK7 |
0.798 | -0.054 | 1 | 0.668 |
PKMYT1_TYR |
0.798 | -0.097 | 3 | 0.828 |
MAPKAPK3 |
0.798 | -0.156 | -3 | 0.703 |
PKCE |
0.798 | -0.057 | 2 | 0.704 |
CHK2 |
0.798 | -0.146 | -3 | 0.559 |
SSTK |
0.798 | -0.145 | 4 | 0.773 |
PKACG |
0.797 | -0.087 | -2 | 0.694 |
AKT1 |
0.797 | -0.078 | -3 | 0.635 |
MAP2K7_TYR |
0.797 | -0.221 | 2 | 0.836 |
PRKD3 |
0.797 | -0.119 | -3 | 0.689 |
RSK3 |
0.797 | -0.081 | -3 | 0.711 |
MARK1 |
0.797 | -0.149 | 4 | 0.762 |
AURA |
0.796 | -0.064 | -2 | 0.582 |
MSK2 |
0.796 | -0.108 | -3 | 0.681 |
EPHA4 |
0.796 | 0.123 | 2 | 0.767 |
QSK |
0.795 | -0.124 | 4 | 0.784 |
MARK3 |
0.795 | -0.100 | 4 | 0.739 |
TXK |
0.795 | 0.182 | 1 | 0.876 |
TTBK1 |
0.795 | -0.178 | 2 | 0.592 |
EPHB4 |
0.794 | 0.053 | -1 | 0.888 |
PKCI |
0.794 | -0.128 | 2 | 0.719 |
CDK10 |
0.794 | -0.003 | 1 | 0.622 |
PINK1_TYR |
0.794 | -0.195 | 1 | 0.839 |
CDK9 |
0.793 | -0.085 | 1 | 0.640 |
CK1A2 |
0.793 | -0.023 | -3 | 0.514 |
SRPK2 |
0.792 | 0.004 | -3 | 0.610 |
YANK3 |
0.792 | -0.078 | 2 | 0.394 |
PKCT |
0.792 | -0.135 | 2 | 0.711 |
MNK1 |
0.792 | -0.092 | -2 | 0.755 |
PRKD2 |
0.792 | -0.034 | -3 | 0.696 |
MAPKAPK2 |
0.792 | -0.030 | -3 | 0.648 |
SRMS |
0.791 | 0.100 | 1 | 0.888 |
PKACB |
0.791 | -0.013 | -2 | 0.619 |
FER |
0.791 | 0.019 | 1 | 0.891 |
CK1E |
0.790 | -0.007 | -3 | 0.569 |
NUAK1 |
0.789 | -0.134 | -3 | 0.733 |
PKG2 |
0.789 | -0.103 | -2 | 0.619 |
AURC |
0.789 | -0.022 | -2 | 0.601 |
CDK19 |
0.788 | -0.028 | 1 | 0.620 |
INSRR |
0.788 | 0.013 | 3 | 0.748 |
MNK2 |
0.788 | -0.115 | -2 | 0.737 |
LIMK2_TYR |
0.788 | -0.140 | -3 | 0.869 |
P70S6K |
0.788 | -0.131 | -3 | 0.646 |
EPHB2 |
0.787 | 0.088 | -1 | 0.871 |
YES1 |
0.786 | -0.013 | -1 | 0.878 |
EPHB1 |
0.786 | 0.032 | 1 | 0.878 |
MST1R |
0.786 | -0.171 | 3 | 0.796 |
RET |
0.786 | -0.210 | 1 | 0.787 |
CSF1R |
0.786 | -0.090 | 3 | 0.778 |
YANK2 |
0.786 | -0.090 | 2 | 0.411 |
BLK |
0.785 | 0.110 | -1 | 0.872 |
KIS |
0.785 | 0.075 | 1 | 0.686 |
ABL2 |
0.785 | -0.031 | -1 | 0.863 |
TYRO3 |
0.785 | -0.157 | 3 | 0.776 |
TYK2 |
0.785 | -0.226 | 1 | 0.785 |
SIK |
0.785 | -0.137 | -3 | 0.704 |
FGR |
0.784 | -0.097 | 1 | 0.837 |
LCK |
0.784 | 0.049 | -1 | 0.868 |
HCK |
0.783 | -0.023 | -1 | 0.864 |
SBK |
0.783 | -0.103 | -3 | 0.484 |
EPHB3 |
0.783 | 0.015 | -1 | 0.870 |
ROS1 |
0.783 | -0.164 | 3 | 0.746 |
KIT |
0.783 | -0.061 | 3 | 0.789 |
LIMK1_TYR |
0.783 | -0.286 | 2 | 0.824 |
EPHA7 |
0.783 | 0.061 | 2 | 0.763 |
JAK2 |
0.782 | -0.199 | 1 | 0.778 |
DDR1 |
0.782 | -0.208 | 4 | 0.818 |
FGFR2 |
0.781 | -0.103 | 3 | 0.799 |
ITK |
0.781 | -0.025 | -1 | 0.842 |
PHKG1 |
0.781 | -0.206 | -3 | 0.766 |
FYN |
0.780 | 0.089 | -1 | 0.847 |
CAMK1A |
0.780 | -0.148 | -3 | 0.583 |
JAK3 |
0.780 | -0.135 | 1 | 0.772 |
TEC |
0.779 | 0.009 | -1 | 0.782 |
ABL1 |
0.779 | -0.077 | -1 | 0.855 |
EPHA5 |
0.779 | 0.094 | 2 | 0.754 |
BMX |
0.779 | 0.013 | -1 | 0.780 |
KDR |
0.778 | -0.104 | 3 | 0.753 |
FLT3 |
0.778 | -0.138 | 3 | 0.762 |
MET |
0.778 | -0.056 | 3 | 0.771 |
FLT1 |
0.777 | -0.043 | -1 | 0.883 |
EPHA3 |
0.777 | -0.043 | 2 | 0.739 |
TNK2 |
0.777 | -0.088 | 3 | 0.751 |
AKT3 |
0.777 | -0.067 | -3 | 0.547 |
PRKX |
0.777 | 0.048 | -3 | 0.603 |
MERTK |
0.776 | -0.067 | 3 | 0.754 |
SNRK |
0.776 | -0.352 | 2 | 0.646 |
PDGFRB |
0.776 | -0.180 | 3 | 0.790 |
PAK6 |
0.776 | -0.071 | -2 | 0.661 |
PTK2 |
0.776 | 0.103 | -1 | 0.835 |
SYK |
0.775 | 0.137 | -1 | 0.826 |
TEK |
0.775 | -0.148 | 3 | 0.728 |
EPHA8 |
0.774 | 0.031 | -1 | 0.860 |
PKACA |
0.774 | -0.066 | -2 | 0.563 |
WEE1_TYR |
0.774 | -0.088 | -1 | 0.810 |
FGFR3 |
0.773 | -0.091 | 3 | 0.782 |
BRSK1 |
0.772 | -0.179 | -3 | 0.733 |
AXL |
0.772 | -0.145 | 3 | 0.772 |
FGFR1 |
0.772 | -0.181 | 3 | 0.762 |
ERBB2 |
0.772 | -0.132 | 1 | 0.762 |
LYN |
0.772 | -0.027 | 3 | 0.705 |
LTK |
0.772 | -0.106 | 3 | 0.739 |
NTRK1 |
0.772 | -0.146 | -1 | 0.871 |
MAPKAPK5 |
0.771 | -0.255 | -3 | 0.649 |
ALK |
0.771 | -0.125 | 3 | 0.715 |
FRK |
0.771 | -0.055 | -1 | 0.871 |
MATK |
0.770 | -0.065 | -1 | 0.810 |
EGFR |
0.770 | -0.019 | 1 | 0.679 |
PTK2B |
0.770 | -0.007 | -1 | 0.819 |
BTK |
0.770 | -0.186 | -1 | 0.801 |
PKN1 |
0.770 | -0.174 | -3 | 0.659 |
JAK1 |
0.769 | -0.137 | 1 | 0.718 |
PTK6 |
0.769 | -0.193 | -1 | 0.772 |
BRSK2 |
0.768 | -0.255 | -3 | 0.758 |
INSR |
0.768 | -0.128 | 3 | 0.721 |
TNNI3K_TYR |
0.768 | -0.133 | 1 | 0.813 |
EPHA2 |
0.767 | 0.046 | -1 | 0.830 |
NEK10_TYR |
0.767 | -0.218 | 1 | 0.649 |
NTRK2 |
0.767 | -0.183 | 3 | 0.759 |
SRC |
0.767 | -0.031 | -1 | 0.846 |
PHKG2 |
0.767 | -0.185 | -3 | 0.750 |
FGFR4 |
0.767 | -0.037 | -1 | 0.830 |
NTRK3 |
0.766 | -0.104 | -1 | 0.825 |
EPHA1 |
0.766 | -0.112 | 3 | 0.750 |
FLT4 |
0.766 | -0.188 | 3 | 0.753 |
PDGFRA |
0.765 | -0.305 | 3 | 0.785 |
CSK |
0.763 | -0.124 | 2 | 0.762 |
TNK1 |
0.763 | -0.252 | 3 | 0.746 |
DDR2 |
0.762 | -0.078 | 3 | 0.754 |
ERBB4 |
0.761 | -0.004 | 1 | 0.721 |
IGF1R |
0.758 | -0.097 | 3 | 0.669 |
CK1G1 |
0.756 | -0.067 | -3 | 0.577 |
PAK5 |
0.755 | -0.154 | -2 | 0.589 |
CK1G3 |
0.753 | -0.050 | -3 | 0.388 |
FES |
0.748 | -0.073 | -1 | 0.763 |
PAK4 |
0.746 | -0.137 | -2 | 0.594 |
MUSK |
0.745 | -0.202 | 1 | 0.660 |
ZAP70 |
0.742 | -0.018 | -1 | 0.770 |
CK1G2 |
0.738 | -0.029 | -3 | 0.489 |
PKG1 |
0.734 | -0.182 | -2 | 0.530 |
CK1A |
0.731 | -0.029 | -3 | 0.432 |