Motif 1108 (n=289)
Position-wise Probabilities
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uniprot | genes | site | source | protein | function |
---|---|---|---|---|---|
A0A075B759 | PPIAL4E | T68 | ochoa | Peptidyl-prolyl cis-trans isomerase A-like 4E (PPIase A-like 4E) (EC 5.2.1.8) | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. |
A0A0B4J203 | None | T68 | ochoa | receptor protein-tyrosine kinase (EC 2.7.10.1) | None |
A0A0B4J2A2 | PPIAL4C | T68 | ochoa | Peptidyl-prolyl cis-trans isomerase A-like 4C (PPIase A-like 4C) (EC 5.2.1.8) | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. |
A4UGR9 | XIRP2 | T1263 | ochoa | Xin actin-binding repeat-containing protein 2 (Beta-xin) (Cardiomyopathy-associated protein 3) (Xeplin) | Protects actin filaments from depolymerization (PubMed:15454575). Required for correct morphology of cell membranes and maturation of intercalated disks of cardiomyocytes via facilitating localization of XIRP1 and CDH2 to the termini of aligned mature cardiomyocytes (By similarity). Thereby required for correct postnatal heart development and growth regulation that is crucial for overall heart morphology and diastolic function (By similarity). Required for normal electrical conduction in the heart including formation of the infranodal ventricular conduction system and normal action potential configuration, as a result of its interaction with the cardiac ion channel components Scn5a/Nav1.5 and Kcna5/Kv1.5 (By similarity). Required for regular actin filament spacing of the paracrystalline array in both inner and outer hair cells of the cochlea, thereby required for maintenance of stereocilia morphology (By similarity). {ECO:0000250|UniProtKB:Q4U4S6, ECO:0000269|PubMed:15454575}. |
A6NEC2 | NPEPPSL1 | T136 | ochoa | Puromycin-sensitive aminopeptidase-like protein (EC 3.4.11.-) | Aminopeptidase with broad substrate specificity to several peptides. {ECO:0000250}. |
A6NKT7 | RGPD3 | T1178 | ochoa | RanBP2-like and GRIP domain-containing protein 3 | None |
F5H284 | PPIAL4D | T68 | ochoa | Peptidyl-prolyl cis-trans isomerase A-like 4D (PPIase A-like 4D) (EC 5.2.1.8) | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. |
H3BQZ7 | HNRNPUL2-BSCL2 | T165 | ochoa | Heterogeneous nuclear ribonucleoprotein U-like protein 2 | None |
H3BU86 | STX16-NPEPL1 | T212 | ochoa | Syntaxin-16 | SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000256|ARBA:ARBA00037772}. |
K7ELQ4 | ATF7-NPFF | T51 | ochoa | ATF7-NPFF readthrough | None |
O14662 | STX16 | T212 | ochoa | Syntaxin-16 (Syn16) | SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}. |
O14715 | RGPD8 | T1177 | ochoa | RANBP2-like and GRIP domain-containing protein 8 (Ran-binding protein 2-like 3) (RanBP2-like 3) (RanBP2L3) | None |
O43264 | ZW10 | T89 | ochoa | Centromere/kinetochore protein zw10 homolog | Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}. |
O43290 | SART1 | T430 | ochoa | U4/U6.U5 tri-snRNP-associated protein 1 (SNU66 homolog) (hSnu66) (Squamous cell carcinoma antigen recognized by T-cells 1) (SART-1) (hSART-1) (U4/U6.U5 tri-snRNP-associated 110 kDa protein) (allergen Hom s 1) | Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:25092792}. |
O43290 | SART1 | T764 | ochoa | U4/U6.U5 tri-snRNP-associated protein 1 (SNU66 homolog) (hSnu66) (Squamous cell carcinoma antigen recognized by T-cells 1) (SART-1) (hSART-1) (U4/U6.U5 tri-snRNP-associated 110 kDa protein) (allergen Hom s 1) | Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:25092792}. |
O43491 | EPB41L2 | T194 | ochoa | Band 4.1-like protein 2 (Erythrocyte membrane protein band 4.1-like 2) (Generally expressed protein 4.1) (4.1G) | Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127). {ECO:0000269|PubMed:23870127}. |
O60701 | UGDH | T93 | ochoa | UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) | Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). {ECO:0000250|UniProtKB:O70475, ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21961565, ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:25478983, ECO:0000269|PubMed:27966912, ECO:0000269|PubMed:30420606, ECO:0000269|PubMed:30457329, ECO:0000269|PubMed:32001716}. |
O60884 | DNAJA2 | T379 | ochoa | DnaJ homolog subfamily A member 2 (Cell cycle progression restoration gene 3 protein) (Dnj3) (Dj3) (HIRA-interacting protein 4) (Renal carcinoma antigen NY-REN-14) | Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877}. |
O75475 | PSIP1 | T134 | 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}. |
O95684 | CEP43 | T380 | ochoa | Centrosomal protein 43 (FGFR1 oncogene partner) | Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385). {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}. |
O95866 | MPIG6B | T127 | ochoa | Megakaryocyte and platelet inhibitory receptor G6b (Protein G6b) | Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production (PubMed:12665801, PubMed:17311996, PubMed:27743390). Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (PubMed:12665801). This regulation of megakaryocate function as well as platelet production ann activation is done through the inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling (PubMed:17311996). Appears to operate in a calcium-independent manner (PubMed:12665801). {ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:17311996, ECO:0000269|PubMed:27743390}.; FUNCTION: Isoform B, displayed in this entry, is the only isoform to contain both a transmembrane region and 2 immunoreceptor tyrosine-based inhibitor motifs (ITIMs) and, thus, the only one which probably has a role of inhibitory receptor. Isoform A may be the activating counterpart of isoform B. {ECO:0000305|PubMed:11544253}. |
P02730 | SLC4A1 | T44 | psp | Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233) | Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307, ECO:0000269|PubMed:35835865}.; FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305). {ECO:0000269|PubMed:12692305, ECO:0000269|PubMed:14630931}. |
P02763 | ORM1 | T65 | ochoa | Alpha-1-acid glycoprotein 1 (AGP 1) (Orosomucoid-1) (OMD 1) | Functions as a transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000269|PubMed:17008009, ECO:0000269|PubMed:17321687}. |
P04083 | ANXA1 | T223 | ochoa | Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26] | Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963, ECO:0000269|PubMed:8425544, ECO:0000269|PubMed:8557678}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades (PubMed:15187149, PubMed:22879591, PubMed:25664854). Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors (PubMed:15187149). Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration (PubMed:15187149). Promotes resolution of inflammation and wound healing (PubMed:25664854). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). {ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:25664854}. |
P04179 | SOD2 | T79 | psp | Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:10334867}. |
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}. |
P04626 | ERBB2 | T1003 | ochoa | Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Metastatic lymph node gene 19 protein) (MLN 19) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (Tyrosine kinase-type cell surface receptor HER2) (p185erbB2) (CD antigen CD340) | Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. {ECO:0000305}.; FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth. {ECO:0000269|PubMed:10358079, ECO:0000269|PubMed:15380516, ECO:0000269|PubMed:21555369}. |
P05412 | JUN | T89 | ochoa|psp | Transcription factor Jun (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39) | Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306). {ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:12618758, ECO:0000269|PubMed:17210646, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24623306}.; FUNCTION: (Microbial infection) Upon Epstein-Barr virus (EBV) infection, binds to viral BZLF1 Z promoter and activates viral BZLF1 expression. {ECO:0000269|PubMed:31341047}. |
P05976 | MYL1 | T65 | ochoa | Myosin light chain 1/3, skeletal muscle isoform (MLC1/MLC3) (MLC1F/MLC3F) (Myosin light chain alkali 1/2) (Myosin light chain A1/A2) | Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function. {ECO:0000269|PubMed:30215711}. |
P06748 | NPM1 | T199 | ochoa|psp | Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin) | Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25956029}. |
P07355 | ANXA2 | T55 | ochoa | Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) | Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic surveillance and neoangiogenesis (By similarity). {ECO:0000250|UniProtKB:P07356, ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.; FUNCTION: (Microbial infection) Binds M.pneumoniae CARDS toxin, probably serves as one receptor for this pathogen. When ANXA2 is down-regulated by siRNA, less toxin binds to human cells and less vacuolization (a symptom of M.pneumoniae infection) is seen. {ECO:0000269|PubMed:25139904}. |
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 | T1162 | ochoa | RANBP2-like and GRIP domain-containing protein 1 (Ran-binding protein 2-like 6) (RanBP2-like 6) (RanBP2L6) | None |
P0DJD1 | RGPD2 | T1170 | ochoa | RANBP2-like and GRIP domain-containing protein 2 (Ran-binding protein 2-like 2) (RanBP2-like 2) (RanBP2L2) | None |
P0DN26 | PPIAL4F | T68 | ochoa | Peptidyl-prolyl cis-trans isomerase A-like 4F (PPIase A-like 4F) (EC 5.2.1.8) | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}. |
P10645 | CHGA | T146 | ochoa | Chromogranin-A (CgA) (Pituitary secretory protein I) (SP-I) [Cleaved into: Vasostatin-1 (Vasostatin I); Vasostatin-2 (Vasostatin II); EA-92; ES-43; Pancreastatin; SS-18; WA-8; WE-14; LF-19; Catestatin (SL21); AL-11; GV-19; GR-44; ER-37; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor] | [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:15326220). Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa (PubMed:15723172, PubMed:24723458). Can induce mast cell migration, degranulation and production of cytokines and chemokines (PubMed:21214543). Acts as a potent scavenger of free radicals in vitro (PubMed:24723458). May play a role in the regulation of cardiac function and blood pressure (PubMed:18541522). {ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:15723172, ECO:0000269|PubMed:21214543, ECO:0000269|PubMed:24723458, ECO:0000303|PubMed:18541522}.; FUNCTION: [Serpinin]: Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation. {ECO:0000250|UniProtKB:P26339}. |
P11021 | HSPA5 | T229 | psp | Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) | Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:11907036, PubMed:1550958, PubMed:19538957, PubMed:36739529). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Also binds and inactivates EIF2AK3/PERK in unstressed cells (PubMed:11907036). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1 and EIF2AK3/PERK, allowing their homodimerization and subsequent activation (PubMed:11907036). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (PubMed:26045166). {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P20029, ECO:0000269|PubMed:11907036, ECO:0000269|PubMed:1550958, ECO:0000269|PubMed:19538957, ECO:0000269|PubMed:2294010, ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:26045166, ECO:0000269|PubMed:28332555, ECO:0000269|PubMed:29719251, ECO:0000269|PubMed:36739529}.; FUNCTION: (Microbial infection) Plays an important role in viral binding to the host cell membrane and entry for several flaviruses such as Dengue virus, Zika virus and Japanese encephalitis virus (PubMed:15098107, PubMed:28053106, PubMed:33432092). Acts as a component of the cellular receptor for Dengue virus serotype 2/DENV-2 on human liver cells (PubMed:15098107). {ECO:0000269|PubMed:15098107, ECO:0000269|PubMed:28053106, ECO:0000269|PubMed:33432092}.; FUNCTION: (Microbial infection) Acts as a receptor for CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi (PubMed:20484814, PubMed:24355926, PubMed:32487760). Acts as a receptor for R.delemar CotH3 in nasal epithelial cells, which may be an early step in rhinoorbital/cerebral mucormycosis (RCM) disease progression (PubMed:32487760). {ECO:0000269|PubMed:20484814, ECO:0000269|PubMed:24355926, ECO:0000269|PubMed:32487760}. |
P11171 | EPB41 | T633 | ochoa | Protein 4.1 (P4.1) (4.1R) (Band 4.1) (EPB4.1) (Erythrocyte membrane protein band 4.1) | Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127). {ECO:0000269|PubMed:23870127}. |
P11388 | TOP2A | T1112 | ochoa | DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme) | Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612}. |
P11532 | DMD | T3654 | ochoa | Dystrophin | Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000250|UniProtKB:P11531, ECO:0000269|PubMed:16710609}. |
P12270 | TPR | T2133 | ochoa | Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein) | Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:11952838, PubMed:22253824). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:9864356}. |
P14317 | HCLS1 | T114 | ochoa | Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1) (p75) | Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression. |
P14625 | HSP90B1 | T44 | ochoa | Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Heat shock protein family C member 4) (Tumor rejection antigen 1) (gp96 homolog) | ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}. |
P14923 | JUP | T19 | ochoa | Junction plakoglobin (Catenin gamma) (Desmoplakin III) (Desmoplakin-3) | Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). {ECO:0000250}. |
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}. |
P15311 | EZR | T98 | ochoa | Ezrin (Cytovillin) (Villin-2) (p81) | Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. {ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19111582}. |
P15336 | ATF2 | T69 | ochoa|psp | Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (Activating transcription factor 2) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (HB16) (cAMP response element-binding protein CRE-BP1) | Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro (PubMed:10821277). In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type. {ECO:0000269|PubMed:10821277, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:22304920}. |
P16284 | PECAM1 | T711 | ochoa | Platelet endothelial cell adhesion molecule (PECAM-1) (EndoCAM) (GPIIA') (PECA1) (CD antigen CD31) | Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:17580308, PubMed:19342684). Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis (By similarity). {ECO:0000250|UniProtKB:Q08481, ECO:0000269|PubMed:12110892, ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18672896, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:27958302}.; FUNCTION: [Isoform Delta15]: Does not protect against apoptosis. {ECO:0000269|PubMed:18388311}. |
P16989 | YBX3 | T121 | ochoa | Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Single-strand DNA-binding protein NF-GMB) | Binds to the GM-CSF promoter. Seems to act as a repressor. Also binds to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. |
P17535 | JUND | T115 | ochoa | Transcription factor JunD (Transcription factor AP-1 subunit JunD) | Transcription factor binding AP-1 sites (PubMed:9989505). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (PubMed:28981703, PubMed:9989505). {ECO:0000269|PubMed:28981703, ECO:0000269|PubMed:9989505}. |
P17544 | ATF7 | T51 | psp | Cyclic AMP-dependent transcription factor ATF-7 (cAMP-dependent transcription factor ATF-7) (Activating transcription factor 7) (Transcription factor ATF-A) | Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation (PubMed:29490055). In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recruiting histone H3K9 tri- and di-methyltransferases thus silencing the transcription of target genes such as STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes (By similarity). Stress induces ATF7 phosphorylation that disrupts interactions with histone methyltransferase and enhances the association with coactivators containing histone acetyltransferase and/or histone demethylase, leading to disruption of the heterochromatin-like structure and subsequently transcriptional activation (By similarity). In response to TNF-alpha, which is induced by various stresses, phosphorylated ATF7 and telomerase are released from telomeres leading to telomere shortening (PubMed:29490055). Also plays a role in maintaining epithelial regenerative capacity and protecting against cell death during intestinal epithelial damage and repair (By similarity). {ECO:0000250|UniProtKB:Q8R0S1, ECO:0000269|PubMed:29490055}.; FUNCTION: [Isoform 4]: Acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter.; FUNCTION: [Isoform 5]: Acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation. {ECO:0000269|PubMed:21858082}. |
P19652 | ORM2 | T65 | ochoa | Alpha-1-acid glycoprotein 2 (AGP 2) (Orosomucoid-2) (OMD 2) | Functions as a transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction. {ECO:0000269|PubMed:21349832}. |
P21127 | CDK11B | T448 | ochoa | Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1) | Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity-dependent manner. Isoform 7 may act as a negative regulator of normal cell cycle progression. {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:18216018, ECO:0000269|PubMed:2217177}. |
P21333 | FLNA | T1288 | ochoa | Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin) | Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:22121117, ECO:0000269|PubMed:25358863}. |
P22626 | HNRNPA2B1 | T140 | ochoa | Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) | Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}. |
P22626 | HNRNPA2B1 | T145 | ochoa | Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1) | Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}. |
P23396 | RPS3 | T42 | psp | Small ribosomal subunit protein uS3 (40S ribosomal protein S3) (EC 4.2.99.18) | Component of the small ribosomal subunit (PubMed:23636399, PubMed:8706699). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408). {ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971, ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:23911537, ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}. |
P30414 | NKTR | T1155 | ochoa | NK-tumor recognition protein (NK-TR protein) (Natural-killer cells cyclophilin-related protein) (Peptidyl-prolyl cis-trans isomerase NKTR) (PPIase) (EC 5.2.1.8) (Rotamase) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688). {ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:8421688}. |
P30566 | ADSL | T239 | ochoa | Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) | Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. {ECO:0000269|PubMed:10888601}. |
P31645 | SLC6A4 | T59 | ochoa | Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) | Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation (PubMed:17506858, PubMed:18317590). Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity). {ECO:0000250|UniProtKB:P31652, ECO:0000250|UniProtKB:Q60857, ECO:0000269|PubMed:10407194, ECO:0000269|PubMed:12869649, ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:18317590, ECO:0000269|PubMed:21730057, ECO:0000269|PubMed:27049939, ECO:0000269|PubMed:27756841, ECO:0000269|PubMed:34851672}. |
P33981 | TTK | T45 | 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}. |
P35222 | CTNNB1 | T653 | ochoa|psp | Catenin beta-1 (Beta-catenin) | Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22187462, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:29910125}. |
P35372 | OPRM1 | T372 | psp | Mu-type opioid receptor (M-OR-1) (MOR-1) (Mu opiate receptor) (Mu opioid receptor) (MOP) (hMOP) | Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:10529478, PubMed:12589820, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:10529478, PubMed:10836142, PubMed:12589820, PubMed:19300905, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity). Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors (PubMed:7905839). The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 (PubMed:12068084). They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (By similarity). Also couples to adenylate cyclase stimulatory G alpha proteins (By similarity). The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4 (By similarity). Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (By similarity). Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction (By similarity). The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins (By similarity). The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation (By similarity). Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling (By similarity). Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling (By similarity). Endogenous ligands induce rapid desensitization, endocytosis and recycling (By similarity). Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (By similarity). {ECO:0000250|UniProtKB:P33535, ECO:0000269|PubMed:10529478, ECO:0000269|PubMed:12068084, ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:7891175, ECO:0000269|PubMed:7905839, ECO:0000269|PubMed:7957926, ECO:0000269|PubMed:9689128, ECO:0000303|PubMed:10836142, ECO:0000303|PubMed:19300905}.; FUNCTION: [Isoform 12]: Couples to GNAS and is proposed to be involved in excitatory effects. {ECO:0000269|PubMed:20525224}.; FUNCTION: [Isoform 16]: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. {ECO:0000269|PubMed:16580639}.; FUNCTION: [Isoform 17]: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. {ECO:0000269|PubMed:16580639}. |
P35968 | KDR | T1217 | ochoa | Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor) (KDR) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309) | Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. {ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:10368301, ECO:0000269|PubMed:10600473, ECO:0000269|PubMed:11387210, ECO:0000269|PubMed:12649282, ECO:0000269|PubMed:1417831, ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:16966330, ECO:0000269|PubMed:17303569, ECO:0000269|PubMed:18529047, ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:19834490, ECO:0000269|PubMed:20080685, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:20705758, ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:7929439, ECO:0000269|PubMed:9160888, ECO:0000269|PubMed:9804796, ECO:0000269|PubMed:9837777}. |
P36915 | GNL1 | T342 | ochoa | Guanine nucleotide-binding protein-like 1 (GTP-binding protein HSR1) | Possible regulatory or functional link with the histocompatibility cluster. |
P46821 | MAP1B | T1896 | ochoa | Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] | Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:33268592}. |
P46821 | MAP1B | T1930 | ochoa | Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] | Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:33268592}. |
P46821 | MAP1B | T2032 | ochoa | Microtubule-associated protein 1B (MAP-1B) [Cleaved into: MAP1B heavy chain; MAP1 light chain LC1] | Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B is required for proper microtubule dynamics and plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (PubMed:33268592). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017, ECO:0000269|PubMed:33268592}. |
P49407 | ARRB1 | T381 | ochoa | Beta-arrestin-1 (Arrestin beta-1) (Non-visual arrestin-2) | Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as a signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as a signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates in the recruitment of the ubiquitin-protein ligase to the receptor (PubMed:23886940). {ECO:0000250, ECO:0000269|PubMed:12464600, ECO:0000269|PubMed:14711824, ECO:0000269|PubMed:15475570, ECO:0000269|PubMed:15611106, ECO:0000269|PubMed:15671180, ECO:0000269|PubMed:15878855, ECO:0000269|PubMed:16144840, ECO:0000269|PubMed:16280323, ECO:0000269|PubMed:16378096, ECO:0000269|PubMed:16492667, ECO:0000269|PubMed:16709866, ECO:0000269|PubMed:18337459, ECO:0000269|PubMed:18419762, ECO:0000269|PubMed:19620252, ECO:0000269|PubMed:19643177, ECO:0000269|PubMed:22457824, ECO:0000269|PubMed:23341447, ECO:0000269|PubMed:23633677, ECO:0000269|PubMed:23886940}. |
P49792 | RANBP2 | T2153 | ochoa|psp | 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}. |
P49848 | TAF6 | T120 | ochoa | Transcription initiation factor TFIID subunit 6 (RNA polymerase II TBP-associated factor subunit E) (Transcription initiation factor TFIID 70 kDa subunit) (TAF(II)70) (TAFII-70) (TAFII70) (Transcription initiation factor TFIID 80 kDa subunit) (TAF(II)80) (TAFII-80) (TAFII80) | The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TAF6 homodimer connects TFIID modules, forming a rigid core (PubMed:33795473). {ECO:0000269|PubMed:33795473}.; FUNCTION: [Isoform 4]: Transcriptional regulator which acts primarily as a positive regulator of transcription (PubMed:20096117, PubMed:29358700). Recruited to the promoters of a number of genes including GADD45A and CDKN1A/p21, leading to transcriptional up-regulation and subsequent induction of apoptosis (PubMed:11583621). Also up-regulates expression of other genes including GCNA/ACRC, HES1 and IFFO1 (PubMed:18628956). In contrast, down-regulates transcription of MDM2 (PubMed:11583621). Acts as a transcriptional coactivator to enhance transcription of TP53/p53-responsive genes such as DUSP1 (PubMed:20096117). Can also activate transcription and apoptosis independently of TP53 (PubMed:18628956). Drives apoptosis via the intrinsic apoptotic pathway by up-regulating apoptosis effectors such as BCL2L11/BIM and PMAIP1/NOXA (PubMed:29358700). {ECO:0000269|PubMed:11583621, ECO:0000269|PubMed:18628956, ECO:0000269|PubMed:20096117, ECO:0000269|PubMed:29358700}. |
P51617 | IRAK1 | T66 | psp | Interleukin-1 receptor-associated kinase 1 (IRAK-1) (EC 2.7.11.1) | Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. {ECO:0000269|PubMed:11397809, ECO:0000269|PubMed:12860405, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:15767370, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509}. |
P54296 | MYOM2 | T676 | 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. |
P55010 | EIF5 | T208 | psp | Eukaryotic translation initiation factor 5 (eIF-5) | Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744). {ECO:0000269|PubMed:11166181, ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:24319994}. |
P55786 | NPEPPS | T136 | ochoa | Puromycin-sensitive aminopeptidase (PSA) (EC 3.4.11.14) (Cytosol alanyl aminopeptidase) (AAP-S) | Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:11062501, ECO:0000269|PubMed:17154549, ECO:0000269|PubMed:17318184, ECO:0000269|PubMed:19917696}. |
P60660 | MYL6 | T22 | ochoa | Myosin light polypeptide 6 (17 kDa myosin light chain) (LC17) (Myosin light chain 3) (MLC-3) (Myosin light chain alkali 3) (Myosin light chain A3) (Smooth muscle and nonmuscle myosin light chain alkali 6) | Regulatory light chain of myosin. Does not bind calcium. |
P62937 | PPIA | T68 | ochoa | Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed] | Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.; FUNCTION: (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269|PubMed:15688292}.; FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269|PubMed:21593166}. |
P67809 | YBX1 | T89 | ochoa|psp | Y-box-binding protein 1 (YB-1) (CCAAT-binding transcription factor I subunit A) (CBF-A) (DNA-binding protein B) (DBPB) (Enhancer factor I subunit A) (EFI-A) (Nuclease-sensitive element-binding protein 1) (Y-box transcription factor) | DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation (PubMed:10817758, PubMed:11698476, PubMed:14718551, PubMed:18809583, PubMed:31358969, PubMed:8188694). Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (PubMed:19561594, PubMed:31358969). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay (PubMed:10817758, PubMed:11698476, PubMed:31358969). Component of the CRD-mediated complex that promotes MYC mRNA stability (PubMed:19029303). Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs (PubMed:27559612, PubMed:29073095). Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (PubMed:28341602, PubMed:29073095). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (PubMed:29712925). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (PubMed:12604611). Binds to TSC22D1 transcripts, thereby inhibiting their translation and negatively regulating TGF-beta-mediated transcription of COL1A2 (By similarity). Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7' (PubMed:18809583). Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:18809583, PubMed:8188694). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin (PubMed:14718551). Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair (PubMed:14718551). The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (PubMed:19483673). {ECO:0000250|UniProtKB:P62960, ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:10817758, ECO:0000269|PubMed:11698476, ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19483673, ECO:0000269|PubMed:19561594, ECO:0000269|PubMed:27559612, ECO:0000269|PubMed:28341602, ECO:0000269|PubMed:29073095, ECO:0000269|PubMed:29712925, ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:8188694}. |
P67809 | YBX1 | T271 | ochoa | Y-box-binding protein 1 (YB-1) (CCAAT-binding transcription factor I subunit A) (CBF-A) (DNA-binding protein B) (DBPB) (Enhancer factor I subunit A) (EFI-A) (Nuclease-sensitive element-binding protein 1) (Y-box transcription factor) | DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation (PubMed:10817758, PubMed:11698476, PubMed:14718551, PubMed:18809583, PubMed:31358969, PubMed:8188694). Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (PubMed:19561594, PubMed:31358969). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay (PubMed:10817758, PubMed:11698476, PubMed:31358969). Component of the CRD-mediated complex that promotes MYC mRNA stability (PubMed:19029303). Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs (PubMed:27559612, PubMed:29073095). Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (PubMed:28341602, PubMed:29073095). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (PubMed:29712925). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (PubMed:12604611). Binds to TSC22D1 transcripts, thereby inhibiting their translation and negatively regulating TGF-beta-mediated transcription of COL1A2 (By similarity). Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7' (PubMed:18809583). Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:18809583, PubMed:8188694). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin (PubMed:14718551). Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair (PubMed:14718551). The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (PubMed:19483673). {ECO:0000250|UniProtKB:P62960, ECO:0000250|UniProtKB:Q28618, ECO:0000269|PubMed:10817758, ECO:0000269|PubMed:11698476, ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:14718551, ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19483673, ECO:0000269|PubMed:19561594, ECO:0000269|PubMed:27559612, ECO:0000269|PubMed:28341602, ECO:0000269|PubMed:29073095, ECO:0000269|PubMed:29712925, ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:8188694}. |
P68104 | EEF1A1 | T88 | ochoa|psp | 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}. |
P78317 | RNF4 | T110 | ochoa | E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Small nuclear ring finger protein) (Protein SNURF) | E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:18408734, PubMed:19307308, PubMed:35013556). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:18408734, PubMed:19307308, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (PubMed:20212317). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (PubMed:19779455, PubMed:20026589). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (PubMed:12885770). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (PubMed:35013556). {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:19779455, ECO:0000269|PubMed:20026589, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20943951, ECO:0000269|PubMed:35013556}. |
P82094 | TMF1 | T401 | ochoa | TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa) | Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269|PubMed:10428808, ECO:0000269|PubMed:1409643, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:17698061}. |
Q00536 | CDK16 | T380 | psp | Cyclin-dependent kinase 16 (EC 2.7.11.22) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1) | Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}. |
Q00610 | CLTC | T105 | ochoa | Clathrin heavy chain 1 (Clathrin heavy chain on chromosome 17) (CLH-17) | Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872). Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (By similarity). {ECO:0000250|UniProtKB:P49951, ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:20639872, ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}. |
Q01118 | SCN7A | T794 | ochoa | Sodium channel protein type 7 subunit alpha (Atypical sodium channel Nav2.1) (Nax channel) (Sodium channel protein type VII subunit alpha) | Sodium leak channel functioning as an osmosensor regulating sodium ion levels in various tissues and organs. While most sodium channels are voltage-gated, SCN7A is not and lets sodium flow through membrane along its concentration gradient (PubMed:26537257, PubMed:35301303). In glial cells of the central nervous system, senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake through activation of nearby neurons to maintain appropriate sodium levels in the body (By similarity). By mediating sodium influx into keratinocytes, also plays a role in skin barrier homeostasis (PubMed:26537257). {ECO:0000250|UniProtKB:B1AYL1, ECO:0000269|PubMed:26537257, ECO:0000269|PubMed:35301303}. |
Q02446 | SP4 | T609 | ochoa | Transcription factor Sp4 (SPR-1) | Binds to GT and GC boxes promoters elements. Probable transcriptional activator. |
Q03188 | CENPC | T231 | ochoa | Centromere protein C (CENP-C) (Centromere autoantigen C) (Centromere protein C 1) (CENP-C 1) (Interphase centromere complex protein 7) | Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269|PubMed:19482874, ECO:0000269|PubMed:21529714}. |
Q05397 | PTK2 | T386 | ochoa | Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK) | Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076, ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453, ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381, ECO:0000269|PubMed:21454698, ECO:0000269|PubMed:9360983}.; FUNCTION: [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:20109444}. |
Q05519 | SRSF11 | T452 | ochoa | Serine/arginine-rich splicing factor 11 (Arginine-rich 54 kDa nuclear protein) (p54) (Splicing factor, arginine/serine-rich 11) | May function in pre-mRNA splicing. |
Q09666 | AHNAK | T3716 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q09666 | AHNAK | T4430 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q09666 | AHNAK | T4766 | ochoa | Neuroblast differentiation-associated protein AHNAK (Desmoyokin) | May be required for neuronal cell differentiation. |
Q12888 | TP53BP1 | T591 | ochoa | TP53-binding protein 1 (53BP1) (p53-binding protein 1) (p53BP1) | Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}. |
Q12888 | TP53BP1 | 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}. |
Q12888 | TP53BP1 | T1709 | 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}. |
Q13043 | STK4 | T387 | psp | 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}. |
Q13137 | CALCOCO2 | T39 | psp | Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52) | Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (PubMed:22246324). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation (PubMed:23022382, PubMed:25771791). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (PubMed:23022382, PubMed:25771791). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (PubMed:17635994). {ECO:0000269|PubMed:17635994, ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:25771791}. |
Q13247 | SRSF6 | T146 | ochoa | Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6) | Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269|PubMed:12549914, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:24440982}. |
Q13435 | SF3B2 | T785 | ochoa | Splicing factor 3B subunit 2 (Pre-mRNA-splicing factor SF3b 145 kDa subunit) (SF3b145) (Spliceosome-associated protein 145) (SAP 145) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B2 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:27720643). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34822310}. |
Q13501 | SQSTM1 | T339 | ochoa | Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62) (p62) | Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12471037, ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:15911346, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16079148, ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19931284, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20452972, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22622177, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:25101860, ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:27368102, ECO:0000269|PubMed:28380357, ECO:0000269|PubMed:28404643, ECO:0000269|PubMed:29343546, ECO:0000269|PubMed:29496741, ECO:0000269|PubMed:29507397, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:33393215, ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:33509017, ECO:0000269|PubMed:34471133, ECO:0000269|PubMed:34893540, ECO:0000269|PubMed:35831301, ECO:0000269|PubMed:37306101, ECO:0000269|PubMed:37802024}. |
Q13586 | STIM1 | T389 | psp | Stromal interaction molecule 1 | Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671). {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19622606, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:28219928, ECO:0000269|PubMed:32415068}. |
Q13621 | SLC12A1 | T100 | psp | Solute carrier family 12 member 1 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1) (BSC1) (Kidney-specific Na-K-Cl symporter) (Na-K-2Cl cotransporter 2) (NKCC2) | Renal sodium, potassium and chloride ion cotransporter that mediates the transepithelial NaCl reabsorption in the thick ascending limb and plays an essential role in the urinary concentration and volume regulation (PubMed:21321328). Electrically silent transporter system (By similarity). {ECO:0000250|UniProtKB:P55014, ECO:0000250|UniProtKB:P55016, ECO:0000269|PubMed:21321328}. |
Q13813 | SPTAN1 | T1258 | ochoa | Spectrin alpha chain, non-erythrocytic 1 (Alpha-II spectrin) (Fodrin alpha chain) (Spectrin, non-erythroid alpha subunit) | Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. |
Q13838 | DDX39B | T20 | ochoa | Spliceosome RNA helicase DDX39B (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (ATP-dependent RNA helicase p47) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein) | Involved in nuclear export of spliced and unspliced mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). The THOC1-THOC2-THOC3 core complex alone is sufficient to promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). Associates with SARNP/CIP29, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC4 and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability. {ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:15585580, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17562711, ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:20844015, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:33191911, ECO:0000269|PubMed:37578863, ECO:0000269|PubMed:9242493}.; FUNCTION: Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect. {ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:9242493}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}. |
Q14162 | SCARF1 | T689 | ochoa | Scavenger receptor class F member 1 (Acetyl LDL receptor) (Scavenger receptor expressed by endothelial cells 1) (SREC-I) | Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). {ECO:0000250}. |
Q14574 | DSC3 | T788 | ochoa | Desmocollin-3 (Cadherin family member 3) (Desmocollin-4) (HT-CP) | A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (By similarity). Required for cell-cell adhesion in the epidermis, as a result required for the maintenance of the dermal cohesion and the dermal barrier function (PubMed:19717567). Required for cell-cell adhesion of epithelial cell layers surrounding the telogen hair club, as a result plays an important role in telogen hair shaft anchorage (By similarity). Essential for successful completion of embryo compaction and embryo development (By similarity). {ECO:0000250|UniProtKB:P55850, ECO:0000269|PubMed:19717567}. |
Q14643 | ITPR1 | T1152 | ochoa | Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 (IP3 receptor isoform 1) (IP3R 1) (InsP3R1) (Inositol 1,4,5 trisphosphate receptor) (Inositol 1,4,5-trisphosphate receptor type 1) (Type 1 inositol 1,4,5-trisphosphate receptor) (Type 1 InsP3 receptor) | Inositol 1,4,5-trisphosphate-gated calcium channel that, upon inositol 1,4,5-trisphosphate binding, mediates calcium release from the endoplasmic reticulum (ER) (PubMed:10620513, PubMed:27108797). Undergoes conformational changes upon ligand binding, suggesting structural flexibility that allows the channel to switch from a closed state, capable of interacting with its ligands such as 1,4,5-trisphosphate and calcium, to an open state, capable of transferring calcium ions across the ER membrane (By similarity). Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CAMK2 complex (By similarity). Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Regulates fertilization and egg activation by tuning the frequency and amplitude of calcium oscillations (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000250|UniProtKB:P29994, ECO:0000269|PubMed:10620513, ECO:0000269|PubMed:27108797}. |
Q14839 | CHD4 | T367 | ochoa | Chromodomain-helicase-DNA-binding protein 4 (CHD-4) (EC 3.6.4.-) (ATP-dependent helicase CHD4) (Mi-2 autoantigen 218 kDa protein) (Mi2-beta) | ATP-dependent chromatin-remodeling factor that binds and distorts nucleosomal DNA (PubMed:28977666, PubMed:32543371). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:17626165, PubMed:28977666, PubMed:9804427). Localizes to acetylated damaged chromatin in a ZMYND8-dependent manner, to promote transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309). Involved in neurogenesis (By similarity). {ECO:0000250|UniProtKB:Q6PDQ2, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:32543371, ECO:0000269|PubMed:9804427}. |
Q15007 | WTAP | T148 | ochoa|psp | Pre-mRNA-splicing regulator WTAP (Female-lethal(2)D homolog) (hFL(2)D) (WT1-associated protein) (Wilms tumor 1-associating protein) | Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Required for accumulation of METTL3 and METTL14 to nuclear speckle (PubMed:24316715, PubMed:24407421, PubMed:24981863). Acts as a mRNA splicing regulator (PubMed:12444081). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (PubMed:17088532). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (PubMed:17095724). {ECO:0000269|PubMed:12444081, ECO:0000269|PubMed:17088532, ECO:0000269|PubMed:17095724, ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:24981863, ECO:0000269|PubMed:29507755}. |
Q15057 | ACAP2 | T749 | ochoa | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2) | GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). Doesn't show GAP activity for RAB35 (PubMed:30905672). {ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:30905672}. |
Q15058 | KIF14 | T915 | ochoa | Kinesin-like protein KIF14 | Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:16648480, PubMed:24784001). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250|UniProtKB:L0N7N1, ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480, ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001, ECO:0000269|PubMed:24854087}. |
Q15149 | PLEC | T3152 | ochoa | Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1) | Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}. |
Q15149 | PLEC | T3370 | ochoa | Plectin (PCN) (PLTN) (Hemidesmosomal protein 1) (HD1) (Plectin-1) | Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}. |
Q15637 | SF1 | T232 | ochoa | Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) | Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}. |
Q15796 | SMAD2 | T197 | psp | Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2) | Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209). {ECO:0000250|UniProtKB:Q62432, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:9892009}. |
Q15831 | STK11 | T363 | psp | Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1) (LKB1) (hLKB1) (Renal carcinoma antigen NY-REN-19) | Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:11430832, ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15016379, ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:15987703, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.; FUNCTION: [Isoform 2]: Has a role in spermiogenesis. {ECO:0000250}. |
Q1KMD3 | HNRNPUL2 | T165 | ochoa | Heterogeneous nuclear ribonucleoprotein U-like protein 2 (Scaffold-attachment factor A2) (SAF-A2) | None |
Q2M2Z5 | KIZ | T379 | psp | Centrosomal protein kizuna (Polo-like kinase 1 substrate 1) | Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole. {ECO:0000269|PubMed:16980960}. |
Q58WW2 | DCAF6 | T654 | ochoa | DDB1- and CUL4-associated factor 6 (Androgen receptor complex-associated protein) (ARCAP) (IQ motif and WD repeat-containing protein 1) (Nuclear receptor interaction protein) (NRIP) | Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:15784617, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}. |
Q5K651 | SAMD9 | T160 | ochoa | Sterile alpha motif domain-containing protein 9 (SAM domain-containing protein 9) | Double-stranded nucleic acid binding that acts as an antiviral factor by playing an essential role in the formation of cytoplasmic antiviral granules (PubMed:25428864, PubMed:28157624). May play a role in the inflammatory response to tissue injury and the control of extra-osseous calcification, acting as a downstream target of TNF-alpha signaling. Involved in the regulation of EGR1, in coordination with RGL2. May be involved in endosome fusion. {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730, ECO:0000269|PubMed:21160498, ECO:0000269|PubMed:24029230, ECO:0000269|PubMed:25428864, ECO:0000269|PubMed:28157624}. |
Q5MJ10 | SPANXN2 | T51 | ochoa | Sperm protein associated with the nucleus on the X chromosome N2 (Nuclear-associated protein SPAN-Xn2) (SPANX-N2) (SPANX family member N2) | None |
Q5SW79 | CEP170 | T682 | ochoa | Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein) | Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:28422092}. |
Q5SW79 | CEP170 | T891 | ochoa | Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein) | Plays a role in microtubule organization (PubMed:15616186). Required for centriole subdistal appendage assembly (PubMed:28422092). {ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:28422092}. |
Q5TCX8 | MAP3K21 | T592 | ochoa | Mitogen-activated protein kinase kinase kinase 21 (EC 2.7.11.25) (Mitogen-activated protein kinase kinase kinase MLK4) (Mixed lineage kinase 4) | Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways. {ECO:0000269|PubMed:21602844}. |
Q5UIP0 | RIF1 | T1979 | ochoa | Telomere-associated protein RIF1 (Rap1-interacting factor 1 homolog) | Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage: acts by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs (PubMed:15342490, PubMed:28241136). In response to DNA damage, interacts with ATM-phosphorylated TP53BP1 (PubMed:23333306, PubMed:28241136). Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs (PubMed:28241136). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1 and TP53BP1 specifically counteract the function of BRCA1 by blocking DSBs resection via homologous recombination (HR) during G1 phase (PubMed:23333306). Also required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (By similarity). Promotes NHEJ of dysfunctional telomeres (By similarity). {ECO:0000250|UniProtKB:Q6PR54, ECO:0000269|PubMed:15342490, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:28241136}. |
Q5VST9 | OBSCN | T4788 | ochoa | Obscurin (EC 2.7.11.1) (Obscurin-RhoGEF) (Obscurin-myosin light chain kinase) (Obscurin-MLCK) | Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (PubMed:11448995, PubMed:16205939). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (By similarity). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (PubMed:28826662). {ECO:0000250|UniProtKB:A2AAJ9, ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:16205939, ECO:0000269|PubMed:28826662}. |
Q5VTB9 | RNF220 | T401 | ochoa | E3 ubiquitin-protein ligase RNF220 (EC 2.3.2.27) (RING finger protein 220) (RING-type E3 ubiquitin transferase RNF220) | E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658, PubMed:33964137). Plays a critical role in the regulation of nuclear lamina (PubMed:33964137). {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658, ECO:0000269|PubMed:33964137}. |
Q5VTE0 | EEF1A1P5 | T88 | 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}. |
Q5VTT5 | MYOM3 | T1143 | ochoa | Myomesin-3 (Myomesin family member 3) | May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. {ECO:0000250}. |
Q5VUB5 | FAM171A1 | T448 | ochoa | Protein FAM171A1 (Astroprincin) (APCN) | Involved in the regulation of the cytoskeletal dynamics, plays a role in actin stress fiber formation. {ECO:0000269|PubMed:30312582}. |
Q66K14 | TBC1D9B | T1148 | ochoa | TBC1 domain family member 9B | May act as a GTPase-activating protein for Rab family protein(s). |
Q6AI08 | HEATR6 | T1119 | ochoa | HEAT repeat-containing protein 6 (Amplified in breast cancer protein 1) | Amplification-dependent oncogene. |
Q6KC79 | NIPBL | T1733 | ochoa | Nipped-B-like protein (Delangin) (SCC2 homolog) | Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodimeric complex (also known as cohesin loading complex) with MAU2/SCC4 which mediates the loading of the cohesin complex onto chromatin (PubMed:22628566, PubMed:28914604). Plays a role in cohesin loading at sites of DNA damage. Its recruitment to double-strand breaks (DSBs) sites occurs in a CBX3-, RNF8- and RNF168-dependent manner whereas its recruitment to UV irradiation-induced DNA damage sites occurs in a ATM-, ATR-, RNF8- and RNF168-dependent manner (PubMed:28167679). Along with ZNF609, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others (By similarity). {ECO:0000250|UniProtKB:Q6KCD5, ECO:0000269|PubMed:22628566, ECO:0000269|PubMed:28167679, ECO:0000269|PubMed:28914604}. |
Q6PGQ7 | BORA | T501 | psp | Protein aurora borealis (HsBora) | Required for the activation of AURKA at the onset of mitosis. {ECO:0000269|PubMed:16890155}. |
Q6PJT7 | ZC3H14 | T325 | ochoa | Zinc finger CCCH domain-containing protein 14 (Mammalian suppressor of tau pathology-2) (MSUT-2) (Renal carcinoma antigen NY-REN-37) | RNA-binding protein involved in the biogenesis of circular RNAs (circRNAs), which are produced by back-splicing circularization of pre-mRNAs (PubMed:39461343). Acts by binding to both exon-intron boundary and 3'-UTR of pre-mRNAs to promote circRNA biogenesis through dimerization and the association with the spliceosome (PubMed:39461343). Required for spermatogenesis via involvement in circRNA biogenesis (PubMed:39461343). Regulates the pre-mRNA processing of ATP5MC1; preventing its degradation (PubMed:27563065). Also binds the poly(A) tail of mRNAs; controlling poly(A) length in neuronal cells (PubMed:17630287, PubMed:24671764). {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:24671764, ECO:0000269|PubMed:27563065, ECO:0000269|PubMed:39461343}. |
Q6UN15 | FIP1L1 | T68 | ochoa | Pre-mRNA 3'-end-processing factor FIP1 (hFip1) (FIP1-like 1 protein) (Factor interacting with PAP) (Rearranged in hypereosinophilia) | Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex. {ECO:0000269|PubMed:14749727}. |
Q6VMQ6 | ATF7IP | T427 | ochoa | Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621) | Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Required for HUSH-mediated heterochromatin formation and gene silencing (PubMed:27732843). Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1 (PubMed:12665582). Stabilizes SETDB1, is required to stimulate histone methyltransferase activity of SETDB1 and facilitates the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) (PubMed:14536086, PubMed:27732843). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells (PubMed:19106100). {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:27732843}. |
Q6VMQ6 | ATF7IP | T432 | ochoa | Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621) | Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Required for HUSH-mediated heterochromatin formation and gene silencing (PubMed:27732843). Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1 (PubMed:12665582). Stabilizes SETDB1, is required to stimulate histone methyltransferase activity of SETDB1 and facilitates the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) (PubMed:14536086, PubMed:27732843). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells (PubMed:19106100). {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:27732843}. |
Q76G19 | PDZD4 | T662 | ochoa | PDZ domain-containing protein 4 (PDZ domain-containing RING finger protein 4-like protein) | None |
Q7Z2T5 | TRMT1L | T599 | ochoa | tRNA (guanine(27)-N(2))-dimethyltransferase (EC 2.1.1.-) (tRNA methyltransferase 1-like protein) (TRMT1-like protein) | Specifically dimethylates a single guanine residue at position 27 of tRNA(Tyr) using S-adenosyl-L-methionine as donor of the methyl groups (PubMed:39786990, PubMed:39786998). Dimethylation at position 27 of tRNA(Tyr) is required for efficient translation of tyrosine codons (PubMed:39786990, PubMed:39786998). Also required to maintain 3-(3-amino-3-carboxypropyl)uridine (acp3U) in the D-loop of several cytoplasmic tRNAs (PubMed:39786990, PubMed:39786998). {ECO:0000269|PubMed:39786990, ECO:0000269|PubMed:39786998}. |
Q7Z2T5 | TRMT1L | T600 | ochoa | tRNA (guanine(27)-N(2))-dimethyltransferase (EC 2.1.1.-) (tRNA methyltransferase 1-like protein) (TRMT1-like protein) | Specifically dimethylates a single guanine residue at position 27 of tRNA(Tyr) using S-adenosyl-L-methionine as donor of the methyl groups (PubMed:39786990, PubMed:39786998). Dimethylation at position 27 of tRNA(Tyr) is required for efficient translation of tyrosine codons (PubMed:39786990, PubMed:39786998). Also required to maintain 3-(3-amino-3-carboxypropyl)uridine (acp3U) in the D-loop of several cytoplasmic tRNAs (PubMed:39786990, PubMed:39786998). {ECO:0000269|PubMed:39786990, ECO:0000269|PubMed:39786998}. |
Q7Z403 | TMC6 | T60 | ochoa | Transmembrane channel-like protein 6 (Epidermodysplasia verruciformis protein 1) (Protein LAK-4) | Acts as a regulatory protein involved in the regulation of numerous cellular processes (PubMed:18158319, PubMed:30068544, PubMed:32917726). Together with its homolog TMC8/EVER2, forms a complex with CIB1 in lymphocytes and keratynocytes where TMC6 and TMC8 stabilize CIB1 and reciprocally (PubMed:30068544, PubMed:32917726). Together with TMC8, also forms a complex with and activates zinc transporter ZNT1 at the ER membrane of keratynocytes, thereby facilitating zinc uptake into the ER (PubMed:18158319). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319). Also plays a role in thermal sensation by inhibiting the M-channel (KCNQ2-KCNQ3 channel) current in primary sensory neurons (By similarity). {ECO:0000250|UniProtKB:Q7TN60, ECO:0000269|PubMed:18158319, ECO:0000269|PubMed:30068544, ECO:0000269|PubMed:32917726}. |
Q7Z417 | NUFIP2 | T260 | ochoa | FMR1-interacting protein NUFIP2 (82 kDa FMRP-interacting protein) (82-FIP) (Cell proliferation-inducing gene 1 protein) (FMRP-interacting protein 2) (Nuclear FMR1-interacting protein 2) | Binds RNA. {ECO:0000269|PubMed:12837692}. |
Q86V48 | LUZP1 | T725 | 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}. |
Q86X53 | ERICH1 | T259 | ochoa | Glutamate-rich protein 1 | None |
Q8IVF2 | AHNAK2 | T369 | ochoa | Protein AHNAK2 | None |
Q8IWE5 | PLEKHM2 | T286 | ochoa | Pleckstrin homology domain-containing family M member 2 (PH domain-containing family M member 2) (Salmonella-induced filaments A and kinesin-interacting protein) (SifA and kinesin-interacting protein) | Plays a role in lysosomes movement and localization at the cell periphery acting as an effector of ARL8B. Required for ARL8B to exert its effects on lysosome location, recruits kinesin-1 to lysosomes and hence direct their movement toward microtubule plus ends. Binding to ARL8B provides a link from lysosomal membranes to plus-end-directed motility (PubMed:22172677, PubMed:24088571, PubMed:25898167, PubMed:28325809). Critical factor involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). Required for maintenance of the Golgi apparatus organization (PubMed:22172677). May play a role in membrane tubulation (PubMed:15905402). {ECO:0000269|PubMed:15905402, ECO:0000269|PubMed:22172677, ECO:0000269|PubMed:24088571, ECO:0000269|PubMed:25898167, ECO:0000269|PubMed:28325809}. |
Q8IX18 | DHX40 | T50 | ochoa | Probable ATP-dependent RNA helicase DHX40 (EC 3.6.4.13) (DEAH box protein 40) (Protein PAD) | Probable ATP-dependent RNA helicase. {ECO:0000250}. |
Q8N108 | MIER1 | T128 | ochoa | Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) (hMi-er1) | Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269|PubMed:12482978}. |
Q8N344 | MIER2 | T147 | ochoa | Mesoderm induction early response protein 2 (Mi-er2) | Transcriptional repressor. {ECO:0000250}. |
Q8N5D0 | WDTC1 | T652 | ochoa | WD and tetratricopeptide repeats protein 1 | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16964240}. |
Q8NG08 | HELB | T1027 | ochoa | DNA helicase B (hDHB) (EC 3.6.4.12) | 5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection (PubMed:25617833, PubMed:26774285). Recruitment to single-stranded DNA (ssDNA) following DNA damage leads to inhibit the nucleases catalyzing resection, such as EXO1, BLM and DNA2, possibly via the 5'-3' ssDNA translocase activity of HELB (PubMed:26774285). As cells approach S phase, DNA end resection is promoted by the nuclear export of HELB following phosphorylation (PubMed:26774285). Acts independently of TP53BP1 (PubMed:26774285). Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates (PubMed:12181327). During S phase, may facilitate cellular recovery from replication stress (PubMed:22194613). {ECO:0000269|PubMed:12181327, ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:25617833, ECO:0000269|PubMed:26774285}. |
Q8TEK3 | DOT1L | T772 | ochoa | Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (DOT1-like protein) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4) | Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones (PubMed:12123582). Binds to DNA (PubMed:12628190). {ECO:0000269|PubMed:12123582, ECO:0000269|PubMed:12628190}. |
Q8WU17 | RNF139 | T635 | ochoa | E3 ubiquitin-protein ligase RNF139 (EC 2.3.2.27) (RING finger protein 139) (RING-type E3 ubiquitin transferase RNF139) (Translocation in renal carcinoma on chromosome 8 protein) | E3-ubiquitin ligase; acts as a negative regulator of cell proliferation through mechanisms involving G2/M arrest and cell death (PubMed:10500182, PubMed:12032852, PubMed:17016439). Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER) (PubMed:19720873). Affects SREBP processing by hindering the SREBP-SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression (PubMed:19706601, PubMed:20068067). Involved in the sterol-accelerated degradation of HMGCR (PubMed:22143767, PubMed:23223569). This is achieved through binding of RNF139 to INSIG1 and/or INSIG2 at the ER membrane (PubMed:22143767). In addition, interaction of RNF139 with AUP1 facilitates interaction of RNF139 with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase AMFR, leading to ubiquitination of HMGCR (PubMed:23223569). The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction (PubMed:22143767, PubMed:23223569). Required for INSIG1 ubiquitination (PubMed:20068067). May be required for EIF3 complex ubiquitination (PubMed:20068067). {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12032852, ECO:0000269|PubMed:17016439, ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:19720873, ECO:0000269|PubMed:20068067, ECO:0000269|PubMed:22143767, ECO:0000269|PubMed:23223569}. |
Q92539 | LPIN2 | T130 | ochoa | Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2) | Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the endoplasmic reticulum membrane. Plays important roles in controlling the metabolism of fatty acids at different levels. Also acts as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism. {ECO:0000250|UniProtKB:Q99PI5}. |
Q92630 | DYRK2 | T106 | psp | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) | Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro). {ECO:0000269|PubMed:11311121, ECO:0000269|PubMed:12588975, ECO:0000269|PubMed:14593110, ECO:0000269|PubMed:15910284, ECO:0000269|PubMed:16511445, ECO:0000269|PubMed:16611631, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:18455992, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:9748265}. |
Q92734 | TFG | T188 | ochoa | Protein TFG (TRK-fused gene protein) | Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858). {ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:23479643, ECO:0000269|PubMed:27813252}. |
Q92794 | KAT6A | T1119 | ochoa | Histone acetyltransferase KAT6A (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3) (MYST-3) (Monocytic leukemia zinc finger protein) (Runt-related transcription factor-binding protein 2) (Zinc finger protein 220) | Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}. |
Q92973 | TNPO1 | T335 | ochoa | Transportin-1 (Importin beta-2) (Karyopherin beta-2) (M9 region interaction protein) (MIP) | Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:24753571). May 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). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones (By similarity). In vitro, mediates nuclear import of SRP19 (PubMed:11682607). Mediates nuclear import of ADAR/ADAR1 isoform 1 and isoform 5 in a RanGTP-dependent manner (PubMed:19124606, PubMed:24753571). Main mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with the karyopherins KPNA1 and KPNA2 (PubMed:35446349). {ECO:0000250|UniProtKB:Q8BFY9, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:24753571, ECO:0000269|PubMed:35446349, ECO:0000269|PubMed:8986607, ECO:0000269|PubMed:9687515}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:16704975}. |
Q96J84 | KIRREL1 | T558 | 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}. |
Q96KC8 | DNAJC1 | T435 | ochoa | DnaJ homolog subfamily C member 1 (DnaJ protein homolog MTJ1) | May modulate protein synthesis. {ECO:0000250}. |
Q96LZ7 | RMDN2 | T116 | ochoa | Regulator of microtubule dynamics protein 2 (RMD-2) (hRMD-2) (Protein FAM82A1) | None |
Q96MW1 | CCDC43 | T155 | ochoa | Coiled-coil domain-containing protein 43 | None |
Q96QT4 | TRPM7 | T1435 | psp | Transient receptor potential cation channel subfamily M member 7 (EC 2.7.11.1) (Channel-kinase 1) (Long transient receptor potential channel 7) (LTrpC-7) (LTrpC7) [Cleaved into: TRPM7 kinase, cleaved form (M7CK); TRPM7 channel, cleaved form] | Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx (PubMed:11385574, PubMed:12887921, PubMed:15485879, PubMed:24316671, PubMed:35561741, PubMed:36027648). Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation (By similarity). The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7 (PubMed:18365021). In vivo, TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways. In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (PubMed:15485879, PubMed:18394644). {ECO:0000250|UniProtKB:Q923J1, ECO:0000269|PubMed:11385574, ECO:0000269|PubMed:12887921, ECO:0000269|PubMed:15485879, ECO:0000269|PubMed:18365021, ECO:0000269|PubMed:18394644, ECO:0000269|PubMed:24316671, ECO:0000269|PubMed:35561741, ECO:0000269|PubMed:36027648}.; FUNCTION: [TRPM7 channel, cleaved form]: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. {ECO:0000250|UniProtKB:Q923J1}.; FUNCTION: [TRPM7 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development. {ECO:0000250|UniProtKB:Q923J1}. |
Q96T58 | SPEN | T1946 | ochoa | Msx2-interacting protein (SMART/HDAC1-associated repressor protein) (SPEN homolog) | May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250|UniProtKB:Q62504, ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:12374742}. |
Q99459 | CDC5L | T510 | ochoa | Cell division cycle 5-like protein (Cdc5-like protein) (Pombe cdc5-related protein) | DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:11991638, PubMed:20176811, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30705154, PubMed:30728453). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR) (PubMed:20176811). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9468527, ECO:0000269|PubMed:9632794, ECO:0000305|PubMed:33509932}. |
Q99666 | RGPD5 | T1177 | 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 |
Q9BWH6 | RPAP1 | T290 | ochoa | RNA polymerase II-associated protein 1 | Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Required for interaction of the RNA polymerase II complex with acetylated histone H3. {ECO:0000269|PubMed:17643375}. |
Q9BXS5 | AP1M1 | T144 | ochoa | AP-1 complex subunit mu-1 (AP-mu chain family member mu1A) (Adaptor protein complex AP-1 subunit mu-1) (Adaptor-related protein complex 1 subunit mu-1) (Clathrin assembly protein complex 1 mu-1 medium chain 1) (Clathrin coat assembly protein AP47) (Clathrin coat-associated protein AP47) (Golgi adaptor HA1/AP1 adaptin mu-1 subunit) (Mu-adaptin 1) (Mu1A-adaptin) | Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. |
Q9BYW2 | SETD2 | T2051 | ochoa | Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.359) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP) | Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (PubMed:19332550). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (PubMed:23622243). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (PubMed:24843002). Acts as a tumor suppressor (PubMed:24509477). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (PubMed:27317772). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (PubMed:21792193). Required during angiogenesis (By similarity). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (By similarity). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565, PubMed:28753426). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (PubMed:28753426). {ECO:0000250|UniProtKB:E9Q5F9, ECO:0000269|PubMed:16118227, ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:21526191, ECO:0000269|PubMed:21792193, ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:23325844, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:24509477, ECO:0000269|PubMed:24843002, ECO:0000269|PubMed:27317772, ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:27518565, ECO:0000269|PubMed:28753426}.; FUNCTION: (Microbial infection) Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. {ECO:0000269|PubMed:11461154}. |
Q9H2G2 | SLK | T545 | ochoa | 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}. |
Q9H2Y7 | ZNF106 | T1478 | 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}. |
Q9H9C1 | VIPAS39 | T21 | ochoa | Spermatogenesis-defective protein 39 homolog (hSPE-39) (VPS33B-interacting protein in apical-basolateral polarity regulator) (VPS33B-interacting protein in polarity and apical restriction) | Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity). {ECO:0000250|UniProtKB:Q23288, ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:20190753}. |
Q9NP97 | DYNLRB1 | T40 | ochoa | Dynein light chain roadblock-type 1 (Bithoraxoid-like protein) (BLP) (Dynein light chain 2A, cytoplasmic) (Dynein-associated protein Km23) (Roadblock domain-containing protein 1) | Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. {ECO:0000305|PubMed:36071160}. |
Q9NQ84 | GPRC5C | T326 | ochoa | G-protein coupled receptor family C group 5 member C (Retinoic acid-induced gene 3 protein) (RAIG-3) | This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways. {ECO:0000250}. |
Q9NRC8 | SIRT7 | T153 | psp | NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7) | NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context (PubMed:22722849, PubMed:26907567, PubMed:30653310, PubMed:31542297, PubMed:35939806). Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac) (PubMed:22722849, PubMed:30420520, PubMed:35939806). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression (PubMed:22722849, PubMed:30653310). H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor (PubMed:22722849). Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells (PubMed:22722849). Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes (PubMed:30653310). Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 (PubMed:24207024, PubMed:26867678, PubMed:28147277, PubMed:28426094, PubMed:28790157, PubMed:28886238, PubMed:30540930, PubMed:30944854, PubMed:31075303). Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex (PubMed:16618798, PubMed:19174463, PubMed:24207024). Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:16618798, PubMed:19174463, PubMed:24207024). In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription (PubMed:24207024). Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis (PubMed:19174463). Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex (PubMed:26867678). Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65 (PubMed:31075303). Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation (PubMed:30944854). Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B) (PubMed:28886238). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PubMed:28426094). Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (PubMed:30540930). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51 (PubMed:28147277). Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase (PubMed:27436229, PubMed:27997115, PubMed:31542297). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (PubMed:27436229). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ) (By similarity). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina (PubMed:31226208). Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (PubMed:29728458). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity). {ECO:0000250|UniProtKB:Q8BKJ9, ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:19174463, ECO:0000269|PubMed:22722849, ECO:0000269|PubMed:24207024, ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:26907567, ECO:0000269|PubMed:27436229, ECO:0000269|PubMed:27997115, ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:28426094, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:28886238, ECO:0000269|PubMed:29728458, ECO:0000269|PubMed:30420520, ECO:0000269|PubMed:30540930, ECO:0000269|PubMed:30653310, ECO:0000269|PubMed:30944854, ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:31226208, ECO:0000269|PubMed:31542297, ECO:0000269|PubMed:35939806}. |
Q9NSK0 | KLC4 | T444 | ochoa | Kinesin light chain 4 (KLC 4) (Kinesin-like protein 8) | Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}. |
Q9NV58 | RNF19A | T492 | ochoa | E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.31) (Double ring-finger protein) (Dorfin) (RING finger protein 19A) (p38) | E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection. {ECO:0000269|PubMed:11237715, ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12750386, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16513638}. |
Q9NVM1 | EVA1B | T94 | ochoa | Protein eva-1 homolog B (Protein FAM176B) | None |
Q9NVS9 | PNPO | T238 | ochoa | Pyridoxine-5'-phosphate oxidase (EC 1.4.3.5) (Pyridoxamine-phosphate oxidase) | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000269|PubMed:12824491, ECO:0000269|PubMed:15182361, ECO:0000269|PubMed:15772097}. |
Q9NWH9 | SLTM | T69 | ochoa | SAFB-like transcription modulator (Modulator of estrogen-induced transcription) | When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000250}. |
Q9NWH9 | SLTM | T205 | ochoa | SAFB-like transcription modulator (Modulator of estrogen-induced transcription) | When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000250}. |
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}. |
Q9NZN5 | ARHGEF12 | T736 | ochoa | Rho guanine nucleotide exchange factor 12 (Leukemia-associated RhoGEF) | May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. {ECO:0000269|PubMed:11094164}. |
Q9UBW8 | COPS7A | T223 | ochoa | COP9 signalosome complex subunit 7a (SGN7a) (Signalosome subunit 7a) (Dermal papilla-derived protein 10) (JAB1-containing signalosome subunit 7a) | Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}. |
Q9UDY2 | TJP2 | T707 | ochoa | Tight junction protein 2 (Tight junction protein ZO-2) (Zona occludens protein 2) (Zonula occludens protein 2) | Plays a role in tight junctions and adherens junctions (By similarity). Acts as a positive regulator of RANKL-induced osteoclast differentiation, potentially via mediating downstream transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q9Z0U1}. |
Q9UHG3 | PCYOX1 | T402 | ochoa | Prenylcysteine oxidase 1 (EC 1.8.3.5) (Prenylcysteine lyase) | Prenylcysteine oxidase that cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (PubMed:10585463, PubMed:11078725, PubMed:12186880). Only active against free prenylcysteines and not prenylcysteine residues within prenylated proteins or peptides (By similarity). Involved in the final step in the degradation of prenylated proteins, by degrading prenylcysteines after the protein has been degraded (PubMed:10585463). {ECO:0000250|UniProtKB:F1N2K1, ECO:0000269|PubMed:10585463, ECO:0000269|PubMed:11078725, ECO:0000269|PubMed:12186880}. |
Q9UK61 | TASOR | T921 | ochoa | Protein TASOR (CTCL tumor antigen se89-1) (Retinoblastoma-associated protein RAP140) (Transgene activation suppressor protein) | Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Plays a crucial role in early embryonic development (By similarity). Involved in the organization of spindle poles and spindle apparatus assembly during zygotic division (By similarity). Plays an important role in maintaining epiblast fitness or potency (By similarity). {ECO:0000250|UniProtKB:Q69ZR9, ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:29211708, ECO:0000269|PubMed:30487602}. |
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}. |
Q9UKV3 | ACIN1 | T910 | ochoa | Apoptotic chromatin condensation inducer in the nucleus (Acinus) | Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269|PubMed:10490026, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}. |
Q9UKV3 | ACIN1 | T978 | ochoa | Apoptotic chromatin condensation inducer in the nucleus (Acinus) | Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269|PubMed:10490026, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}. |
Q9ULV3 | CIZ1 | T786 | ochoa | Cip1-interacting zinc finger protein (CDKN1A-interacting zinc finger protein 1) (Nuclear protein NP94) (Zinc finger protein 356) | May regulate the subcellular localization of CIP/WAF1. |
Q9UMZ2 | SYNRG | T767 | ochoa | Synergin gamma (AP1 subunit gamma-binding protein 1) (Gamma-synergin) | Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025, ECO:0000305|PubMed:12538641}. |
Q9UPN9 | TRIM33 | T1102 | ochoa | E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RET-fused gene 7 protein) (Protein Rfg7) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33) | Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade). {ECO:0000250, ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}. |
Q9UPQ7 | PDZRN3 | T959 | ochoa | E3 ubiquitin-protein ligase PDZRN3 (EC 2.3.2.27) (Ligand of Numb protein X 3) (PDZ domain-containing RING finger protein 3) (RING-type E3 ubiquitin transferase PDZRN3) (Semaphorin cytoplasmic domain-associated protein 3) (Protein SEMACAP3) | E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation. {ECO:0000250|UniProtKB:Q69ZS0}. |
Q9UPT8 | ZC3H4 | T72 | ochoa | Zinc finger CCCH domain-containing protein 4 | RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein (PubMed:33767452, PubMed:33913806). Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452, PubMed:33913806). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs (PubMed:33767452). {ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806}. |
Q9UQ88 | CDK11A | T436 | ochoa | Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2) | Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}. |
Q9Y232 | CDYL | T92 | ochoa | Chromodomain Y-like protein (CDY-like) (Crotonyl-CoA hydratase) (EC 4.2.1.-) | [Isoform 2]: Chromatin reader protein that recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) (PubMed:19808672, PubMed:28402439). Part of multimeric repressive chromatin complexes, where it is required for transmission and restoration of repressive histone marks, thereby preserving the epigenetic landscape (PubMed:28402439). Required for chromatin targeting and maximal enzymatic activity of Polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes (PubMed:22009739). Acts as a corepressor for REST by facilitating histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression (PubMed:19061646). Involved in X chromosome inactivation in females: recruited to Xist RNA-coated X chromosome and facilitates propagation of H3K9me2 by anchoring EHMT2 (By similarity). Promotes EZH2 accumulation and H3K27me3 methylation at DNA double strand breaks (DSBs), thereby facilitating transcriptional repression at sites of DNA damage and homology-directed repair of DSBs (PubMed:29177481). Required for neuronal migration during brain development by repressing expression of RHOA (By similarity). By repressing the expression of SCN8A, contributes to the inhibition of intrinsic neuronal excitability and epileptogenesis (By similarity). In addition to acting as a chromatin reader, acts as a hydro-lyase (PubMed:28803779). Shows crotonyl-coA hydratase activity by mediating the conversion of crotonyl-CoA ((2E)-butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), thereby acting as a negative regulator of histone crotonylation (PubMed:28803779). Histone crotonylation is required during spermatogenesis; down-regulation of histone crotonylation by CDYL regulates the reactivation of sex chromosome-linked genes in round spermatids and histone replacement in elongating spermatids (By similarity). By regulating histone crotonylation and trimethylation of H3K27, may be involved in stress-induced depression-like behaviors, possibly by regulating VGF expression (By similarity). {ECO:0000250|UniProtKB:Q9WTK2, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19808672, ECO:0000269|PubMed:22009739, ECO:0000269|PubMed:28402439, ECO:0000269|PubMed:28803779, ECO:0000269|PubMed:29177481}.; FUNCTION: [Isoform 1]: Not able to recognize and bind histone H3K9me3, histone H3K27me2 and histone H3K27me3, due to the presence of a N-terminal extension that inactivates the chromo domain (PubMed:19808672). {ECO:0000269|PubMed:19808672}.; FUNCTION: [Isoform 3]: Not able to recognize and bind histone H3K9me3, histone H3K27me2 and histone H3K27me3, due to the absence of the chromo domain (PubMed:19808672). Acts as a negative regulator of isoform 2 by displacing isoform 2 from chromatin. {ECO:0000269|PubMed:19808672}. |
Q9Y2L9 | LRCH1 | T391 | ochoa | Leucine-rich repeat and calponin homology domain-containing protein 1 (Calponin homology domain-containing protein 1) (Neuronal protein 81) (NP81) | Acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. Probably by preventing CDC42 activation, negatively regulates CD4(+) T-cell migration. {ECO:0000269|PubMed:28028151}. |
Q9Y2T7 | YBX2 | T124 | ochoa | Y-box-binding protein 2 (Contrin) (DNA-binding protein C) (Dbpc) (Germ cell-specific Y-box-binding protein) (MSY2 homolog) | Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity). {ECO:0000250|UniProtKB:Q9Z2C8}. |
Q9Y2X3 | NOP58 | T435 | ochoa | Nucleolar protein 58 (Nucleolar protein 5) | Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (PubMed:15574333, PubMed:17636026, PubMed:19620283, PubMed:34516797). 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:39570315). {ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:39570315}. |
Q9Y478 | PRKAB1 | T80 | psp | 5'-AMP-activated protein kinase subunit beta-1 (AMPK subunit beta-1) (AMPKb) | Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). |
Q9Y485 | DMXL1 | T1383 | ochoa | DmX-like protein 1 (X-like 1 protein) | None |
Q9Y4F5 | CEP170B | T571 | ochoa | Centrosomal protein of 170 kDa protein B (Centrosomal protein 170B) (Cep170B) | Plays a role in microtubule organization. {ECO:0000250|UniProtKB:Q5SW79}. |
Q9Y5B9 | SUPT16H | T190 | 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}. |
Q9Y623 | MYH4 | T758 | ochoa | Myosin-4 (Myosin heavy chain 2b) (MyHC-2b) (Myosin heavy chain 4) (Myosin heavy chain IIb) (MyHC-IIb) (Myosin heavy chain, skeletal muscle, fetal) | Muscle contraction. |
Q9Y6K1 | DNMT3A | T138 | ochoa | DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase HsaIIIA) (DNA MTase HsaIIIA) (M.HsaIIIA) | Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:12138111, PubMed:16357870, PubMed:30478443). DNA methylation is coordinated with methylation of histones (PubMed:12138111, PubMed:16357870, PubMed:30478443). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:12138111, PubMed:16357870, PubMed:30478443). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (By similarity). Plays a role in paternal and maternal imprinting (By similarity). Required for methylation of most imprinted loci in germ cells (By similarity). Acts as a transcriptional corepressor for ZBTB18 (By similarity). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (By similarity). Can actively repress transcription through the recruitment of HDAC activity (By similarity). Also has weak auto-methylation activity on Cys-710 in absence of DNA (By similarity). {ECO:0000250|UniProtKB:O88508, ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:30478443}. |
Q9Y6X8 | ZHX2 | T37 | ochoa | Zinc fingers and homeoboxes protein 2 (Alpha-fetoprotein regulator 1) (AFP regulator 1) (Regulator of AFP) (Zinc finger and homeodomain protein 2) | Acts as a transcriptional repressor (PubMed:12741956). Represses the promoter activity of the CDC25C gene stimulated by NFYA (PubMed:12741956). May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells (By similarity). In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex (By similarity). {ECO:0000250|UniProtKB:Q8C0C0, ECO:0000269|PubMed:12741956}. |
Q02543 | RPL18A | T107 | Sugiyama | Large ribosomal subunit protein eL20 (60S ribosomal protein L18a) | 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}. |
Q96G46 | DUS3L | T99 | Sugiyama | tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like (EC 1.3.1.89) (mRNA-dihydrouridine synthase DUS3L) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3-like) | Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs) (PubMed:34556860). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs (PubMed:34556860). Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regulating their translation (PubMed:34556860). {ECO:0000269|PubMed:34556860}. |
P06733 | ENO1 | T55 | Sugiyama | 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}. |
P04632 | CAPNS1 | T143 | Sugiyama | Calpain small subunit 1 (CSS1) (Calcium-activated neutral proteinase small subunit) (CANP small subunit) (Calcium-dependent protease small subunit) (CDPS) (Calcium-dependent protease small subunit 1) (Calpain regulatory subunit) | Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:O88456}. |
P50991 | CCT4 | T69 | Sugiyama | T-complex protein 1 subunit delta (TCP-1-delta) (EC 3.6.1.-) (CCT-delta) (Chaperonin containing T-complex polypeptide 1 subunit 4) (Stimulator of TAR RNA-binding) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
P61254 | RPL26 | T94 | Sugiyama | Large ribosomal subunit protein uL24 (60S ribosomal protein L26) | Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:26100019}. |
Q00839 | HNRNPU | T532 | 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}. |
Q9UNX3 | RPL26L1 | T94 | Sugiyama | Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) | None |
P62899 | RPL31 | T107 | 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}. |
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}. |
O96019 | ACTL6A | T67 | Sugiyama | Actin-like protein 6A (53 kDa BRG1-associated factor A) (Actin-related protein Baf53a) (ArpNbeta) (BRG1-associated factor 53A) (BAF53A) (INO80 complex subunit K) | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250|UniProtKB:Q9Z2N8, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:15196461, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. |
P22314 | UBA1 | T233 | Sugiyama | Ubiquitin-like modifier-activating enzyme 1 (EC 6.2.1.45) (Protein A1S9) (Ubiquitin-activating enzyme E1) | Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1447181, PubMed:1606621, PubMed:33108101). Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:1447181). Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (PubMed:22456334). {ECO:0000269|PubMed:1447181, ECO:0000269|PubMed:1606621, ECO:0000269|PubMed:22456334, ECO:0000269|PubMed:33108101}. |
Q92598 | HSPH1 | T795 | Sugiyama | Heat shock protein 105 kDa (Antigen NY-CO-25) (Heat shock 110 kDa protein) (Heat shock protein family H member 1) | Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed:24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity). {ECO:0000250|UniProtKB:Q60446, ECO:0000250|UniProtKB:Q61699, ECO:0000269|PubMed:24318877}. |
P23284 | PPIB | T108 | Sugiyama | Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP) | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. {ECO:0000269|PubMed:20676357}. |
P33176 | KIF5B | T182 | Sugiyama | Kinesin-1 heavy chain (Conventional kinesin heavy chain) (Ubiquitous kinesin heavy chain) (UKHC) | Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (PubMed:20386726). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends (Probable). Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). {ECO:0000250|UniProtKB:Q2PQA9, ECO:0000250|UniProtKB:Q61768, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:24088571, ECO:0000305|PubMed:22172677, ECO:0000305|PubMed:24088571}. |
P07237 | P4HB | T453 | 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}. |
P11142 | HSPA8 | T37 | Sugiyama | Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Heat shock protein family A member 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity). {ECO:0000250|UniProtKB:P19120, ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:11559757, ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:15894275, ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:27916661, ECO:0000269|PubMed:2799391, ECO:0000269|PubMed:36586411, ECO:0000303|PubMed:24121476, ECO:0000303|PubMed:26865365}. |
P34931 | HSPA1L | T39 | Sugiyama | Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa protein 1-Hom) (HSP70-Hom) (Heat shock protein family A member 1L) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810). {ECO:0000269|PubMed:24270810, ECO:0000303|PubMed:26865365}. |
P54652 | HSPA2 | T38 | Sugiyama | Heat shock-related 70 kDa protein 2 (Heat shock 70 kDa protein 2) (Heat shock protein family A member 2) | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity). {ECO:0000250|UniProtKB:P17156, ECO:0000303|PubMed:26865365}. |
P52907 | CAPZA1 | T249 | Sugiyama | F-actin-capping protein subunit alpha-1 (CapZ alpha-1) | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (PubMed:22891260). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250|UniProtKB:A0PFK5, ECO:0000269|PubMed:22891260}. |
P00558 | PGK1 | T369 | Sugiyama | 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}. |
P04150 | NR3C1 | T519 | PSP | Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) | Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:25775514, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:28139699, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9590696}.; FUNCTION: [Isoform Alpha]: Has transcriptional activation and repression activity (PubMed:11435610, PubMed:15769988, PubMed:15866175, PubMed:17635946, PubMed:19141540, PubMed:19248771, PubMed:20484466, PubMed:21664385, PubMed:23820903). Mediates glucocorticoid-induced apoptosis (PubMed:23303127). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:21664385, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903, ECO:0000269|PubMed:25847991}.; FUNCTION: [Isoform Beta]: Acts as a dominant negative inhibitor of isoform Alpha (PubMed:20484466, PubMed:7769088, PubMed:8621628). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (PubMed:19248771, PubMed:26711253). Loses this transcription modulator function on its own (PubMed:20484466). Has no hormone-binding activity (PubMed:8621628). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (PubMed:26711253). Directly regulates STAT1 expression in isoform Alpha-independent manner (PubMed:26711253). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:26711253, ECO:0000269|PubMed:7769088, ECO:0000269|PubMed:8621628}.; FUNCTION: [Isoform Alpha-2]: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism (PubMed:20484466).; FUNCTION: [Isoform GR-P]: Increases activity of isoform Alpha. {ECO:0000269|PubMed:11358809}.; FUNCTION: [Isoform Alpha-B]: More effective than isoform Alpha in transcriptional activation, but not repression activity. {ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform 10]: Has transcriptional activation activity. {ECO:0000269|PubMed:20484466}.; FUNCTION: [Isoform Alpha-C1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-C3]: Has highest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). Mediates glucocorticoid-induced apoptosis (PubMed:23303127, PubMed:23820903). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}.; FUNCTION: [Isoform Alpha-D1]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D2]: Has transcriptional activation activity. {ECO:0000269|PubMed:15866175}.; FUNCTION: [Isoform Alpha-D3]: Has lowest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). {ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}. |
P43034 | PAFAH1B1 | T247 | Sugiyama | Platelet-activating factor acetylhydrolase IB subunit beta (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha) | Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (PubMed:22956769). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:22956769}. |
P62269 | RPS18 | T69 | Sugiyama | Small ribosomal subunit protein uS13 (40S ribosomal protein S18) (Ke-3) (Ke3) | Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000269|PubMed:23636399}. |
Q14204 | DYNC1H1 | T4218 | Sugiyama | Cytoplasmic dynein 1 heavy chain 1 (Cytoplasmic dynein heavy chain 1) (Dynein heavy chain, cytosolic) | Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074). {ECO:0000269|PubMed:27462074}. |
Q16658 | FSCN1 | T79 | Sugiyama | Fascin (55 kDa actin-bundling protein) (Singed-like protein) (p55) | Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:23184945, ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}. |
Q9BV20 | MRI1 | T351 | Sugiyama | Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (Mediator of RhoA-dependent invasion) (S-methyl-5-thioribose-1-phosphate isomerase) (Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein) | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:19620624}. |
P14866 | HNRNPL | T282 | Sugiyama | Heterogeneous nuclear ribonucleoprotein L (hnRNP L) | Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8. {ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:22570490, ECO:0000269|PubMed:25623890, ECO:0000269|PubMed:26051023, ECO:0000269|PubMed:2687284, ECO:0000269|PubMed:33174841, ECO:0000269|PubMed:36537238}. |
P35579 | MYH9 | T156 | Sugiyama | Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) | Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1 envelope glycoprotein B. {ECO:0000269|PubMed:20944748, ECO:0000269|PubMed:39048823}. |
Q96RP9 | GFM1 | T727 | Sugiyama | Elongation factor G, mitochondrial (EF-Gmt) (EC 3.6.5.-) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (hEFG1) | Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:19716793}. |
Q8NDI1 | EHBP1 | T1070 | Sugiyama | EH domain-binding protein 1 | May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking (PubMed:14676205, PubMed:27552051). Required for perinuclear sorting and insulin-regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity). {ECO:0000250|UniProtKB:Q69ZW3, ECO:0000269|PubMed:14676205, ECO:0000305|PubMed:27552051}. |
Q99798 | ACO2 | T543 | Sugiyama | Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250|UniProtKB:P16276}. |
Q13228 | SELENBP1 | T36 | Sugiyama | Methanethiol oxidase (MTO) (EC 1.8.3.4) (56 kDa selenium-binding protein) (SBP56) (SP56) (Selenium-binding protein 1) | Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria (PubMed:29255262). Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). {ECO:0000250|UniProtKB:Q8VIF7, ECO:0000269|PubMed:29255262}. |
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}. |
P04075 | ALDOA | T65 | 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}. |
P52948 | NUP98 | T743 | Sugiyama | Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)] | Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}.; FUNCTION: (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed:23523133). {ECO:0000269|PubMed:23523133}. |
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}. |
Q9Y624 | F11R | T70 | iPTMNet|EPSD | Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (Platelet F11 receptor) (Platelet adhesion molecule 1) (PAM-1) (CD antigen CD321) | Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11489913). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992). Involved in platelet activation (PubMed:10753840). {ECO:0000250|UniProtKB:O88792, ECO:0000269|PubMed:10753840, ECO:0000269|PubMed:11489913, ECO:0000269|PubMed:11812992}.; FUNCTION: (Microbial infection) Acts as a receptor for Mammalian reovirus sigma-1. {ECO:0000269|PubMed:11239401}.; FUNCTION: (Microbial infection) Acts as a receptor for Human Rotavirus strain Wa. {ECO:0000269|PubMed:25481868}. |
Q07020 | RPL18 | T87 | Sugiyama | Large ribosomal subunit protein eL18 (60S ribosomal protein L18) | Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. |
P23458 | JAK1 | T901 | Sugiyama | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1) | Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). Kinase partner for the interleukin (IL)-2 receptor (PubMed:11909529) as well as interleukin (IL)-10 receptor (PubMed:12133952). Kinase partner for the type I interferon receptor IFNAR2 (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins (PubMed:7759950). Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors (PubMed:16239216, PubMed:32750333, PubMed:8232552). {ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12133952, ECO:0000269|PubMed:16239216, ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7657660, ECO:0000269|PubMed:8232552}. |
Q96EK9 | KTI12 | T189 | Sugiyama | Protein KTI12 homolog | None |
O43776 | NARS1 | T503 | Sugiyama | Asparagine--tRNA ligase, cytoplasmic (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) (Asparaginyl-tRNA synthetase 1) | Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (PubMed:32738225, PubMed:32788587, PubMed:9421509). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells (PubMed:12235211, PubMed:30171954). Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells (PubMed:32788587). {ECO:0000269|PubMed:12235211, ECO:0000269|PubMed:30171954, ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509}. |
P43034 | PAFAH1B1 | T139 | Sugiyama | Platelet-activating factor acetylhydrolase IB subunit beta (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha) | Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (PubMed:22956769). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:22956769}. |
P50395 | GDI2 | T407 | Sugiyama | Rab GDP dissociation inhibitor beta (Rab GDI beta) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) | GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking (PubMed:25860027). Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A (PubMed:25860027). {ECO:0000269|PubMed:25860027}. |
O00541 | PES1 | T365 | Sugiyama | Pescadillo homolog | Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269}. |
P29597 | TYK2 | T919 | Sugiyama | Non-receptor tyrosine-protein kinase TYK2 (EC 2.7.10.2) | Tyrosine kinase of the non-receptor type involved in numerous cytokines and interferons signaling, which regulates cell growth, development, cell migration, innate and adaptive immunity (PubMed:10542297, PubMed:10995743, PubMed:7657660, PubMed:7813427, PubMed:8232552). Plays both structural and catalytic roles in numerous interleukins and interferons (IFN-alpha/beta) signaling (PubMed:10542297). Associates with heterodimeric cytokine receptor complexes and activates STAT family members including STAT1, STAT3, STAT4 or STAT6 (PubMed:10542297, PubMed:7638186). The heterodimeric cytokine receptor complexes are composed of (1) a TYK2-associated receptor chain (IFNAR1, IL12RB1, IL10RB or IL13RA1), and (2) a second receptor chain associated either with JAK1 or JAK2 (PubMed:10542297, PubMed:25762719, PubMed:7526154, PubMed:7813427). In response to cytokine-binding to receptors, phosphorylates and activates receptors (IFNAR1, IL12RB1, IL10RB or IL13RA1), creating docking sites for STAT members (PubMed:7526154, PubMed:7657660). In turn, recruited STATs are phosphorylated by TYK2 (or JAK1/JAK2 on the second receptor chain), form homo- and heterodimers, translocate to the nucleus, and regulate cytokine/growth factor responsive genes (PubMed:10542297, PubMed:25762719, PubMed:7657660). Negatively regulates STAT3 activity by promototing phosphorylation at a specific tyrosine that differs from the site used for signaling (PubMed:29162862). {ECO:0000269|PubMed:10542297, ECO:0000269|PubMed:10995743, ECO:0000269|PubMed:25762719, ECO:0000269|PubMed:29162862, ECO:0000269|PubMed:7526154, ECO:0000269|PubMed:7638186, ECO:0000269|PubMed:7657660, ECO:0000269|PubMed:7813427, ECO:0000269|PubMed:8232552}. |
P08174 | CD55 | T102 | Sugiyama | Complement decay-accelerating factor (CD antigen CD55) | This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade (PubMed:7525274). Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage (PubMed:28657829). {ECO:0000269|PubMed:7525274, ECO:0000305|PubMed:28657829}.; FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus A21, coxsackieviruses B1, B3 and B5. {ECO:0000269|PubMed:9151867}.; FUNCTION: (Microbial infection) Acts as a receptor for Human enterovirus 70 and D68 (Probable). {ECO:0000269|PubMed:8764022}.; FUNCTION: (Microbial infection) Acts as a receptor for Human echoviruses 6, 7, 11, 12, 20 and 21. {ECO:0000269|PubMed:7525274, ECO:0000305|PubMed:12409401}. |
P40227 | CCT6A | T147 | Sugiyama | T-complex protein 1 subunit zeta (TCP-1-zeta) (EC 3.6.1.-) (Acute morphine dependence-related protein 2) (CCT-zeta-1) (Chaperonin containing T-complex polypeptide 1 subunit 6A) (HTR3) (Tcp20) | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). {ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:35449234, ECO:0000269|PubMed:36493755, ECO:0000269|PubMed:37193829}. |
Q12792 | TWF1 | T164 | Sugiyama | Twinfilin-1 (Protein A6) (Protein tyrosine kinase 9) | Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). {ECO:0000250}. |
Q66K64 | DCAF15 | T184 | Sugiyama | DDB1- and CUL4-associated factor 15 | Substrate-recognition component of the DCX(DCAF15) complex, a cullin-4-RING E3 ubiquitin-protein ligase complex that mediates ubiquitination and degradation of target proteins (PubMed:16949367, PubMed:31452512). The DCX(DCAF15) complex acts as a regulator of the natural killer (NK) cells effector functions, possibly by mediating ubiquitination and degradation of cohesin subunits SMC1A and SMC3 (PubMed:31452512). May play a role in the activation of antigen-presenting cells (APC) and their interaction with NK cells (PubMed:31452512). {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:31452512}.; FUNCTION: Binding of aryl sulfonamide anticancer drugs, such as indisulam (E7070) or E7820, change the substrate specificity of the DCX(DCAF15) complex, leading to promote ubiquitination and degradation of splicing factor RBM39 (PubMed:28302793, PubMed:28437394, PubMed:31452512, PubMed:31693891). RBM39 degradation results in splicing defects and death in cancer cell lines (PubMed:28302793, PubMed:28437394, PubMed:31693891). Aryl sulfonamide anticancer drugs change the substrate specificity of DCAF15 by acting as a molecular glue that promotes binding between DCAF15 and weak affinity interactor RBM39 (PubMed:31686031, PubMed:31819272). Aryl sulfonamide anticancer drugs also promote ubiquitination and degradation of RBM23 and PRPF39 (PubMed:31626998, PubMed:31686031, PubMed:31693891). {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31626998, ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31693891, ECO:0000269|PubMed:31819272}. |
P20073 | ANXA7 | T203 | Sugiyama | Annexin A7 (Annexin VII) (Annexin-7) (Synexin) | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. |
Q9NZL9 | MAT2B | T34 | Sugiyama | Methionine adenosyltransferase 2 subunit beta (Methionine adenosyltransferase II beta) (MAT II beta) (Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase) | Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine (PubMed:10644686, PubMed:23189196, PubMed:25075345). Can bind NADP (in vitro) (PubMed:23189196, PubMed:23425511). {ECO:0000269|PubMed:10644686, ECO:0000269|PubMed:23189196, ECO:0000269|PubMed:23425511, ECO:0000269|PubMed:25075345}. |
O75369 | FLNB | T1579 | Sugiyama | Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP) | Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro. |
P33981 | TTK | T210 | SIGNOR|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}. |
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}. |
P30419 | NMT1 | T122 | Sugiyama | Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (HsNMT1) (NMT 1) (Type I N-myristoyltransferase) (Peptide N-myristoyltransferase 1) (Protein-lysine myristoyltransferase NMT1) (EC 2.3.1.-) | Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (PubMed:22865860, PubMed:25255805, PubMed:32686708, PubMed:34999170, PubMed:9353336, PubMed:9506952). Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (PubMed:32103017, PubMed:32111831). Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle (PubMed:32103017). {ECO:0000269|PubMed:22865860, ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831, ECO:0000269|PubMed:32686708, ECO:0000269|PubMed:34999170, ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952}. |
Q14677 | CLINT1 | T265 | Sugiyama | Clathrin interactor 1 (Clathrin-interacting protein localized in the trans-Golgi region) (Clint) (Enthoprotin) (Epsin-4) (Epsin-related protein) (EpsinR) | Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}. |
P41208 | CETN2 | T47 | Sugiyama | 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}. |
P02786 | TFRC | T362 | Sugiyama | Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (T9) (p90) (CD antigen CD71) [Cleaved into: Transferrin receptor protein 1, serum form (sTfR)] | Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity). {ECO:0000250|UniProtKB:Q62351, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:26642240, ECO:0000269|PubMed:3568132}.; FUNCTION: (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus. {ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:18268337}.; FUNCTION: (Microbial infection) Acts as a host entry factor for rabies virus that hijacks the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762, ECO:0000269|PubMed:36779763}.; FUNCTION: (Microbial infection) Acts as a host entry factor for SARS-CoV, MERS-CoV and SARS-CoV-2 viruses that hijack the endocytosis of TFRC to enter cells. {ECO:0000269|PubMed:36779762}. |
P13667 | PDIA4 | T503 | Sugiyama | Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72) | None |
P61758 | VBP1 | T171 | Sugiyama | Prefoldin subunit 3 (HIBBJ46) (von Hippel-Lindau-binding protein 1) (VBP-1) (VHL-binding protein 1) | Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}. |
Q16881 | TXNRD1 | T454 | Sugiyama | Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Peroxidase TXNRD1) (EC 1.11.1.2) (Thioredoxin reductase TR1) | Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437). {ECO:0000269|PubMed:10849437, ECO:0000269|PubMed:8577704, ECO:0000305|PubMed:17512005}.; FUNCTION: [Isoform 1]: Induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. {ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704}.; FUNCTION: [Isoform 4]: Enhances the transcriptional activity of estrogen receptors ESR1 and ESR2. {ECO:0000269|PubMed:15199063}.; FUNCTION: [Isoform 5]: Enhances the transcriptional activity of the estrogen receptor ESR2 only (PubMed:15199063). Mediates cell death induced by a combination of interferon-beta and retinoic acid (PubMed:9774665). {ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:9774665}. |
Q96SU4 | OSBPL9 | T673 | Sugiyama | Oxysterol-binding protein-related protein 9 (ORP-9) (OSBP-related protein 9) | Interacts with OSBPL11 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189). {ECO:0000269|PubMed:39106189}. |
P09104 | ENO2 | T19 | Sugiyama | Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE) | Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}. |
Q14289 | PTK2B | T149 | Sugiyama | Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK) | Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:15050747, ECO:0000269|PubMed:15166227, ECO:0000269|PubMed:17634955, ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:18339875, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18765415, ECO:0000269|PubMed:19086031, ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:19244237, ECO:0000269|PubMed:19428251, ECO:0000269|PubMed:19648005, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20001213, ECO:0000269|PubMed:20381867, ECO:0000269|PubMed:20521079, ECO:0000269|PubMed:21357692, ECO:0000269|PubMed:21533080, ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:8670418, ECO:0000269|PubMed:8849729}. |
Q99615 | DNAJC7 | T445 | 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}. |
P62899 | RPL31 | T59 | 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}. |
Q7L014 | DDX46 | T721 | Sugiyama | Probable ATP-dependent RNA helicase DDX46 (EC 3.6.4.13) (DEAD box protein 46) (PRP5 homolog) | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:32494006, PubMed:34822310, PubMed:36797247). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, DDX46 plays essential roles during assembly of pre-spliceosome and proofreading of the branch site (PubMed:34822310). {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:36797247}. |
Q05682 | CALD1 | T124 | Sugiyama | 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}. |
O60488 | ACSL4 | T508 | Sugiyama | Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4) | Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590). {ECO:0000250|UniProtKB:O35547, ECO:0000269|PubMed:21242590, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233}. |
P20810 | CAST | T334 | Sugiyama | Calpastatin (Calpain inhibitor) (Sperm BS-17 component) | Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue. |
Q5T3I0 | GPATCH4 | T356 | Sugiyama | G patch domain-containing protein 4 | None |
O15371 | EIF3D | T229 | Sugiyama | Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66) | mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (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:18599441, PubMed:25849773). 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). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815). {ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}. |
P01893 | HLA-H | T264 | Sugiyama | Putative HLA class I histocompatibility antigen, alpha chain H (HLA-12.4) (HLA-AR) (MHC class I antigen H) | Involved in the presentation of foreign antigens to the immune system. |
Q00688 | FKBP3 | T103 | Sugiyama | Peptidyl-prolyl cis-trans isomerase FKBP3 (PPIase FKBP3) (EC 5.2.1.8) (25 kDa FK506-binding protein) (25 kDa FKBP) (FKBP-25) (FK506-binding protein 3) (FKBP-3) (Immunophilin FKBP25) (Rapamycin-selective 25 kDa immunophilin) (Rotamase) | FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins. |
Q9P2K8 | EIF2AK4 | T462 | Sugiyama | eIF-2-alpha kinase GCN2 (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 4) (GCN2-like protein) | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (PubMed:25329545, PubMed:32610081). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:32610081). Binds uncharged tRNAs (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442, ECO:0000250|UniProtKB:Q9QZ05, ECO:0000269|PubMed:25329545, ECO:0000269|PubMed:26102367, ECO:0000269|PubMed:32610081}.; FUNCTION: (Microbial infection) Plays a role in modulating the adaptive immune response to yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation (PubMed:24310610). {ECO:0000269|PubMed:24310610}. |
P25705 | ATP5F1A | T225 | Sugiyama | ATP synthase F(1) complex subunit alpha, mitochondrial (ATP synthase F1 subunit alpha) | Subunit alpha, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed:37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159). {ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:30146159, ECO:0000269|PubMed:37244256, ECO:0000305|PubMed:37244256}. |
Q9UHD1 | CHORDC1 | T212 | Sugiyama | Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1) (CHORD-containing protein 1) (CHP-1) (Protein morgana) | Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:20230755). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). In vitro, has intrinsic chaperone activity (PubMed:20230755). This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755). Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105). Involved in stress response (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755). {ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:32053105}. |
Q10713 | PMPCA | T294 | Sugiyama | Mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (P-55) | Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins. {ECO:0000269|PubMed:25808372}. |
Q9UBW7 | ZMYM2 | T157 | Sugiyama | Zinc finger MYM-type protein 2 (Fused in myeloproliferative disorders protein) (Rearranged in atypical myeloproliferative disorder protein) (Zinc finger protein 198) | Involved in the negative regulation of transcription. {ECO:0000269|PubMed:32891193}. |
Q9NR30 | DDX21 | T377 | Sugiyama | Nucleolar RNA helicase 2 (EC 3.6.4.13) (DEAD box protein 21) (Gu-alpha) (Nucleolar RNA helicase Gu) (Nucleolar RNA helicase II) (RH II/Gu) | RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as a cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required to prevent R-loop-associated DNA damage and transcription-associated genomic instability: deacetylation by SIRT7 activates the helicase activity, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins (PubMed:28431233). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305}. |
Download
reactome_id | name | p | -log10_p |
---|---|---|---|
R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | 1.753784e-09 | 8.756 |
R-HSA-3371556 | Cellular response to heat stress | 3.053542e-09 | 8.515 |
R-HSA-9020591 | Interleukin-12 signaling | 2.140752e-08 | 7.669 |
R-HSA-447115 | Interleukin-12 family signaling | 9.836849e-08 | 7.007 |
R-HSA-8953897 | Cellular responses to stimuli | 5.774719e-07 | 6.238 |
R-HSA-72203 | Processing of Capped Intron-Containing Pre-mRNA | 8.390092e-07 | 6.076 |
R-HSA-8950505 | Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulati... | 2.687569e-06 | 5.571 |
R-HSA-3371568 | Attenuation phase | 5.739701e-06 | 5.241 |
R-HSA-383280 | Nuclear Receptor transcription pathway | 1.105228e-05 | 4.957 |
R-HSA-2262752 | Cellular responses to stress | 1.041290e-05 | 4.982 |
R-HSA-3371571 | HSF1-dependent transactivation | 2.885982e-05 | 4.540 |
R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's dis... | 3.548808e-05 | 4.450 |
R-HSA-8863678 | Neurodegenerative Diseases | 3.548808e-05 | 4.450 |
R-HSA-9734009 | Defective Intrinsic Pathway for Apoptosis | 5.983357e-05 | 4.223 |
R-HSA-1280215 | Cytokine Signaling in Immune system | 7.449175e-05 | 4.128 |
R-HSA-72202 | Transport of Mature Transcript to Cytoplasm | 9.501963e-05 | 4.022 |
R-HSA-70171 | Glycolysis | 9.211865e-05 | 4.036 |
R-HSA-72163 | mRNA Splicing - Major Pathway | 1.143953e-04 | 3.942 |
R-HSA-111465 | Apoptotic cleavage of cellular proteins | 1.284661e-04 | 3.891 |
R-HSA-159236 | Transport of Mature mRNA derived from an Intron-Containing Transcript | 2.508642e-04 | 3.601 |
R-HSA-72706 | GTP hydrolysis and joining of the 60S ribosomal subunit | 1.720457e-04 | 3.764 |
R-HSA-72172 | mRNA Splicing | 1.909531e-04 | 3.719 |
R-HSA-156842 | Eukaryotic Translation Elongation | 2.387786e-04 | 3.622 |
R-HSA-180746 | Nuclear import of Rev protein | 1.929101e-04 | 3.715 |
R-HSA-9725370 | Signaling by ALK fusions and activated point mutants | 1.609803e-04 | 3.793 |
R-HSA-9700206 | Signaling by ALK in cancer | 1.609803e-04 | 3.793 |
R-HSA-449147 | Signaling by Interleukins | 2.578315e-04 | 3.589 |
R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | 2.523557e-04 | 3.598 |
R-HSA-8953854 | Metabolism of RNA | 2.338136e-04 | 3.631 |
R-HSA-3371511 | HSF1 activation | 2.484190e-04 | 3.605 |
R-HSA-168273 | Influenza Viral RNA Transcription and Replication | 2.152542e-04 | 3.667 |
R-HSA-168255 | Influenza Infection | 2.014633e-04 | 3.696 |
R-HSA-1169410 | Antiviral mechanism by IFN-stimulated genes | 2.043084e-04 | 3.690 |
R-HSA-180910 | Vpr-mediated nuclear import of PICs | 2.805143e-04 | 3.552 |
R-HSA-72613 | Eukaryotic Translation Initiation | 3.225572e-04 | 3.491 |
R-HSA-72737 | Cap-dependent Translation Initiation | 3.225572e-04 | 3.491 |
R-HSA-159231 | Transport of Mature mRNA Derived from an Intronless Transcript | 3.544241e-04 | 3.450 |
R-HSA-70326 | Glucose metabolism | 3.423155e-04 | 3.466 |
R-HSA-159234 | Transport of Mature mRNAs Derived from Intronless Transcripts | 3.966760e-04 | 3.402 |
R-HSA-176033 | Interactions of Vpr with host cellular proteins | 3.966760e-04 | 3.402 |
R-HSA-177243 | Interactions of Rev with host cellular proteins | 3.966760e-04 | 3.402 |
R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | 4.036320e-04 | 3.394 |
R-HSA-9633012 | Response of EIF2AK4 (GCN2) to amino acid deficiency | 5.631663e-04 | 3.249 |
R-HSA-156827 | L13a-mediated translational silencing of Ceruloplasmin expression | 7.586398e-04 | 3.120 |
R-HSA-156902 | Peptide chain elongation | 8.099622e-04 | 3.092 |
R-HSA-75153 | Apoptotic execution phase | 8.135617e-04 | 3.090 |
R-HSA-5619107 | Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC... | 8.336588e-04 | 3.079 |
R-HSA-3371497 | HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of lig... | 9.081057e-04 | 3.042 |
R-HSA-1855196 | IP3 and IP4 transport between cytosol and nucleus | 9.408951e-04 | 3.026 |
R-HSA-1855229 | IP6 and IP7 transport between cytosol and nucleus | 9.408951e-04 | 3.026 |
R-HSA-1855170 | IPs transport between nucleus and cytosol | 1.185712e-03 | 2.926 |
R-HSA-159227 | Transport of the SLBP independent Mature mRNA | 1.185712e-03 | 2.926 |
R-HSA-199992 | trans-Golgi Network Vesicle Budding | 1.216733e-03 | 2.915 |
R-HSA-159230 | Transport of the SLBP Dependant Mature mRNA | 1.324411e-03 | 2.878 |
R-HSA-170822 | Regulation of Glucokinase by Glucokinase Regulatory Protein | 1.324411e-03 | 2.878 |
R-HSA-72689 | Formation of a pool of free 40S subunits | 1.415689e-03 | 2.849 |
R-HSA-1169408 | ISG15 antiviral mechanism | 1.497882e-03 | 2.825 |
R-HSA-432722 | Golgi Associated Vesicle Biogenesis | 1.507698e-03 | 2.822 |
R-HSA-3301854 | Nuclear Pore Complex (NPC) Disassembly | 1.637243e-03 | 2.786 |
R-HSA-416572 | Sema4D induced cell migration and growth-cone collapse | 1.668374e-03 | 2.778 |
R-HSA-9636667 | Manipulation of host energy metabolism | 1.692618e-03 | 2.771 |
R-HSA-432720 | Lysosome Vesicle Biogenesis | 1.812534e-03 | 2.742 |
R-HSA-162909 | Host Interactions of HIV factors | 1.966044e-03 | 2.706 |
R-HSA-2980766 | Nuclear Envelope Breakdown | 2.067657e-03 | 2.685 |
R-HSA-165054 | Rev-mediated nuclear export of HIV RNA | 2.203793e-03 | 2.657 |
R-HSA-390450 | Folding of actin by CCT/TriC | 2.331593e-03 | 2.632 |
R-HSA-168276 | NS1 Mediated Effects on Host Pathways | 2.420944e-03 | 2.616 |
R-HSA-389957 | Prefoldin mediated transfer of substrate to CCT/TriC | 2.840562e-03 | 2.547 |
R-HSA-168271 | Transport of Ribonucleoproteins into the Host Nucleus | 2.901262e-03 | 2.537 |
R-HSA-162587 | HIV Life Cycle | 2.917938e-03 | 2.535 |
R-HSA-913531 | Interferon Signaling | 3.291404e-03 | 2.483 |
R-HSA-9645723 | Diseases of programmed cell death | 3.536998e-03 | 2.451 |
R-HSA-400685 | Sema4D in semaphorin signaling | 3.596879e-03 | 2.444 |
R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | 3.670961e-03 | 2.435 |
R-HSA-9954714 | PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA | 4.165932e-03 | 2.380 |
R-HSA-209543 | p75NTR recruits signalling complexes | 4.161723e-03 | 2.381 |
R-HSA-162906 | HIV Infection | 4.293116e-03 | 2.367 |
R-HSA-975956 | Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) | 4.393321e-03 | 2.357 |
R-HSA-168333 | NEP/NS2 Interacts with the Cellular Export Machinery | 4.398294e-03 | 2.357 |
R-HSA-9662360 | Sensory processing of sound by inner hair cells of the cochlea | 4.417536e-03 | 2.355 |
R-HSA-168256 | Immune System | 4.652668e-03 | 2.332 |
R-HSA-6791226 | Major pathway of rRNA processing in the nucleolus and cytosol | 4.963572e-03 | 2.304 |
R-HSA-162599 | Late Phase of HIV Life Cycle | 5.131281e-03 | 2.290 |
R-HSA-168274 | Export of Viral Ribonucleoproteins from Nucleus | 4.753234e-03 | 2.323 |
R-HSA-9705671 | SARS-CoV-2 activates/modulates innate and adaptive immune responses | 5.131281e-03 | 2.290 |
R-HSA-9954716 | ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ri... | 5.397792e-03 | 2.268 |
R-HSA-70263 | Gluconeogenesis | 5.523345e-03 | 2.258 |
R-HSA-5663202 | Diseases of signal transduction by growth factor receptors and second messengers | 5.646900e-03 | 2.248 |
R-HSA-72764 | Eukaryotic Translation Termination | 5.673812e-03 | 2.246 |
R-HSA-380270 | Recruitment of mitotic centrosome proteins and complexes | 5.970399e-03 | 2.224 |
R-HSA-2132295 | MHC class II antigen presentation | 6.559741e-03 | 2.183 |
R-HSA-389958 | Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding | 6.658815e-03 | 2.177 |
R-HSA-193639 | p75NTR signals via NF-kB | 6.673002e-03 | 2.176 |
R-HSA-380287 | Centrosome maturation | 6.691137e-03 | 2.175 |
R-HSA-2408557 | Selenocysteine synthesis | 7.557308e-03 | 2.122 |
R-HSA-6798695 | Neutrophil degranulation | 7.719400e-03 | 2.112 |
R-HSA-199991 | Membrane Trafficking | 8.049101e-03 | 2.094 |
R-HSA-192823 | Viral mRNA Translation | 8.277450e-03 | 2.082 |
R-HSA-8868773 | rRNA processing in the nucleus and cytosol | 9.082342e-03 | 2.042 |
R-HSA-9860931 | Response of endothelial cells to shear stress | 8.655895e-03 | 2.063 |
R-HSA-9711097 | Cellular response to starvation | 9.242388e-03 | 2.034 |
R-HSA-9659379 | Sensory processing of sound | 8.318750e-03 | 2.080 |
R-HSA-72702 | Ribosomal scanning and start codon recognition | 9.490163e-03 | 2.023 |
R-HSA-9662361 | Sensory processing of sound by outer hair cells of the cochlea | 9.490163e-03 | 2.023 |
R-HSA-9692914 | SARS-CoV-1-host interactions | 9.867549e-03 | 2.006 |
R-HSA-9860927 | Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZ... | 1.024414e-02 | 1.990 |
R-HSA-1799339 | SRP-dependent cotranslational protein targeting to membrane | 1.029765e-02 | 1.987 |
R-HSA-9833576 | CDH11 homotypic and heterotypic interactions | 1.127847e-02 | 1.948 |
R-HSA-141424 | Amplification of signal from the kinetochores | 1.182139e-02 | 1.927 |
R-HSA-141444 | Amplification of signal from unattached kinetochores via a MAD2 inhibitory si... | 1.182139e-02 | 1.927 |
R-HSA-191859 | snRNP Assembly | 1.138218e-02 | 1.944 |
R-HSA-194441 | Metabolism of non-coding RNA | 1.138218e-02 | 1.944 |
R-HSA-9764302 | Regulation of CDH19 Expression and Function | 1.127847e-02 | 1.948 |
R-HSA-2408522 | Selenoamino acid metabolism | 1.129958e-02 | 1.947 |
R-HSA-9705683 | SARS-CoV-2-host interactions | 1.153725e-02 | 1.938 |
R-HSA-9754189 | Germ layer formation at gastrulation | 1.251413e-02 | 1.903 |
R-HSA-927802 | Nonsense-Mediated Decay (NMD) | 1.265524e-02 | 1.898 |
R-HSA-975957 | Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) | 1.265524e-02 | 1.898 |
R-HSA-168325 | Viral Messenger RNA Synthesis | 1.277715e-02 | 1.894 |
R-HSA-6784531 | tRNA processing in the nucleus | 1.351615e-02 | 1.869 |
R-HSA-9855142 | Cellular responses to mechanical stimuli | 1.369916e-02 | 1.863 |
R-HSA-373755 | Semaphorin interactions | 1.428344e-02 | 1.845 |
R-HSA-5653656 | Vesicle-mediated transport | 1.498060e-02 | 1.824 |
R-HSA-4420097 | VEGFA-VEGFR2 Pathway | 1.537868e-02 | 1.813 |
R-HSA-76002 | Platelet activation, signaling and aggregation | 1.550185e-02 | 1.810 |
R-HSA-74160 | Gene expression (Transcription) | 1.568489e-02 | 1.805 |
R-HSA-9674415 | Drug resistance of PDGFR mutants | 1.961565e-02 | 1.707 |
R-HSA-9674428 | PDGFR mutants bind TKIs | 1.961565e-02 | 1.707 |
R-HSA-9674401 | Sunitinib-resistant PDGFR mutants | 1.961565e-02 | 1.707 |
R-HSA-9674403 | Regorafenib-resistant PDGFR mutants | 1.961565e-02 | 1.707 |
R-HSA-9674404 | Sorafenib-resistant PDGFR mutants | 1.961565e-02 | 1.707 |
R-HSA-9674396 | Imatinib-resistant PDGFR mutants | 1.961565e-02 | 1.707 |
R-HSA-9671555 | Signaling by PDGFR in disease | 1.706710e-02 | 1.768 |
R-HSA-9615017 | FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes | 1.706504e-02 | 1.768 |
R-HSA-9613354 | Lipophagy | 2.409922e-02 | 1.618 |
R-HSA-9700645 | ALK mutants bind TKIs | 2.409922e-02 | 1.618 |
R-HSA-389960 | Formation of tubulin folding intermediates by CCT/TriC | 2.242812e-02 | 1.649 |
R-HSA-450341 | Activation of the AP-1 family of transcription factors | 2.409922e-02 | 1.618 |
R-HSA-9020933 | Interleukin-23 signaling | 2.051253e-02 | 1.688 |
R-HSA-194138 | Signaling by VEGF | 2.279056e-02 | 1.642 |
R-HSA-112411 | MAPK1 (ERK2) activation | 2.409922e-02 | 1.618 |
R-HSA-351906 | Apoptotic cleavage of cell adhesion proteins | 2.051253e-02 | 1.688 |
R-HSA-264870 | Caspase-mediated cleavage of cytoskeletal proteins | 2.409922e-02 | 1.618 |
R-HSA-5578749 | Transcriptional regulation by small RNAs | 2.253026e-02 | 1.647 |
R-HSA-9614085 | FOXO-mediated transcription | 2.348165e-02 | 1.629 |
R-HSA-9824446 | Viral Infection Pathways | 2.102942e-02 | 1.677 |
R-HSA-9679506 | SARS-CoV Infections | 2.227920e-02 | 1.652 |
R-HSA-114608 | Platelet degranulation | 2.436364e-02 | 1.613 |
R-HSA-69618 | Mitotic Spindle Checkpoint | 2.439870e-02 | 1.613 |
R-HSA-69278 | Cell Cycle, Mitotic | 2.633939e-02 | 1.579 |
R-HSA-9762292 | Regulation of CDH11 function | 2.792179e-02 | 1.554 |
R-HSA-9020956 | Interleukin-27 signaling | 2.792179e-02 | 1.554 |
R-HSA-110056 | MAPK3 (ERK1) activation | 2.792179e-02 | 1.554 |
R-HSA-8856688 | Golgi-to-ER retrograde transport | 2.952675e-02 | 1.530 |
R-HSA-72312 | rRNA processing | 3.041136e-02 | 1.517 |
R-HSA-76005 | Response to elevated platelet cytosolic Ca2+ | 3.045373e-02 | 1.516 |
R-HSA-68886 | M Phase | 3.184951e-02 | 1.497 |
R-HSA-9020558 | Interleukin-2 signaling | 3.196966e-02 | 1.495 |
R-HSA-9856530 | High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR... | 3.203129e-02 | 1.494 |
R-HSA-6811442 | Intra-Golgi and retrograde Golgi-to-ER traffic | 3.221951e-02 | 1.492 |
R-HSA-72187 | mRNA 3'-end processing | 3.250023e-02 | 1.488 |
R-HSA-9759475 | Regulation of CDH11 Expression and Function | 3.316654e-02 | 1.479 |
R-HSA-180689 | APOBEC3G mediated resistance to HIV-1 infection | 3.623258e-02 | 1.441 |
R-HSA-3000484 | Scavenging by Class F Receptors | 4.070062e-02 | 1.390 |
R-HSA-72649 | Translation initiation complex formation | 3.595963e-02 | 1.444 |
R-HSA-9948299 | Ribosome-associated quality control | 3.642793e-02 | 1.439 |
R-HSA-2173793 | Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer | 3.962379e-02 | 1.402 |
R-HSA-162592 | Integration of provirus | 3.623258e-02 | 1.441 |
R-HSA-2565942 | Regulation of PLK1 Activity at G2/M Transition | 3.759405e-02 | 1.425 |
R-HSA-8984722 | Interleukin-35 Signalling | 4.070062e-02 | 1.390 |
R-HSA-209560 | NF-kB is activated and signals survival | 3.623258e-02 | 1.441 |
R-HSA-72766 | Translation | 3.656228e-02 | 1.437 |
R-HSA-6804756 | Regulation of TP53 Activity through Phosphorylation | 4.213134e-02 | 1.375 |
R-HSA-445355 | Smooth Muscle Contraction | 3.420438e-02 | 1.466 |
R-HSA-1500931 | Cell-Cell communication | 3.764452e-02 | 1.424 |
R-HSA-9648025 | EML4 and NUDC in mitotic spindle formation | 3.490466e-02 | 1.457 |
R-HSA-422475 | Axon guidance | 3.482100e-02 | 1.458 |
R-HSA-1640170 | Cell Cycle | 3.472378e-02 | 1.459 |
R-HSA-9678108 | SARS-CoV-1 Infection | 4.133372e-02 | 1.384 |
R-HSA-9764260 | Regulation of Expression and Function of Type II Classical Cadherins | 4.335751e-02 | 1.363 |
R-HSA-72662 | Activation of the mRNA upon binding of the cap-binding complex and eIFs, and sub... | 4.349308e-02 | 1.362 |
R-HSA-397014 | Muscle contraction | 4.364152e-02 | 1.360 |
R-HSA-9796292 | Formation of axial mesoderm | 4.536414e-02 | 1.343 |
R-HSA-6788467 | IL-6-type cytokine receptor ligand interactions | 4.536414e-02 | 1.343 |
R-HSA-1059683 | Interleukin-6 signaling | 4.536414e-02 | 1.343 |
R-HSA-5696394 | DNA Damage Recognition in GG-NER | 4.612232e-02 | 1.336 |
R-HSA-390471 | Association of TriC/CCT with target proteins during biosynthesis | 4.612232e-02 | 1.336 |
R-HSA-9768727 | Regulation of CDH1 posttranslational processing and trafficking to plasma membra... | 4.612232e-02 | 1.336 |
R-HSA-6814122 | Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding | 4.897226e-02 | 1.310 |
R-HSA-9735869 | SARS-CoV-1 modulates host translation machinery | 4.897226e-02 | 1.310 |
R-HSA-73856 | RNA Polymerase II Transcription Termination | 4.968123e-02 | 1.304 |
R-HSA-391160 | Signal regulatory protein family interactions | 5.021381e-02 | 1.299 |
R-HSA-68875 | Mitotic Prophase | 5.239223e-02 | 1.281 |
R-HSA-2500257 | Resolution of Sister Chromatid Cohesion | 5.392345e-02 | 1.268 |
R-HSA-2682334 | EPH-Ephrin signaling | 5.395321e-02 | 1.268 |
R-HSA-380284 | Loss of proteins required for interphase microtubule organization from the centr... | 5.406173e-02 | 1.267 |
R-HSA-380259 | Loss of Nlp from mitotic centrosomes | 5.406173e-02 | 1.267 |
R-HSA-9010553 | Regulation of expression of SLITs and ROBOs | 5.459400e-02 | 1.263 |
R-HSA-8876725 | Protein methylation | 5.524058e-02 | 1.258 |
R-HSA-3304347 | Loss of Function of SMAD4 in Cancer | 5.770365e-02 | 1.239 |
R-HSA-5619050 | Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tu... | 5.770365e-02 | 1.239 |
R-HSA-3315487 | SMAD2/3 MH2 Domain Mutants in Cancer | 5.770365e-02 | 1.239 |
R-HSA-3311021 | SMAD4 MH2 Domain Mutants in Cancer | 5.770365e-02 | 1.239 |
R-HSA-9665230 | Drug resistance in ERBB2 KD mutants | 7.619081e-02 | 1.118 |
R-HSA-9652282 | Drug-mediated inhibition of ERBB2 signaling | 7.619081e-02 | 1.118 |
R-HSA-9665249 | Resistance of ERBB2 KD mutants to afatinib | 7.619081e-02 | 1.118 |
R-HSA-9665247 | Resistance of ERBB2 KD mutants to osimertinib | 7.619081e-02 | 1.118 |
R-HSA-9665737 | Drug resistance in ERBB2 TMD/JMD mutants | 7.619081e-02 | 1.118 |
R-HSA-9665246 | Resistance of ERBB2 KD mutants to neratinib | 7.619081e-02 | 1.118 |
R-HSA-9665233 | Resistance of ERBB2 KD mutants to trastuzumab | 7.619081e-02 | 1.118 |
R-HSA-9665251 | Resistance of ERBB2 KD mutants to lapatinib | 7.619081e-02 | 1.118 |
R-HSA-9665250 | Resistance of ERBB2 KD mutants to AEE788 | 7.619081e-02 | 1.118 |
R-HSA-5619104 | Defective SLC12A1 causes Bartter syndrome 1 (BS1) | 7.619081e-02 | 1.118 |
R-HSA-9665244 | Resistance of ERBB2 KD mutants to sapitinib | 7.619081e-02 | 1.118 |
R-HSA-9665245 | Resistance of ERBB2 KD mutants to tesevatinib | 7.619081e-02 | 1.118 |
R-HSA-8854518 | AURKA Activation by TPX2 | 6.101184e-02 | 1.215 |
R-HSA-2173796 | SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription | 5.802301e-02 | 1.236 |
R-HSA-9842860 | Regulation of endogenous retroelements | 7.603605e-02 | 1.119 |
R-HSA-9954709 | Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide | 6.148913e-02 | 1.211 |
R-HSA-139853 | Elevation of cytosolic Ca2+ levels | 7.129721e-02 | 1.147 |
R-HSA-170834 | Signaling by TGF-beta Receptor Complex | 6.546963e-02 | 1.184 |
R-HSA-194306 | Neurophilin interactions with VEGF and VEGFR | 7.619081e-02 | 1.118 |
R-HSA-9925563 | Developmental Lineage of Pancreatic Ductal Cells | 6.841148e-02 | 1.165 |
R-HSA-68877 | Mitotic Prometaphase | 6.265230e-02 | 1.203 |
R-HSA-2028269 | Signaling by Hippo | 7.129721e-02 | 1.147 |
R-HSA-3214841 | PKMTs methylate histone lysines | 7.121768e-02 | 1.147 |
R-HSA-193704 | p75 NTR receptor-mediated signalling | 6.959113e-02 | 1.157 |
R-HSA-75108 | Activation, myristolyation of BID and translocation to mitochondria | 7.619081e-02 | 1.118 |
R-HSA-8874177 | ATF6B (ATF6-beta) activates chaperones | 7.619081e-02 | 1.118 |
R-HSA-9675108 | Nervous system development | 5.731413e-02 | 1.242 |
R-HSA-5633007 | Regulation of TP53 Activity | 6.624536e-02 | 1.179 |
R-HSA-5218920 | VEGFR2 mediated vascular permeability | 7.121768e-02 | 1.147 |
R-HSA-8866910 | TFAP2 (AP-2) family regulates transcription of growth factors and their receptor... | 6.579064e-02 | 1.182 |
R-HSA-109581 | Apoptosis | 6.937558e-02 | 1.159 |
R-HSA-9694516 | SARS-CoV-2 Infection | 6.633060e-02 | 1.178 |
R-HSA-9613829 | Chaperone Mediated Autophagy | 7.694743e-02 | 1.114 |
R-HSA-1839117 | Signaling by cytosolic FGFR1 fusion mutants | 7.694743e-02 | 1.114 |
R-HSA-9614657 | FOXO-mediated transcription of cell death genes | 7.694743e-02 | 1.114 |
R-HSA-5619102 | SLC transporter disorders | 7.758260e-02 | 1.110 |
R-HSA-1852241 | Organelle biogenesis and maintenance | 7.861580e-02 | 1.104 |
R-HSA-449836 | Other interleukin signaling | 8.273360e-02 | 1.082 |
R-HSA-8864260 | Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors | 8.562651e-02 | 1.067 |
R-HSA-9823730 | Formation of definitive endoderm | 8.864823e-02 | 1.052 |
R-HSA-373753 | Nephrin family interactions | 8.864823e-02 | 1.052 |
R-HSA-1362277 | Transcription of E2F targets under negative control by DREAM complex | 8.864823e-02 | 1.052 |
R-HSA-211000 | Gene Silencing by RNA | 8.985767e-02 | 1.046 |
R-HSA-72165 | mRNA Splicing - Minor Pathway | 9.325863e-02 | 1.030 |
R-HSA-72695 | Formation of the ternary complex, and subsequently, the 43S complex | 9.325863e-02 | 1.030 |
R-HSA-9673766 | Signaling by cytosolic PDGFRA and PDGFRB fusion proteins | 9.431639e-02 | 1.025 |
R-HSA-162594 | Early Phase of HIV Life Cycle | 9.468411e-02 | 1.024 |
R-HSA-392499 | Metabolism of proteins | 9.740033e-02 | 1.011 |
R-HSA-9833482 | PKR-mediated signaling | 9.923661e-02 | 1.003 |
R-HSA-9705462 | Inactivation of CSF3 (G-CSF) signaling | 1.008342e-01 | 0.996 |
R-HSA-9031628 | NGF-stimulated transcription | 1.011603e-01 | 0.995 |
R-HSA-1251932 | PLCG1 events in ERBB2 signaling | 1.120874e-01 | 0.950 |
R-HSA-1306955 | GRB7 events in ERBB2 signaling | 1.120874e-01 | 0.950 |
R-HSA-3656532 | TGFBR1 KD Mutants in Cancer | 1.120874e-01 | 0.950 |
R-HSA-9673768 | Signaling by membrane-tethered fusions of PDGFRA or PDGFRB | 1.295108e-01 | 0.888 |
R-HSA-3304356 | SMAD2/3 Phosphorylation Motif Mutants in Cancer | 1.295108e-01 | 0.888 |
R-HSA-164525 | Plus-strand DNA synthesis | 1.465934e-01 | 0.834 |
R-HSA-9017802 | Noncanonical activation of NOTCH3 | 1.465934e-01 | 0.834 |
R-HSA-3304349 | Loss of Function of SMAD2/3 in Cancer | 1.465934e-01 | 0.834 |
R-HSA-8869496 | TFAP2A acts as a transcriptional repressor during retinoic acid induced cell dif... | 1.633418e-01 | 0.787 |
R-HSA-177539 | Autointegration results in viral DNA circles | 1.633418e-01 | 0.787 |
R-HSA-162585 | Uncoating of the HIV Virion | 1.633418e-01 | 0.787 |
R-HSA-5263617 | Metabolism of ingested MeSeO2H into MeSeH | 1.633418e-01 | 0.787 |
R-HSA-8951430 | RUNX3 regulates WNT signaling | 1.797624e-01 | 0.745 |
R-HSA-4411364 | Binding of TCF/LEF:CTNNB1 to target gene promoters | 1.797624e-01 | 0.745 |
R-HSA-9732724 | IFNG signaling activates MAPKs | 1.797624e-01 | 0.745 |
R-HSA-162589 | Reverse Transcription of HIV RNA | 1.958618e-01 | 0.708 |
R-HSA-164516 | Minus-strand DNA synthesis | 1.958618e-01 | 0.708 |
R-HSA-446107 | Type I hemidesmosome assembly | 1.958618e-01 | 0.708 |
R-HSA-196025 | Formation of annular gap junctions | 1.958618e-01 | 0.708 |
R-HSA-9020958 | Interleukin-21 signaling | 2.116462e-01 | 0.674 |
R-HSA-190873 | Gap junction degradation | 2.116462e-01 | 0.674 |
R-HSA-173107 | Binding and entry of HIV virion | 2.271217e-01 | 0.644 |
R-HSA-9938206 | Developmental Lineage of Mammary Stem Cells | 1.070918e-01 | 0.970 |
R-HSA-210990 | PECAM1 interactions | 2.422943e-01 | 0.616 |
R-HSA-8876493 | InlA-mediated entry of Listeria monocytogenes into host cells | 2.422943e-01 | 0.616 |
R-HSA-5339716 | Signaling by GSK3beta mutants | 2.571700e-01 | 0.590 |
R-HSA-9634285 | Constitutive Signaling by Overexpressed ERBB2 | 2.717546e-01 | 0.566 |
R-HSA-937039 | IRAK1 recruits IKK complex | 2.717546e-01 | 0.566 |
R-HSA-975144 | IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation | 2.717546e-01 | 0.566 |
R-HSA-4839743 | Signaling by CTNNB1 phospho-site mutants | 2.717546e-01 | 0.566 |
R-HSA-5358749 | CTNNB1 S37 mutants aren't phosphorylated | 2.717546e-01 | 0.566 |
R-HSA-5358751 | CTNNB1 S45 mutants aren't phosphorylated | 2.717546e-01 | 0.566 |
R-HSA-5358747 | CTNNB1 S33 mutants aren't phosphorylated | 2.717546e-01 | 0.566 |
R-HSA-5358752 | CTNNB1 T41 mutants aren't phosphorylated | 2.717546e-01 | 0.566 |
R-HSA-177504 | Retrograde neurotrophin signalling | 3.000728e-01 | 0.523 |
R-HSA-8847993 | ERBB2 Activates PTK6 Signaling | 3.000728e-01 | 0.523 |
R-HSA-390522 | Striated Muscle Contraction | 1.883853e-01 | 0.725 |
R-HSA-9843970 | Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex | 1.955165e-01 | 0.709 |
R-HSA-9845323 | Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) | 1.535362e-01 | 0.814 |
R-HSA-380320 | Recruitment of NuMA to mitotic centrosomes | 1.284431e-01 | 0.891 |
R-HSA-606279 | Deposition of new CENPA-containing nucleosomes at the centromere | 2.826313e-01 | 0.549 |
R-HSA-774815 | Nucleosome assembly | 2.826313e-01 | 0.549 |
R-HSA-9844594 | Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 | 2.388662e-01 | 0.622 |
R-HSA-9843743 | Transcriptional regulation of brown and beige adipocyte differentiation | 2.388662e-01 | 0.622 |
R-HSA-5620912 | Anchoring of the basal body to the plasma membrane | 1.353738e-01 | 0.868 |
R-HSA-8854691 | Interleukin-20 family signaling | 1.134504e-01 | 0.945 |
R-HSA-380972 | Energy dependent regulation of mTOR by LKB1-AMPK | 1.602794e-01 | 0.795 |
R-HSA-390466 | Chaperonin-mediated protein folding | 1.250352e-01 | 0.903 |
R-HSA-8983432 | Interleukin-15 signaling | 2.717546e-01 | 0.566 |
R-HSA-983170 | Antigen Presentation: Folding, assembly and peptide loading of class I MHC | 1.955165e-01 | 0.709 |
R-HSA-3134973 | LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production | 1.295108e-01 | 0.888 |
R-HSA-912694 | Regulation of IFNA/IFNB signaling | 1.070918e-01 | 0.970 |
R-HSA-437239 | Recycling pathway of L1 | 2.971979e-01 | 0.527 |
R-HSA-451927 | Interleukin-2 family signaling | 2.388662e-01 | 0.622 |
R-HSA-164940 | Nef mediated downregulation of MHC class I complex cell surface expression | 1.958618e-01 | 0.708 |
R-HSA-1236977 | Endosomal/Vacuolar pathway | 2.571700e-01 | 0.590 |
R-HSA-2173795 | Downregulation of SMAD2/3:SMAD4 transcriptional activity | 1.742397e-01 | 0.759 |
R-HSA-909733 | Interferon alpha/beta signaling | 2.539597e-01 | 0.595 |
R-HSA-9674555 | Signaling by CSF3 (G-CSF) | 1.533805e-01 | 0.814 |
R-HSA-5250913 | Positive epigenetic regulation of rRNA expression | 2.073595e-01 | 0.683 |
R-HSA-8856828 | Clathrin-mediated endocytosis | 2.167764e-01 | 0.664 |
R-HSA-6783589 | Interleukin-6 family signaling | 1.199035e-01 | 0.921 |
R-HSA-8849473 | PTK6 Expression | 1.797624e-01 | 0.745 |
R-HSA-444473 | Formyl peptide receptors bind formyl peptides and many other ligands | 1.958618e-01 | 0.708 |
R-HSA-73762 | RNA Polymerase I Transcription Initiation | 2.607401e-01 | 0.584 |
R-HSA-9927418 | Developmental Lineage of Mammary Gland Luminal Epithelial Cells | 2.607401e-01 | 0.584 |
R-HSA-5620924 | Intraflagellar transport | 3.044653e-01 | 0.516 |
R-HSA-9615933 | Postmitotic nuclear pore complex (NPC) reformation | 1.330692e-01 | 0.876 |
R-HSA-3304351 | Signaling by TGF-beta Receptor Complex in Cancer | 1.633418e-01 | 0.787 |
R-HSA-391251 | Protein folding | 1.460472e-01 | 0.836 |
R-HSA-5696399 | Global Genome Nucleotide Excision Repair (GG-NER) | 2.752785e-01 | 0.560 |
R-HSA-8985947 | Interleukin-9 signaling | 1.958618e-01 | 0.708 |
R-HSA-3656534 | Loss of Function of TGFBR1 in Cancer | 1.295108e-01 | 0.888 |
R-HSA-434313 | Intracellular metabolism of fatty acids regulates insulin secretion | 1.633418e-01 | 0.787 |
R-HSA-2470946 | Cohesin Loading onto Chromatin | 1.797624e-01 | 0.745 |
R-HSA-5140745 | WNT5A-dependent internalization of FZD2, FZD5 and ROR2 | 2.271217e-01 | 0.644 |
R-HSA-2151209 | Activation of PPARGC1A (PGC-1alpha) by phosphorylation | 2.271217e-01 | 0.644 |
R-HSA-380615 | Serotonin clearance from the synaptic cleft | 2.717546e-01 | 0.566 |
R-HSA-8866427 | VLDLR internalisation and degradation | 2.717546e-01 | 0.566 |
R-HSA-877312 | Regulation of IFNG signaling | 2.717546e-01 | 0.566 |
R-HSA-445095 | Interaction between L1 and Ankyrins | 1.397701e-01 | 0.855 |
R-HSA-9933947 | Formation of the non-canonical BAF (ncBAF) complex | 2.860536e-01 | 0.544 |
R-HSA-9927432 | Developmental Lineage of Mammary Gland Myoepithelial Cells | 1.533805e-01 | 0.814 |
R-HSA-6807878 | COPI-mediated anterograde transport | 1.645290e-01 | 0.784 |
R-HSA-379716 | Cytosolic tRNA aminoacylation | 2.607401e-01 | 0.584 |
R-HSA-6811440 | Retrograde transport at the Trans-Golgi-Network | 2.971979e-01 | 0.527 |
R-HSA-6811436 | COPI-independent Golgi-to-ER retrograde traffic | 1.307611e-01 | 0.884 |
R-HSA-9006936 | Signaling by TGFB family members | 1.447671e-01 | 0.839 |
R-HSA-5218921 | VEGFR2 mediated cell proliferation | 1.264451e-01 | 0.898 |
R-HSA-8963888 | Chylomicron assembly | 2.422943e-01 | 0.616 |
R-HSA-8856825 | Cargo recognition for clathrin-mediated endocytosis | 1.957007e-01 | 0.708 |
R-HSA-373752 | Netrin-1 signaling | 2.753371e-01 | 0.560 |
R-HSA-418360 | Platelet calcium homeostasis | 1.533805e-01 | 0.814 |
R-HSA-6809371 | Formation of the cornified envelope | 1.413328e-01 | 0.850 |
R-HSA-9612973 | Autophagy | 2.640089e-01 | 0.578 |
R-HSA-5617833 | Cilium Assembly | 1.244408e-01 | 0.905 |
R-HSA-195399 | VEGF binds to VEGFR leading to receptor dimerization | 1.465934e-01 | 0.834 |
R-HSA-175567 | Integration of viral DNA into host genomic DNA | 1.633418e-01 | 0.787 |
R-HSA-8964041 | LDL remodeling | 1.797624e-01 | 0.745 |
R-HSA-2025928 | Calcineurin activates NFAT | 2.116462e-01 | 0.674 |
R-HSA-164843 | 2-LTR circle formation | 2.271217e-01 | 0.644 |
R-HSA-5607763 | CLEC7A (Dectin-1) induces NFAT activation | 3.000728e-01 | 0.523 |
R-HSA-1839124 | FGFR1 mutant receptor activation | 1.812916e-01 | 0.742 |
R-HSA-5655302 | Signaling by FGFR1 in disease | 2.534429e-01 | 0.596 |
R-HSA-9664873 | Pexophagy | 2.271217e-01 | 0.644 |
R-HSA-5693571 | Nonhomologous End-Joining (NHEJ) | 3.044653e-01 | 0.516 |
R-HSA-9663891 | Selective autophagy | 1.284431e-01 | 0.891 |
R-HSA-6796648 | TP53 Regulates Transcription of DNA Repair Genes | 2.435320e-01 | 0.613 |
R-HSA-1679131 | Trafficking and processing of endosomal TLR | 2.717546e-01 | 0.566 |
R-HSA-205043 | NRIF signals cell death from the nucleus | 3.000728e-01 | 0.523 |
R-HSA-6804758 | Regulation of TP53 Activity through Acetylation | 1.812916e-01 | 0.742 |
R-HSA-983189 | Kinesins | 1.535362e-01 | 0.814 |
R-HSA-6811434 | COPI-dependent Golgi-to-ER retrograde traffic | 1.645290e-01 | 0.784 |
R-HSA-8943724 | Regulation of PTEN gene transcription | 1.535362e-01 | 0.814 |
R-HSA-9824585 | Regulation of MITF-M-dependent genes involved in pigmentation | 2.826313e-01 | 0.549 |
R-HSA-373760 | L1CAM interactions | 1.182988e-01 | 0.927 |
R-HSA-194313 | VEGF ligand-receptor interactions | 1.465934e-01 | 0.834 |
R-HSA-9839389 | TGFBR3 regulates TGF-beta signaling | 1.797624e-01 | 0.745 |
R-HSA-426117 | Cation-coupled Chloride cotransporters | 1.797624e-01 | 0.745 |
R-HSA-163680 | AMPK inhibits chREBP transcriptional activation activity | 2.116462e-01 | 0.674 |
R-HSA-9683686 | Maturation of spike protein | 2.271217e-01 | 0.644 |
R-HSA-425381 | Bicarbonate transporters | 2.422943e-01 | 0.616 |
R-HSA-68884 | Mitotic Telophase/Cytokinesis | 2.571700e-01 | 0.590 |
R-HSA-1358803 | Downregulation of ERBB2:ERBB3 signaling | 2.717546e-01 | 0.566 |
R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | 2.717546e-01 | 0.566 |
R-HSA-3928663 | EPHA-mediated growth cone collapse | 1.397701e-01 | 0.855 |
R-HSA-450282 | MAPK targets/ Nuclear events mediated by MAP kinases | 1.533805e-01 | 0.814 |
R-HSA-418457 | cGMP effects | 3.000728e-01 | 0.523 |
R-HSA-2467813 | Separation of Sister Chromatids | 1.555304e-01 | 0.808 |
R-HSA-68882 | Mitotic Anaphase | 1.906942e-01 | 0.720 |
R-HSA-9609690 | HCMV Early Events | 2.557419e-01 | 0.592 |
R-HSA-446728 | Cell junction organization | 2.414308e-01 | 0.617 |
R-HSA-2555396 | Mitotic Metaphase and Anaphase | 1.933873e-01 | 0.714 |
R-HSA-199977 | ER to Golgi Anterograde Transport | 2.310292e-01 | 0.636 |
R-HSA-9768777 | Regulation of NPAS4 gene transcription | 2.116462e-01 | 0.674 |
R-HSA-9762293 | Regulation of CDH11 gene transcription | 2.116462e-01 | 0.674 |
R-HSA-1268020 | Mitochondrial protein import | 1.629751e-01 | 0.788 |
R-HSA-4839726 | Chromatin organization | 1.682388e-01 | 0.774 |
R-HSA-165159 | MTOR signalling | 2.607401e-01 | 0.584 |
R-HSA-8866423 | VLDL assembly | 1.633418e-01 | 0.787 |
R-HSA-5336415 | Uptake and function of diphtheria toxin | 1.797624e-01 | 0.745 |
R-HSA-447041 | CHL1 interactions | 1.797624e-01 | 0.745 |
R-HSA-8949664 | Processing of SMDT1 | 2.860536e-01 | 0.544 |
R-HSA-9933937 | Formation of the canonical BAF (cBAF) complex | 3.000728e-01 | 0.523 |
R-HSA-173599 | Formation of the active cofactor, UDP-glucuronate | 3.000728e-01 | 0.523 |
R-HSA-69275 | G2/M Transition | 1.157945e-01 | 0.936 |
R-HSA-453274 | Mitotic G2-G2/M phases | 1.200772e-01 | 0.921 |
R-HSA-3247509 | Chromatin modifying enzymes | 1.350467e-01 | 0.870 |
R-HSA-450294 | MAP kinase activation | 1.582338e-01 | 0.801 |
R-HSA-3214858 | RMTs methylate histone arginines | 2.753371e-01 | 0.560 |
R-HSA-264876 | Insulin processing | 1.397701e-01 | 0.855 |
R-HSA-204998 | Cell death signalling via NRAGE, NRIF and NADE | 2.175740e-01 | 0.662 |
R-HSA-9839373 | Signaling by TGFBR3 | 2.899191e-01 | 0.538 |
R-HSA-448424 | Interleukin-17 signaling | 2.022941e-01 | 0.694 |
R-HSA-112409 | RAF-independent MAPK1/3 activation | 1.070918e-01 | 0.970 |
R-HSA-1247673 | Erythrocytes take up oxygen and release carbon dioxide | 2.717546e-01 | 0.566 |
R-HSA-9818030 | NFE2L2 regulating tumorigenic genes | 2.860536e-01 | 0.544 |
R-HSA-9933939 | Formation of the polybromo-BAF (pBAF) complex | 3.000728e-01 | 0.523 |
R-HSA-9909649 | Regulation of PD-L1(CD274) transcription | 1.823467e-01 | 0.739 |
R-HSA-198725 | Nuclear Events (kinase and transcription factor activation) | 2.124533e-01 | 0.673 |
R-HSA-114604 | GPVI-mediated activation cascade | 2.098746e-01 | 0.678 |
R-HSA-1643685 | Disease | 2.771526e-01 | 0.557 |
R-HSA-73857 | RNA Polymerase II Transcription | 1.196877e-01 | 0.922 |
R-HSA-901042 | Calnexin/calreticulin cycle | 1.955165e-01 | 0.709 |
R-HSA-9755511 | KEAP1-NFE2L2 pathway | 2.455434e-01 | 0.610 |
R-HSA-9764790 | Positive Regulation of CDH1 Gene Transcription | 2.271217e-01 | 0.644 |
R-HSA-9828642 | Respiratory syncytial virus genome transcription | 3.000728e-01 | 0.523 |
R-HSA-6811558 | PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling | 2.887174e-01 | 0.540 |
R-HSA-109582 | Hemostasis | 2.488646e-01 | 0.604 |
R-HSA-1483249 | Inositol phosphate metabolism | 1.023010e-01 | 0.990 |
R-HSA-5663205 | Infectious disease | 1.174856e-01 | 0.930 |
R-HSA-212436 | Generic Transcription Pathway | 1.568522e-01 | 0.805 |
R-HSA-452723 | Transcriptional regulation of pluripotent stem cells | 2.243344e-01 | 0.649 |
R-HSA-430116 | GP1b-IX-V activation signalling | 2.116462e-01 | 0.674 |
R-HSA-9662834 | CD163 mediating an anti-inflammatory response | 2.422943e-01 | 0.616 |
R-HSA-1592230 | Mitochondrial biogenesis | 2.625724e-01 | 0.581 |
R-HSA-73887 | Death Receptor Signaling | 2.565829e-01 | 0.591 |
R-HSA-9610379 | HCMV Late Events | 2.677404e-01 | 0.572 |
R-HSA-9958790 | SLC-mediated transport of inorganic anions | 2.243344e-01 | 0.649 |
R-HSA-3299685 | Detoxification of Reactive Oxygen Species | 1.352158e-01 | 0.869 |
R-HSA-9833109 | Evasion by RSV of host interferon responses | 1.672341e-01 | 0.777 |
R-HSA-9022699 | MECP2 regulates neuronal receptors and channels | 1.330692e-01 | 0.876 |
R-HSA-1538133 | G0 and Early G1 | 1.742397e-01 | 0.759 |
R-HSA-9818027 | NFE2L2 regulating anti-oxidant/detoxification enzymes | 1.883853e-01 | 0.725 |
R-HSA-9759194 | Nuclear events mediated by NFE2L2 | 1.324759e-01 | 0.878 |
R-HSA-8983711 | OAS antiviral response | 2.717546e-01 | 0.566 |
R-HSA-9637690 | Response of Mtb to phagocytosis | 2.680391e-01 | 0.572 |
R-HSA-216083 | Integrin cell surface interactions | 2.435320e-01 | 0.613 |
R-HSA-1474244 | Extracellular matrix organization | 1.625327e-01 | 0.789 |
R-HSA-8986944 | Transcriptional Regulation by MECP2 | 1.388953e-01 | 0.857 |
R-HSA-75205 | Dissolution of Fibrin Clot | 2.422943e-01 | 0.616 |
R-HSA-9841251 | Mitochondrial unfolded protein response (UPRmt) | 1.397701e-01 | 0.855 |
R-HSA-5357801 | Programmed Cell Death | 1.621347e-01 | 0.790 |
R-HSA-5619115 | Disorders of transmembrane transporters | 2.802981e-01 | 0.552 |
R-HSA-376176 | Signaling by ROBO receptors | 1.547043e-01 | 0.810 |
R-HSA-5683057 | MAPK family signaling cascades | 3.056169e-01 | 0.515 |
R-HSA-9766229 | Degradation of CDH1 | 3.117190e-01 | 0.506 |
R-HSA-532668 | N-glycan trimming in the ER and Calnexin/Calreticulin cycle | 3.117190e-01 | 0.506 |
R-HSA-9673770 | Signaling by PDGFRA extracellular domain mutants | 3.138175e-01 | 0.503 |
R-HSA-9673767 | Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants | 3.138175e-01 | 0.503 |
R-HSA-2173791 | TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) | 3.138175e-01 | 0.503 |
R-HSA-196299 | Beta-catenin phosphorylation cascade | 3.138175e-01 | 0.503 |
R-HSA-450513 | Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA | 3.138175e-01 | 0.503 |
R-HSA-6785631 | ERBB2 Regulates Cell Motility | 3.138175e-01 | 0.503 |
R-HSA-418885 | DCC mediated attractive signaling | 3.138175e-01 | 0.503 |
R-HSA-1502540 | Signaling by Activin | 3.138175e-01 | 0.503 |
R-HSA-399954 | Sema3A PAK dependent Axon repulsion | 3.138175e-01 | 0.503 |
R-HSA-9933946 | Formation of the embryonic stem cell BAF (esBAF) complex | 3.138175e-01 | 0.503 |
R-HSA-9735871 | SARS-CoV-1 targets host intracellular signalling and regulatory pathways | 3.138175e-01 | 0.503 |
R-HSA-446353 | Cell-extracellular matrix interactions | 3.138175e-01 | 0.503 |
R-HSA-69620 | Cell Cycle Checkpoints | 3.144094e-01 | 0.503 |
R-HSA-187037 | Signaling by NTRK1 (TRKA) | 3.152057e-01 | 0.501 |
R-HSA-72306 | tRNA processing | 3.210105e-01 | 0.493 |
R-HSA-199418 | Negative regulation of the PI3K/AKT network | 3.240863e-01 | 0.489 |
R-HSA-354194 | GRB2:SOS provides linkage to MAPK signaling for Integrins | 3.272932e-01 | 0.485 |
R-HSA-168275 | Entry of Influenza Virion into Host Cell via Endocytosis | 3.272932e-01 | 0.485 |
R-HSA-5099900 | WNT5A-dependent internalization of FZD4 | 3.272932e-01 | 0.485 |
R-HSA-5635838 | Activation of SMO | 3.272932e-01 | 0.485 |
R-HSA-9664420 | Killing mechanisms | 3.272932e-01 | 0.485 |
R-HSA-9673324 | WNT5:FZD7-mediated leishmania damping | 3.272932e-01 | 0.485 |
R-HSA-9909648 | Regulation of PD-L1(CD274) expression | 3.287369e-01 | 0.483 |
R-HSA-9734767 | Developmental Cell Lineages | 3.301679e-01 | 0.481 |
R-HSA-9764265 | Regulation of CDH1 Expression and Function | 3.326074e-01 | 0.478 |
R-HSA-9764274 | Regulation of Expression and Function of Type I Classical Cadherins | 3.326074e-01 | 0.478 |
R-HSA-6794361 | Neurexins and neuroligins | 3.333752e-01 | 0.477 |
R-HSA-9692916 | SARS-CoV-1 activates/modulates innate immune responses | 3.333752e-01 | 0.477 |
R-HSA-2219530 | Constitutive Signaling by Aberrant PI3K in Cancer | 3.396751e-01 | 0.469 |
R-HSA-9837999 | Mitochondrial protein degradation | 3.396751e-01 | 0.469 |
R-HSA-1474290 | Collagen formation | 3.396751e-01 | 0.469 |
R-HSA-77595 | Processing of Intronless Pre-mRNAs | 3.405050e-01 | 0.468 |
R-HSA-1963640 | GRB2 events in ERBB2 signaling | 3.405050e-01 | 0.468 |
R-HSA-975110 | TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling | 3.405050e-01 | 0.468 |
R-HSA-9690406 | Transcriptional regulation of testis differentiation | 3.405050e-01 | 0.468 |
R-HSA-964975 | Vitamin B6 activation to pyridoxal phosphate | 3.405050e-01 | 0.468 |
R-HSA-5250924 | B-WICH complex positively regulates rRNA expression | 3.405521e-01 | 0.468 |
R-HSA-9711123 | Cellular response to chemical stress | 3.460435e-01 | 0.461 |
R-HSA-9754678 | SARS-CoV-2 modulates host translation machinery | 3.477050e-01 | 0.459 |
R-HSA-168249 | Innate Immune System | 3.522638e-01 | 0.453 |
R-HSA-1963642 | PI3K events in ERBB2 signaling | 3.534582e-01 | 0.452 |
R-HSA-372708 | p130Cas linkage to MAPK signaling for integrins | 3.534582e-01 | 0.452 |
R-HSA-164938 | Nef-mediates down modulation of cell surface receptors by recruiting them to cla... | 3.534582e-01 | 0.452 |
R-HSA-9768759 | Regulation of NPAS4 gene expression | 3.534582e-01 | 0.452 |
R-HSA-9909505 | Modulation of host responses by IFN-stimulated genes | 3.534582e-01 | 0.452 |
R-HSA-2408550 | Metabolism of ingested H2SeO4 and H2SeO3 into H2Se | 3.534582e-01 | 0.452 |
R-HSA-3858494 | Beta-catenin independent WNT signaling | 3.597279e-01 | 0.444 |
R-HSA-9018519 | Estrogen-dependent gene expression | 3.597279e-01 | 0.444 |
R-HSA-5578775 | Ion homeostasis | 3.619311e-01 | 0.441 |
R-HSA-193648 | NRAGE signals death through JNK | 3.619311e-01 | 0.441 |
R-HSA-9820952 | Respiratory Syncytial Virus Infection Pathway | 3.641865e-01 | 0.439 |
R-HSA-9665348 | Signaling by ERBB2 ECD mutants | 3.661577e-01 | 0.436 |
R-HSA-4419969 | Depolymerization of the Nuclear Lamina | 3.661577e-01 | 0.436 |
R-HSA-432142 | Platelet sensitization by LDL | 3.661577e-01 | 0.436 |
R-HSA-3928664 | Ephrin signaling | 3.661577e-01 | 0.436 |
R-HSA-975871 | MyD88 cascade initiated on plasma membrane | 3.664952e-01 | 0.436 |
R-HSA-168142 | Toll Like Receptor 10 (TLR10) Cascade | 3.664952e-01 | 0.436 |
R-HSA-168176 | Toll Like Receptor 5 (TLR5) Cascade | 3.664952e-01 | 0.436 |
R-HSA-1280218 | Adaptive Immune System | 3.684003e-01 | 0.434 |
R-HSA-9764561 | Regulation of CDH1 Function | 3.690011e-01 | 0.433 |
R-HSA-3700989 | Transcriptional Regulation by TP53 | 3.697603e-01 | 0.432 |
R-HSA-212165 | Epigenetic regulation of gene expression | 3.704092e-01 | 0.431 |
R-HSA-3214847 | HATs acetylate histones | 3.718403e-01 | 0.430 |
R-HSA-381119 | Unfolded Protein Response (UPR) | 3.730995e-01 | 0.428 |
R-HSA-9834899 | Specification of the neural plate border | 3.786085e-01 | 0.422 |
R-HSA-1237112 | Methionine salvage pathway | 3.786085e-01 | 0.422 |
R-HSA-1480926 | O2/CO2 exchange in erythrocytes | 3.786085e-01 | 0.422 |
R-HSA-1237044 | Erythrocytes take up carbon dioxide and release oxygen | 3.786085e-01 | 0.422 |
R-HSA-1632852 | Macroautophagy | 3.820032e-01 | 0.418 |
R-HSA-379724 | tRNA Aminoacylation | 3.900195e-01 | 0.409 |
R-HSA-163210 | Formation of ATP by chemiosmotic coupling | 3.908155e-01 | 0.408 |
R-HSA-9934037 | Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) | 3.908155e-01 | 0.408 |
R-HSA-1181150 | Signaling by NODAL | 3.908155e-01 | 0.408 |
R-HSA-5620922 | BBSome-mediated cargo-targeting to cilium | 3.908155e-01 | 0.408 |
R-HSA-202040 | G-protein activation | 4.027835e-01 | 0.395 |
R-HSA-450321 | JNK (c-Jun kinases) phosphorylation and activation mediated by activated human ... | 4.027835e-01 | 0.395 |
R-HSA-9931295 | PD-L1(CD274) glycosylation and translocation to plasma membrane | 4.027835e-01 | 0.395 |
R-HSA-210991 | Basigin interactions | 4.027835e-01 | 0.395 |
R-HSA-9833110 | RSV-host interactions | 4.037045e-01 | 0.394 |
R-HSA-375165 | NCAM signaling for neurite out-growth | 4.038581e-01 | 0.394 |
R-HSA-5696398 | Nucleotide Excision Repair | 4.089731e-01 | 0.388 |
R-HSA-168164 | Toll Like Receptor 3 (TLR3) Cascade | 4.089731e-01 | 0.388 |
R-HSA-9006927 | Signaling by Non-Receptor Tyrosine Kinases | 4.107214e-01 | 0.386 |
R-HSA-8848021 | Signaling by PTK6 | 4.107214e-01 | 0.386 |
R-HSA-418346 | Platelet homeostasis | 4.142278e-01 | 0.383 |
R-HSA-76066 | RNA Polymerase III Transcription Initiation From Type 2 Promoter | 4.145170e-01 | 0.382 |
R-HSA-8876384 | Listeria monocytogenes entry into host cells | 4.145170e-01 | 0.382 |
R-HSA-9617828 | FOXO-mediated transcription of cell cycle genes | 4.145170e-01 | 0.382 |
R-HSA-450302 | activated TAK1 mediates p38 MAPK activation | 4.145170e-01 | 0.382 |
R-HSA-9825892 | Regulation of MITF-M-dependent genes involved in cell cycle and proliferation | 4.145170e-01 | 0.382 |
R-HSA-8949215 | Mitochondrial calcium ion transport | 4.145170e-01 | 0.382 |
R-HSA-175474 | Assembly Of The HIV Virion | 4.145170e-01 | 0.382 |
R-HSA-166520 | Signaling by NTRKs | 4.174397e-01 | 0.379 |
R-HSA-9759476 | Regulation of Homotypic Cell-Cell Adhesion | 4.219902e-01 | 0.375 |
R-HSA-9734779 | Developmental Cell Lineages of the Integumentary System | 4.246919e-01 | 0.372 |
R-HSA-975138 | TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation | 4.246919e-01 | 0.372 |
R-HSA-76061 | RNA Polymerase III Transcription Initiation From Type 1 Promoter | 4.260208e-01 | 0.371 |
R-HSA-2173788 | Downregulation of TGF-beta receptor signaling | 4.260208e-01 | 0.371 |
R-HSA-8964038 | LDL clearance | 4.260208e-01 | 0.371 |
R-HSA-9013507 | NOTCH3 Activation and Transmission of Signal to the Nucleus | 4.260208e-01 | 0.371 |
R-HSA-6804115 | TP53 regulates transcription of additional cell cycle genes whose exact role in ... | 4.260208e-01 | 0.371 |
R-HSA-9679191 | Potential therapeutics for SARS | 4.262340e-01 | 0.370 |
R-HSA-9006925 | Intracellular signaling by second messengers | 4.270642e-01 | 0.370 |
R-HSA-975155 | MyD88 dependent cascade initiated on endosome | 4.299000e-01 | 0.367 |
R-HSA-1257604 | PIP3 activates AKT signaling | 4.325851e-01 | 0.364 |
R-HSA-9820448 | Developmental Cell Lineages of the Exocrine Pancreas | 4.349949e-01 | 0.362 |
R-HSA-937061 | TRIF (TICAM1)-mediated TLR4 signaling | 4.350913e-01 | 0.361 |
R-HSA-166166 | MyD88-independent TLR4 cascade | 4.350913e-01 | 0.361 |
R-HSA-5684996 | MAPK1/MAPK3 signaling | 4.357833e-01 | 0.361 |
R-HSA-912526 | Interleukin receptor SHC signaling | 4.372992e-01 | 0.359 |
R-HSA-164952 | The role of Nef in HIV-1 replication and disease pathogenesis | 4.372992e-01 | 0.359 |
R-HSA-400451 | Free fatty acids regulate insulin secretion | 4.372992e-01 | 0.359 |
R-HSA-9634638 | Estrogen-dependent nuclear events downstream of ESR-membrane signaling | 4.372992e-01 | 0.359 |
R-HSA-389948 | Co-inhibition by PD-1 | 4.374158e-01 | 0.359 |
R-HSA-167172 | Transcription of the HIV genome | 4.444325e-01 | 0.352 |
R-HSA-1650814 | Collagen biosynthesis and modifying enzymes | 4.444325e-01 | 0.352 |
R-HSA-948021 | Transport to the Golgi and subsequent modification | 4.450952e-01 | 0.352 |
R-HSA-9609646 | HCMV Infection | 4.454942e-01 | 0.351 |
R-HSA-9665686 | Signaling by ERBB2 TMD/JMD mutants | 4.483566e-01 | 0.348 |
R-HSA-75067 | Processing of Capped Intronless Pre-mRNA | 4.483566e-01 | 0.348 |
R-HSA-8963898 | Plasma lipoprotein assembly | 4.483566e-01 | 0.348 |
R-HSA-421270 | Cell-cell junction organization | 4.489583e-01 | 0.348 |
R-HSA-168181 | Toll Like Receptor 7/8 (TLR7/8) Cascade | 4.505574e-01 | 0.346 |
R-HSA-9843940 | Regulation of endogenous retroelements by KRAB-ZFP proteins | 4.576160e-01 | 0.339 |
R-HSA-9764560 | Regulation of CDH1 Gene Transcription | 4.576160e-01 | 0.339 |
R-HSA-1266695 | Interleukin-7 signaling | 4.591975e-01 | 0.338 |
R-HSA-420029 | Tight junction interactions | 4.591975e-01 | 0.338 |
R-HSA-9932444 | ATP-dependent chromatin remodelers | 4.591975e-01 | 0.338 |
R-HSA-9932451 | SWI/SNF chromatin remodelers | 4.591975e-01 | 0.338 |
R-HSA-9839394 | TGFBR3 expression | 4.591975e-01 | 0.338 |
R-HSA-9830364 | Formation of the nephric duct | 4.591975e-01 | 0.338 |
R-HSA-9856649 | Transcriptional and post-translational regulation of MITF-M expression and activ... | 4.641399e-01 | 0.333 |
R-HSA-6805567 | Keratinization | 4.641764e-01 | 0.333 |
R-HSA-877300 | Interferon gamma signaling | 4.653431e-01 | 0.332 |
R-HSA-168138 | Toll Like Receptor 9 (TLR9) Cascade | 4.658494e-01 | 0.332 |
R-HSA-8874081 | MET activates PTK2 signaling | 4.698259e-01 | 0.328 |
R-HSA-9703465 | Signaling by FLT3 fusion proteins | 4.698259e-01 | 0.328 |
R-HSA-525793 | Myogenesis | 4.698259e-01 | 0.328 |
R-HSA-3295583 | TRP channels | 4.698259e-01 | 0.328 |
R-HSA-2122948 | Activated NOTCH1 Transmits Signal to the Nucleus | 4.698259e-01 | 0.328 |
R-HSA-71387 | Metabolism of carbohydrates and carbohydrate derivatives | 4.698362e-01 | 0.328 |
R-HSA-9924644 | Developmental Lineages of the Mammary Gland | 4.706173e-01 | 0.327 |
R-HSA-450531 | Regulation of mRNA stability by proteins that bind AU-rich elements | 4.706173e-01 | 0.327 |
R-HSA-597592 | Post-translational protein modification | 4.743522e-01 | 0.324 |
R-HSA-4086398 | Ca2+ pathway | 4.770478e-01 | 0.321 |
R-HSA-1445148 | Translocation of SLC2A4 (GLUT4) to the plasma membrane | 4.770478e-01 | 0.321 |
R-HSA-167243 | Tat-mediated HIV elongation arrest and recovery | 4.802461e-01 | 0.319 |
R-HSA-167238 | Pausing and recovery of Tat-mediated HIV elongation | 4.802461e-01 | 0.319 |
R-HSA-73863 | RNA Polymerase I Transcription Termination | 4.802461e-01 | 0.319 |
R-HSA-8866652 | Synthesis of active ubiquitin: roles of E1 and E2 enzymes | 4.802461e-01 | 0.319 |
R-HSA-8949613 | Cristae formation | 4.802461e-01 | 0.319 |
R-HSA-4641262 | Disassembly of the destruction complex and recruitment of AXIN to the membrane | 4.802461e-01 | 0.319 |
R-HSA-75109 | Triglyceride biosynthesis | 4.802461e-01 | 0.319 |
R-HSA-1483213 | Synthesis of PE | 4.802461e-01 | 0.319 |
R-HSA-901032 | ER Quality Control Compartment (ERQC) | 4.802461e-01 | 0.319 |
R-HSA-2980736 | Peptide hormone metabolism | 4.809520e-01 | 0.318 |
R-HSA-674695 | RNA Polymerase II Pre-transcription Events | 4.834307e-01 | 0.316 |
R-HSA-1226099 | Signaling by FGFR in disease | 4.834307e-01 | 0.316 |
R-HSA-2219528 | PI3K/AKT Signaling in Cancer | 4.859417e-01 | 0.313 |
R-HSA-9006934 | Signaling by Receptor Tyrosine Kinases | 4.890222e-01 | 0.311 |
R-HSA-917937 | Iron uptake and transport | 4.897652e-01 | 0.310 |
R-HSA-167287 | HIV elongation arrest and recovery | 4.904622e-01 | 0.309 |
R-HSA-9619483 | Activation of AMPK downstream of NMDARs | 4.904622e-01 | 0.309 |
R-HSA-167290 | Pausing and recovery of HIV elongation | 4.904622e-01 | 0.309 |
R-HSA-5576892 | Phase 0 - rapid depolarisation | 4.904622e-01 | 0.309 |
R-HSA-5205685 | PINK1-PRKN Mediated Mitophagy | 4.904622e-01 | 0.309 |
R-HSA-166058 | MyD88:MAL(TIRAP) cascade initiated on plasma membrane | 4.909083e-01 | 0.309 |
R-HSA-168188 | Toll Like Receptor TLR6:TLR2 Cascade | 4.909083e-01 | 0.309 |
R-HSA-73854 | RNA Polymerase I Promoter Clearance | 4.960509e-01 | 0.304 |
R-HSA-5689603 | UCH proteinases | 4.960509e-01 | 0.304 |
R-HSA-9664565 | Signaling by ERBB2 KD Mutants | 5.004780e-01 | 0.301 |
R-HSA-9615710 | Late endosomal microautophagy | 5.004780e-01 | 0.301 |
R-HSA-5334118 | DNA methylation | 5.004780e-01 | 0.301 |
R-HSA-392154 | Nitric oxide stimulates guanylate cyclase | 5.004780e-01 | 0.301 |
R-HSA-168179 | Toll Like Receptor TLR1:TLR2 Cascade | 5.056652e-01 | 0.296 |
R-HSA-181438 | Toll Like Receptor 2 (TLR2) Cascade | 5.056652e-01 | 0.296 |
R-HSA-73864 | RNA Polymerase I Transcription | 5.084738e-01 | 0.294 |
R-HSA-6783783 | Interleukin-10 signaling | 5.084738e-01 | 0.294 |
R-HSA-416482 | G alpha (12/13) signalling events | 5.084738e-01 | 0.294 |
R-HSA-4086400 | PCP/CE pathway | 5.084738e-01 | 0.294 |
R-HSA-418990 | Adherens junctions interactions | 5.091023e-01 | 0.293 |
R-HSA-1227990 | Signaling by ERBB2 in Cancer | 5.102976e-01 | 0.292 |
R-HSA-1250196 | SHC1 events in ERBB2 signaling | 5.102976e-01 | 0.292 |
R-HSA-76046 | RNA Polymerase III Transcription Initiation | 5.102976e-01 | 0.292 |
R-HSA-8863795 | Downregulation of ERBB2 signaling | 5.102976e-01 | 0.292 |
R-HSA-456926 | Thrombin signalling through proteinase activated receptors (PARs) | 5.102976e-01 | 0.292 |
R-HSA-888590 | GABA synthesis, release, reuptake and degradation | 5.102976e-01 | 0.292 |
R-HSA-112311 | Neurotransmitter clearance | 5.102976e-01 | 0.292 |
R-HSA-186763 | Downstream signal transduction | 5.199247e-01 | 0.284 |
R-HSA-162588 | Budding and maturation of HIV virion | 5.199247e-01 | 0.284 |
R-HSA-9913351 | Formation of the dystrophin-glycoprotein complex (DGC) | 5.199247e-01 | 0.284 |
R-HSA-2995410 | Nuclear Envelope (NE) Reassembly | 5.206955e-01 | 0.283 |
R-HSA-5693607 | Processing of DNA double-strand break ends | 5.267300e-01 | 0.278 |
R-HSA-2151201 | Transcriptional activation of mitochondrial biogenesis | 5.267300e-01 | 0.278 |
R-HSA-4791275 | Signaling by WNT in cancer | 5.293632e-01 | 0.276 |
R-HSA-983231 | Factors involved in megakaryocyte development and platelet production | 5.363356e-01 | 0.271 |
R-HSA-354192 | Integrin signaling | 5.386167e-01 | 0.269 |
R-HSA-9930044 | Nuclear RNA decay | 5.386167e-01 | 0.269 |
R-HSA-8939243 | RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not kno... | 5.386167e-01 | 0.269 |
R-HSA-9733709 | Cardiogenesis | 5.386167e-01 | 0.269 |
R-HSA-69273 | Cyclin A/B1/B2 associated events during G2/M transition | 5.386167e-01 | 0.269 |
R-HSA-114508 | Effects of PIP2 hydrolysis | 5.476887e-01 | 0.261 |
R-HSA-5687128 | MAPK6/MAPK4 signaling | 5.503504e-01 | 0.259 |
R-HSA-6794362 | Protein-protein interactions at synapses | 5.503504e-01 | 0.259 |
R-HSA-9909615 | Regulation of PD-L1(CD274) Post-translational modification | 5.561249e-01 | 0.255 |
R-HSA-5205647 | Mitophagy | 5.565830e-01 | 0.254 |
R-HSA-168638 | NOD1/2 Signaling Pathway | 5.565830e-01 | 0.254 |
R-HSA-203615 | eNOS activation | 5.565830e-01 | 0.254 |
R-HSA-5576891 | Cardiac conduction | 5.577876e-01 | 0.254 |
R-HSA-6807505 | RNA polymerase II transcribes snRNA genes | 5.618468e-01 | 0.250 |
R-HSA-1474228 | Degradation of the extracellular matrix | 5.623611e-01 | 0.250 |
R-HSA-917977 | Transferrin endocytosis and recycling | 5.653029e-01 | 0.248 |
R-HSA-2559585 | Oncogene Induced Senescence | 5.653029e-01 | 0.248 |
R-HSA-381042 | PERK regulates gene expression | 5.653029e-01 | 0.248 |
R-HSA-9772755 | Formation of WDR5-containing histone-modifying complexes | 5.653029e-01 | 0.248 |
R-HSA-212300 | PRC2 methylates histones and DNA | 5.738518e-01 | 0.241 |
R-HSA-450408 | AUF1 (hnRNP D0) binds and destabilizes mRNA | 5.738518e-01 | 0.241 |
R-HSA-74158 | RNA Polymerase III Transcription | 5.738518e-01 | 0.241 |
R-HSA-749476 | RNA Polymerase III Abortive And Retractive Initiation | 5.738518e-01 | 0.241 |
R-HSA-9682385 | FLT3 signaling in disease | 5.738518e-01 | 0.241 |
R-HSA-5673001 | RAF/MAP kinase cascade | 5.753092e-01 | 0.240 |
R-HSA-8939211 | ESR-mediated signaling | 5.768671e-01 | 0.239 |
R-HSA-3769402 | Deactivation of the beta-catenin transactivating complex | 5.822332e-01 | 0.235 |
R-HSA-6802948 | Signaling by high-kinase activity BRAF mutants | 5.822332e-01 | 0.235 |
R-HSA-163685 | Integration of energy metabolism | 5.847942e-01 | 0.233 |
R-HSA-8875878 | MET promotes cell motility | 5.904502e-01 | 0.229 |
R-HSA-202131 | Metabolism of nitric oxide: NOS3 activation and regulation | 5.904502e-01 | 0.229 |
R-HSA-1266738 | Developmental Biology | 5.923711e-01 | 0.227 |
R-HSA-6807070 | PTEN Regulation | 5.978987e-01 | 0.223 |
R-HSA-9725554 | Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin | 5.985060e-01 | 0.223 |
R-HSA-167200 | Formation of HIV-1 elongation complex containing HIV-1 Tat | 5.985060e-01 | 0.223 |
R-HSA-8964043 | Plasma lipoprotein clearance | 5.985060e-01 | 0.223 |
R-HSA-381771 | Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) | 5.985060e-01 | 0.223 |
R-HSA-9931509 | Expression of BMAL (ARNTL), CLOCK, and NPAS2 | 5.985060e-01 | 0.223 |
R-HSA-9820965 | Respiratory syncytial virus (RSV) genome replication, transcription and translat... | 5.985060e-01 | 0.223 |
R-HSA-168898 | Toll-like Receptor Cascades | 5.985922e-01 | 0.223 |
R-HSA-174824 | Plasma lipoprotein assembly, remodeling, and clearance | 6.004145e-01 | 0.222 |
R-HSA-983695 | Antigen activates B Cell Receptor (BCR) leading to generation of second messenge... | 6.057113e-01 | 0.218 |
R-HSA-73779 | RNA Polymerase II Transcription Pre-Initiation And Promoter Opening | 6.064040e-01 | 0.217 |
R-HSA-5696395 | Formation of Incision Complex in GG-NER | 6.064040e-01 | 0.217 |
R-HSA-167246 | Tat-mediated elongation of the HIV-1 transcript | 6.064040e-01 | 0.217 |
R-HSA-427389 | ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression | 6.064040e-01 | 0.217 |
R-HSA-167152 | Formation of HIV elongation complex in the absence of HIV Tat | 6.064040e-01 | 0.217 |
R-HSA-9646399 | Aggrephagy | 6.064040e-01 | 0.217 |
R-HSA-167169 | HIV Transcription Elongation | 6.064040e-01 | 0.217 |
R-HSA-9854311 | Maturation of TCA enzymes and regulation of TCA cycle | 6.064040e-01 | 0.217 |
R-HSA-9694548 | Maturation of spike protein | 6.141470e-01 | 0.212 |
R-HSA-8853884 | Transcriptional Regulation by VENTX | 6.141470e-01 | 0.212 |
R-HSA-73817 | Purine ribonucleoside monophosphate biosynthesis | 6.141470e-01 | 0.212 |
R-HSA-167161 | HIV Transcription Initiation | 6.217381e-01 | 0.206 |
R-HSA-75953 | RNA Polymerase II Transcription Initiation | 6.217381e-01 | 0.206 |
R-HSA-5674135 | MAP2K and MAPK activation | 6.217381e-01 | 0.206 |
R-HSA-167162 | RNA Polymerase II HIV Promoter Escape | 6.217381e-01 | 0.206 |
R-HSA-9656223 | Signaling by RAF1 mutants | 6.217381e-01 | 0.206 |
R-HSA-3000480 | Scavenging by Class A Receptors | 6.217381e-01 | 0.206 |
R-HSA-6811438 | Intra-Golgi traffic | 6.217381e-01 | 0.206 |
R-HSA-442660 | SLC-mediated transport of neurotransmitters | 6.217381e-01 | 0.206 |
R-HSA-9683701 | Translation of Structural Proteins | 6.217381e-01 | 0.206 |
R-HSA-512988 | Interleukin-3, Interleukin-5 and GM-CSF signaling | 6.291804e-01 | 0.201 |
R-HSA-381676 | Glucagon-like Peptide-1 (GLP1) regulates insulin secretion | 6.291804e-01 | 0.201 |
R-HSA-400508 | Incretin synthesis, secretion, and inactivation | 6.291804e-01 | 0.201 |
R-HSA-5688426 | Deubiquitination | 6.362535e-01 | 0.196 |
R-HSA-8957275 | Post-translational protein phosphorylation | 6.363759e-01 | 0.196 |
R-HSA-422356 | Regulation of insulin secretion | 6.363759e-01 | 0.196 |
R-HSA-73776 | RNA Polymerase II Promoter Escape | 6.364767e-01 | 0.196 |
R-HSA-9710421 | Defective pyroptosis | 6.364767e-01 | 0.196 |
R-HSA-2173789 | TGF-beta receptor signaling activates SMADs | 6.364767e-01 | 0.196 |
R-HSA-75876 | Synthesis of very long-chain fatty acyl-CoAs | 6.364767e-01 | 0.196 |
R-HSA-388841 | Regulation of T cell activation by CD28 family | 6.393995e-01 | 0.194 |
R-HSA-166016 | Toll Like Receptor 4 (TLR4) Cascade | 6.395967e-01 | 0.194 |
R-HSA-9758941 | Gastrulation | 6.435960e-01 | 0.191 |
R-HSA-190828 | Gap junction trafficking | 6.436299e-01 | 0.191 |
R-HSA-3928662 | EPHB-mediated forward signaling | 6.436299e-01 | 0.191 |
R-HSA-156581 | Methylation | 6.436299e-01 | 0.191 |
R-HSA-2173782 | Binding and Uptake of Ligands by Scavenger Receptors | 6.475640e-01 | 0.189 |
R-HSA-76042 | RNA Polymerase II Transcription Initiation And Promoter Clearance | 6.506427e-01 | 0.187 |
R-HSA-76009 | Platelet Aggregation (Plug Formation) | 6.506427e-01 | 0.187 |
R-HSA-9824272 | Somitogenesis | 6.506427e-01 | 0.187 |
R-HSA-1489509 | DAG and IP3 signaling | 6.506427e-01 | 0.187 |
R-HSA-9020702 | Interleukin-1 signaling | 6.509952e-01 | 0.186 |
R-HSA-6802946 | Signaling by moderate kinase activity BRAF mutants | 6.575180e-01 | 0.182 |
R-HSA-6802955 | Paradoxical activation of RAF signaling by kinase inactive BRAF | 6.575180e-01 | 0.182 |
R-HSA-9649948 | Signaling downstream of RAS mutants | 6.575180e-01 | 0.182 |
R-HSA-6802949 | Signaling by RAS mutants | 6.575180e-01 | 0.182 |
R-HSA-6781823 | Formation of TC-NER Pre-Incision Complex | 6.575180e-01 | 0.182 |
R-HSA-2514859 | Inactivation, recovery and regulation of the phototransduction cascade | 6.575180e-01 | 0.182 |
R-HSA-5693532 | DNA Double-Strand Break Repair | 6.592798e-01 | 0.181 |
R-HSA-9609507 | Protein localization | 6.592798e-01 | 0.181 |
R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | 6.642584e-01 | 0.178 |
R-HSA-3928665 | EPH-ephrin mediated repulsion of cells | 6.642584e-01 | 0.178 |
R-HSA-1483191 | Synthesis of PC | 6.642584e-01 | 0.178 |
R-HSA-111885 | Opioid Signalling | 6.651445e-01 | 0.177 |
R-HSA-1989781 | PPARA activates gene expression | 6.669334e-01 | 0.176 |
R-HSA-9725371 | Nuclear events stimulated by ALK signaling in cancer | 6.708665e-01 | 0.173 |
R-HSA-8963899 | Plasma lipoprotein remodeling | 6.708665e-01 | 0.173 |
R-HSA-400206 | Regulation of lipid metabolism by PPARalpha | 6.744614e-01 | 0.171 |
R-HSA-157858 | Gap junction trafficking and regulation | 6.773450e-01 | 0.169 |
R-HSA-983705 | Signaling by the B Cell Receptor (BCR) | 6.781783e-01 | 0.169 |
R-HSA-5358346 | Hedgehog ligand biogenesis | 6.899231e-01 | 0.161 |
R-HSA-2514856 | The phototransduction cascade | 6.899231e-01 | 0.161 |
R-HSA-983169 | Class I MHC mediated antigen processing & presentation | 6.901291e-01 | 0.161 |
R-HSA-73772 | RNA Polymerase I Promoter Escape | 6.960276e-01 | 0.157 |
R-HSA-112382 | Formation of RNA Pol II elongation complex | 6.960276e-01 | 0.157 |
R-HSA-9931269 | AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) | 6.960276e-01 | 0.157 |
R-HSA-9634815 | Transcriptional Regulation by NPAS4 | 6.960276e-01 | 0.157 |
R-HSA-5339562 | Uptake and actions of bacterial toxins | 6.960276e-01 | 0.157 |
R-HSA-75955 | RNA Polymerase II Transcription Elongation | 7.020123e-01 | 0.154 |
R-HSA-1221632 | Meiotic synapsis | 7.020123e-01 | 0.154 |
R-HSA-8956320 | Nucleotide biosynthesis | 7.020123e-01 | 0.154 |
R-HSA-8951664 | Neddylation | 7.038867e-01 | 0.152 |
R-HSA-156588 | Glucuronidation | 7.078795e-01 | 0.150 |
R-HSA-5693567 | HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA) | 7.131004e-01 | 0.147 |
R-HSA-3214815 | HDACs deacetylate histones | 7.136316e-01 | 0.147 |
R-HSA-9012852 | Signaling by NOTCH3 | 7.136316e-01 | 0.147 |
R-HSA-983168 | Antigen processing: Ubiquitination & Proteasome degradation | 7.151361e-01 | 0.146 |
R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-l... | 7.171622e-01 | 0.144 |
R-HSA-109606 | Intrinsic Pathway for Apoptosis | 7.192707e-01 | 0.143 |
R-HSA-5628897 | TP53 Regulates Metabolic Genes | 7.211757e-01 | 0.142 |
R-HSA-6791312 | TP53 Regulates Transcription of Cell Cycle Genes | 7.247992e-01 | 0.140 |
R-HSA-201722 | Formation of the beta-catenin:TCF transactivating complex | 7.302191e-01 | 0.137 |
R-HSA-5689880 | Ub-specific processing proteases | 7.334136e-01 | 0.135 |
R-HSA-5693565 | Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at... | 7.355325e-01 | 0.133 |
R-HSA-8979227 | Triglyceride metabolism | 7.355325e-01 | 0.133 |
R-HSA-2022090 | Assembly of collagen fibrils and other multimeric structures | 7.355325e-01 | 0.133 |
R-HSA-2029480 | Fcgamma receptor (FCGR) dependent phagocytosis | 7.366046e-01 | 0.133 |
R-HSA-5693538 | Homology Directed Repair | 7.367532e-01 | 0.133 |
R-HSA-1227986 | Signaling by ERBB2 | 7.407417e-01 | 0.130 |
R-HSA-1660661 | Sphingolipid de novo biosynthesis | 7.407417e-01 | 0.130 |
R-HSA-9764725 | Negative Regulation of CDH1 Gene Transcription | 7.407417e-01 | 0.130 |
R-HSA-9793380 | Formation of paraxial mesoderm | 7.458486e-01 | 0.127 |
R-HSA-8939902 | Regulation of RUNX2 expression and activity | 7.458486e-01 | 0.127 |
R-HSA-112043 | PLC beta mediated events | 7.458486e-01 | 0.127 |
R-HSA-73886 | Chromosome Maintenance | 7.479455e-01 | 0.126 |
R-HSA-9635486 | Infection with Mycobacterium tuberculosis | 7.479455e-01 | 0.126 |
R-HSA-186797 | Signaling by PDGF | 7.508552e-01 | 0.124 |
R-HSA-9707616 | Heme signaling | 7.508552e-01 | 0.124 |
R-HSA-162582 | Signal Transduction | 7.557535e-01 | 0.122 |
R-HSA-2426168 | Activation of gene expression by SREBF (SREBP) | 7.557634e-01 | 0.122 |
R-HSA-6790901 | rRNA modification in the nucleus and cytosol | 7.557634e-01 | 0.122 |
R-HSA-168643 | Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signali... | 7.605753e-01 | 0.119 |
R-HSA-73894 | DNA Repair | 7.648570e-01 | 0.116 |
R-HSA-6802952 | Signaling by BRAF and RAF1 fusions | 7.652927e-01 | 0.116 |
R-HSA-5693606 | DNA Double Strand Break Response | 7.744512e-01 | 0.111 |
R-HSA-112040 | G-protein mediated events | 7.744512e-01 | 0.111 |
R-HSA-9830369 | Kidney development | 7.744512e-01 | 0.111 |
R-HSA-446203 | Asparagine N-linked glycosylation | 7.758187e-01 | 0.110 |
R-HSA-195253 | Degradation of beta-catenin by the destruction complex | 7.875253e-01 | 0.104 |
R-HSA-204005 | COPII-mediated vesicle transport | 7.875253e-01 | 0.104 |
R-HSA-1834949 | Cytosolic sensors of pathogen-associated DNA | 7.875253e-01 | 0.104 |
R-HSA-1168372 | Downstream signaling events of B Cell Receptor (BCR) | 7.875253e-01 | 0.104 |
R-HSA-75105 | Fatty acyl-CoA biosynthesis | 7.875253e-01 | 0.104 |
R-HSA-9843745 | Adipogenesis | 7.887133e-01 | 0.103 |
R-HSA-427413 | NoRC negatively regulates rRNA expression | 7.917132e-01 | 0.101 |
R-HSA-5632684 | Hedgehog 'on' state | 7.917132e-01 | 0.101 |
R-HSA-5620920 | Cargo trafficking to the periciliary membrane | 7.917132e-01 | 0.101 |
R-HSA-499943 | Interconversion of nucleotide di- and triphosphates | 7.958188e-01 | 0.099 |
R-HSA-69473 | G2/M DNA damage checkpoint | 8.037896e-01 | 0.095 |
R-HSA-1222556 | ROS and RNS production in phagocytes | 8.037896e-01 | 0.095 |
R-HSA-8852135 | Protein ubiquitination | 8.076579e-01 | 0.093 |
R-HSA-3000171 | Non-integrin membrane-ECM interactions | 8.076579e-01 | 0.093 |
R-HSA-71403 | Citric acid cycle (TCA cycle) | 8.076579e-01 | 0.093 |
R-HSA-6781827 | Transcription-Coupled Nucleotide Excision Repair (TC-NER) | 8.076579e-01 | 0.093 |
R-HSA-1980143 | Signaling by NOTCH1 | 8.114502e-01 | 0.091 |
R-HSA-5358351 | Signaling by Hedgehog | 8.125677e-01 | 0.090 |
R-HSA-9694635 | Translation of Structural Proteins | 8.151679e-01 | 0.089 |
R-HSA-71291 | Metabolism of amino acids and derivatives | 8.158352e-01 | 0.088 |
R-HSA-9664417 | Leishmania phagocytosis | 8.181441e-01 | 0.087 |
R-HSA-9664407 | Parasite infection | 8.181441e-01 | 0.087 |
R-HSA-9664422 | FCGR3A-mediated phagocytosis | 8.181441e-01 | 0.087 |
R-HSA-2029482 | Regulation of actin dynamics for phagocytic cup formation | 8.208764e-01 | 0.086 |
R-HSA-1655829 | Regulation of cholesterol biosynthesis by SREBP (SREBF) | 8.223856e-01 | 0.085 |
R-HSA-6806834 | Signaling by MET | 8.258883e-01 | 0.083 |
R-HSA-5250941 | Negative epigenetic regulation of rRNA expression | 8.258883e-01 | 0.083 |
R-HSA-2559582 | Senescence-Associated Secretory Phenotype (SASP) | 8.326886e-01 | 0.080 |
R-HSA-453279 | Mitotic G1 phase and G1/S transition | 8.365112e-01 | 0.078 |
R-HSA-9730414 | MITF-M-regulated melanocyte development | 8.410296e-01 | 0.075 |
R-HSA-6802957 | Oncogenic MAPK signaling | 8.423957e-01 | 0.074 |
R-HSA-1500620 | Meiosis | 8.423957e-01 | 0.074 |
R-HSA-8876198 | RAB GEFs exchange GTP for GDP on RABs | 8.455050e-01 | 0.073 |
R-HSA-9856651 | MITF-M-dependent gene expression | 8.462397e-01 | 0.073 |
R-HSA-9658195 | Leishmania infection | 8.479777e-01 | 0.072 |
R-HSA-9824443 | Parasitic Infection Pathways | 8.479777e-01 | 0.072 |
R-HSA-1614635 | Sulfur amino acid metabolism | 8.485532e-01 | 0.071 |
R-HSA-446652 | Interleukin-1 family signaling | 8.509047e-01 | 0.070 |
R-HSA-438064 | Post NMDA receptor activation events | 8.515414e-01 | 0.070 |
R-HSA-1236974 | ER-Phagosome pathway | 8.573425e-01 | 0.067 |
R-HSA-112310 | Neurotransmitter release cycle | 8.601578e-01 | 0.065 |
R-HSA-373080 | Class B/2 (Secretin family receptors) | 8.601578e-01 | 0.065 |
R-HSA-1912408 | Pre-NOTCH Transcription and Translation | 8.629177e-01 | 0.064 |
R-HSA-381070 | IRE1alpha activates chaperones | 8.656233e-01 | 0.063 |
R-HSA-9772573 | Late SARS-CoV-2 Infection Events | 8.682757e-01 | 0.061 |
R-HSA-195721 | Signaling by WNT | 8.760998e-01 | 0.057 |
R-HSA-9006931 | Signaling by Nuclear Receptors | 8.771741e-01 | 0.057 |
R-HSA-5389840 | Mitochondrial translation elongation | 8.807748e-01 | 0.055 |
R-HSA-5607764 | CLEC7A (Dectin-1) signaling | 8.807748e-01 | 0.055 |
R-HSA-8878159 | Transcriptional regulation by RUNX3 | 8.831289e-01 | 0.054 |
R-HSA-202733 | Cell surface interactions at the vascular wall | 8.847920e-01 | 0.053 |
R-HSA-192105 | Synthesis of bile acids and bile salts | 8.876992e-01 | 0.052 |
R-HSA-157118 | Signaling by NOTCH | 8.894335e-01 | 0.051 |
R-HSA-9009391 | Extra-nuclear estrogen signaling | 8.920912e-01 | 0.050 |
R-HSA-2559580 | Oxidative Stress Induced Senescence | 8.942226e-01 | 0.049 |
R-HSA-442755 | Activation of NMDA receptors and postsynaptic events | 8.942226e-01 | 0.049 |
R-HSA-9662851 | Anti-inflammatory response favouring Leishmania parasite infection | 8.943385e-01 | 0.048 |
R-HSA-9664433 | Leishmania parasite growth and survival | 8.943385e-01 | 0.048 |
R-HSA-5617472 | Activation of anterior HOX genes in hindbrain development during early embryogen... | 9.003682e-01 | 0.046 |
R-HSA-5619507 | Activation of HOX genes during differentiation | 9.003682e-01 | 0.046 |
R-HSA-2559583 | Cellular Senescence | 9.054860e-01 | 0.043 |
R-HSA-1236975 | Antigen processing-Cross presentation | 9.080121e-01 | 0.042 |
R-HSA-2672351 | Stimuli-sensing channels | 9.080121e-01 | 0.042 |
R-HSA-194068 | Bile acid and bile salt metabolism | 9.116119e-01 | 0.040 |
R-HSA-6803157 | Antimicrobial peptides | 9.133588e-01 | 0.039 |
R-HSA-375276 | Peptide ligand-binding receptors | 9.141582e-01 | 0.039 |
R-HSA-2871796 | FCERI mediated MAPK activation | 9.150713e-01 | 0.039 |
R-HSA-1912422 | Pre-NOTCH Expression and Processing | 9.167500e-01 | 0.038 |
R-HSA-2871809 | FCERI mediated Ca+2 mobilization | 9.231406e-01 | 0.035 |
R-HSA-2029485 | Role of phospholipids in phagocytosis | 9.231406e-01 | 0.035 |
R-HSA-9007101 | Rab regulation of trafficking | 9.261500e-01 | 0.033 |
R-HSA-8878166 | Transcriptional regulation by RUNX2 | 9.290420e-01 | 0.032 |
R-HSA-2454202 | Fc epsilon receptor (FCERI) signaling | 9.348518e-01 | 0.029 |
R-HSA-977606 | Regulation of Complement cascade | 9.370579e-01 | 0.028 |
R-HSA-9664323 | FCGR3A-mediated IL10 synthesis | 9.395239e-01 | 0.027 |
R-HSA-69481 | G2/M Checkpoints | 9.407205e-01 | 0.027 |
R-HSA-1474165 | Reproduction | 9.452757e-01 | 0.024 |
R-HSA-9909396 | Circadian clock | 9.474207e-01 | 0.023 |
R-HSA-5368287 | Mitochondrial translation | 9.542891e-01 | 0.020 |
R-HSA-166658 | Complement cascade | 9.610501e-01 | 0.017 |
R-HSA-2187338 | Visual phototransduction | 9.625784e-01 | 0.017 |
R-HSA-15869 | Metabolism of nucleotides | 9.629361e-01 | 0.016 |
R-HSA-9824439 | Bacterial Infection Pathways | 9.632188e-01 | 0.016 |
R-HSA-156580 | Phase II - Conjugation of compounds | 9.647603e-01 | 0.016 |
R-HSA-112316 | Neuronal System | 9.661980e-01 | 0.015 |
R-HSA-112315 | Transmission across Chemical Synapses | 9.667435e-01 | 0.015 |
R-HSA-9917777 | Epigenetic regulation by WDR5-containing histone modifying complexes | 9.674716e-01 | 0.014 |
R-HSA-416476 | G alpha (q) signalling events | 9.769503e-01 | 0.010 |
R-HSA-418555 | G alpha (s) signalling events | 9.773201e-01 | 0.010 |
R-HSA-5621481 | C-type lectin receptors (CLRs) | 9.773201e-01 | 0.010 |
R-HSA-201681 | TCF dependent signaling in response to WNT | 9.821709e-01 | 0.008 |
R-HSA-983712 | Ion channel transport | 9.841932e-01 | 0.007 |
R-HSA-428157 | Sphingolipid metabolism | 9.875774e-01 | 0.005 |
R-HSA-1483206 | Glycerophospholipid biosynthesis | 9.880666e-01 | 0.005 |
R-HSA-425407 | SLC-mediated transmembrane transport | 9.896597e-01 | 0.005 |
R-HSA-112314 | Neurotransmitter receptors and postsynaptic signal transmission | 9.902388e-01 | 0.004 |
R-HSA-418594 | G alpha (i) signalling events | 9.911923e-01 | 0.004 |
R-HSA-8957322 | Metabolism of steroids | 9.918816e-01 | 0.004 |
R-HSA-8878171 | Transcriptional regulation by RUNX1 | 9.926339e-01 | 0.003 |
R-HSA-198933 | Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell | 9.930653e-01 | 0.003 |
R-HSA-196849 | Metabolism of water-soluble vitamins and cofactors | 9.932034e-01 | 0.003 |
R-HSA-1428517 | Aerobic respiration and respiratory electron transport | 9.939920e-01 | 0.003 |
R-HSA-373076 | Class A/1 (Rhodopsin-like receptors) | 9.977212e-01 | 0.001 |
R-HSA-1483257 | Phospholipid metabolism | 9.981673e-01 | 0.001 |
R-HSA-382551 | Transport of small molecules | 9.981995e-01 | 0.001 |
R-HSA-388396 | GPCR downstream signalling | 9.986393e-01 | 0.001 |
R-HSA-372790 | Signaling by GPCR | 9.987316e-01 | 0.001 |
R-HSA-196854 | Metabolism of vitamins and cofactors | 9.995468e-01 | 0.000 |
R-HSA-500792 | GPCR ligand binding | 9.995882e-01 | 0.000 |
R-HSA-211859 | Biological oxidations | 9.997893e-01 | 0.000 |
R-HSA-8978868 | Fatty acid metabolism | 9.998147e-01 | 0.000 |
R-HSA-9709957 | Sensory Perception | 9.999965e-01 | 0.000 |
R-HSA-556833 | Metabolism of lipids | 1.000000e+00 | 0.000 |
R-HSA-1430728 | Metabolism | 1.000000e+00 | 0.000 |
Download
kinase | JSD_mean | pearson_surrounding | kinase_max_IC_position | max_position_JSD |
---|---|---|---|---|
GAK |
0.877 | -0.023 | 1 | 0.865 |
PRP4 |
0.875 | 0.431 | -3 | 0.907 |
VRK2 |
0.874 | -0.103 | 1 | 0.921 |
PKR |
0.874 | 0.056 | 1 | 0.882 |
TTK |
0.873 | 0.234 | -2 | 0.905 |
VRK1 |
0.868 | -0.114 | 2 | 0.821 |
BMPR2 |
0.868 | 0.162 | -2 | 0.889 |
BRAF |
0.867 | -0.021 | -4 | 0.845 |
MEKK2 |
0.865 | 0.015 | 2 | 0.796 |
TAK1 |
0.864 | -0.170 | 1 | 0.818 |
LKB1 |
0.864 | 0.007 | -3 | 0.792 |
MST1 |
0.864 | -0.047 | 1 | 0.816 |
ALK4 |
0.864 | 0.077 | -2 | 0.828 |
MST2 |
0.863 | -0.025 | 1 | 0.819 |
ALPHAK3 |
0.863 | 0.004 | -1 | 0.799 |
TNIK |
0.863 | -0.042 | 3 | 0.877 |
MINK |
0.862 | -0.088 | 1 | 0.808 |
MEK1 |
0.862 | -0.149 | 2 | 0.867 |
OSR1 |
0.862 | 0.012 | 2 | 0.789 |
EEF2K |
0.861 | -0.034 | 3 | 0.846 |
NEK1 |
0.861 | -0.131 | 1 | 0.840 |
CAMKK1 |
0.861 | -0.096 | -2 | 0.765 |
BIKE |
0.861 | 0.028 | 1 | 0.758 |
ALK2 |
0.860 | 0.128 | -2 | 0.824 |
GCK |
0.860 | -0.070 | 1 | 0.801 |
LRRK2 |
0.860 | -0.224 | 2 | 0.825 |
NEK5 |
0.860 | -0.055 | 1 | 0.860 |
ASK1 |
0.859 | -0.187 | 1 | 0.789 |
TGFBR1 |
0.858 | 0.132 | -2 | 0.804 |
CAMKK2 |
0.858 | -0.119 | -2 | 0.751 |
NIK |
0.857 | -0.142 | -3 | 0.792 |
PDK1 |
0.857 | -0.138 | 1 | 0.829 |
MEK5 |
0.857 | -0.232 | 2 | 0.821 |
TAO2 |
0.857 | -0.128 | 2 | 0.819 |
HGK |
0.857 | -0.090 | 3 | 0.875 |
MEKK1 |
0.856 | -0.059 | 1 | 0.856 |
PRPK |
0.856 | -0.068 | -1 | 0.865 |
MOS |
0.856 | 0.093 | 1 | 0.864 |
ANKRD3 |
0.856 | -0.038 | 1 | 0.883 |
JNK3 |
0.855 | 0.186 | 1 | 0.786 |
JNK2 |
0.855 | 0.192 | 1 | 0.749 |
TAO3 |
0.855 | -0.043 | 1 | 0.828 |
CAMLCK |
0.854 | -0.074 | -2 | 0.795 |
STLK3 |
0.854 | -0.127 | 1 | 0.787 |
DAPK2 |
0.854 | -0.116 | -3 | 0.776 |
ACVR2A |
0.853 | 0.212 | -2 | 0.883 |
MEK2 |
0.853 | -0.190 | 2 | 0.825 |
PLK1 |
0.853 | 0.233 | -2 | 0.901 |
MYO3B |
0.853 | -0.071 | 2 | 0.779 |
DLK |
0.853 | -0.136 | 1 | 0.842 |
ACVR2B |
0.852 | 0.189 | -2 | 0.880 |
NEK8 |
0.852 | -0.116 | 2 | 0.785 |
KHS1 |
0.852 | -0.097 | 1 | 0.804 |
MEKK3 |
0.852 | -0.061 | 1 | 0.827 |
LATS1 |
0.852 | 0.072 | -3 | 0.758 |
CAMK1B |
0.851 | -0.052 | -3 | 0.765 |
MAP3K15 |
0.851 | -0.200 | 1 | 0.802 |
PERK |
0.851 | 0.092 | -2 | 0.895 |
MYO3A |
0.851 | -0.114 | 1 | 0.825 |
P38A |
0.851 | 0.156 | 1 | 0.830 |
TLK2 |
0.851 | 0.127 | 1 | 0.829 |
NLK |
0.850 | 0.084 | 1 | 0.919 |
KHS2 |
0.850 | -0.065 | 1 | 0.806 |
NEK4 |
0.849 | -0.178 | 1 | 0.827 |
P38B |
0.849 | 0.175 | 1 | 0.771 |
ATR |
0.849 | -0.014 | 1 | 0.860 |
AAK1 |
0.849 | 0.060 | 1 | 0.663 |
PBK |
0.848 | -0.043 | 1 | 0.806 |
HRI |
0.848 | 0.058 | -2 | 0.906 |
YSK4 |
0.848 | -0.074 | 1 | 0.790 |
ZAK |
0.847 | -0.092 | 1 | 0.811 |
BMPR1B |
0.846 | 0.115 | 1 | 0.710 |
CAMK2G |
0.846 | 0.105 | 2 | 0.899 |
PASK |
0.846 | -0.047 | -3 | 0.763 |
ICK |
0.846 | 0.017 | -3 | 0.742 |
TLK1 |
0.846 | 0.087 | -2 | 0.864 |
MST3 |
0.846 | -0.117 | 2 | 0.782 |
MPSK1 |
0.845 | -0.065 | 1 | 0.846 |
DMPK1 |
0.845 | -0.017 | -3 | 0.645 |
CDKL1 |
0.845 | -0.026 | -3 | 0.719 |
YSK1 |
0.844 | -0.159 | 2 | 0.763 |
HPK1 |
0.844 | -0.164 | 1 | 0.788 |
MEKK6 |
0.843 | -0.244 | 1 | 0.820 |
PLK3 |
0.843 | 0.182 | 2 | 0.833 |
COT |
0.841 | 0.215 | 2 | 0.868 |
SMMLCK |
0.840 | -0.113 | -3 | 0.721 |
DSTYK |
0.840 | 0.164 | 2 | 0.867 |
NEK11 |
0.840 | -0.280 | 1 | 0.813 |
P38G |
0.840 | 0.190 | 1 | 0.685 |
GRK7 |
0.840 | 0.125 | 1 | 0.782 |
DAPK3 |
0.840 | -0.070 | -3 | 0.693 |
BMPR1A |
0.840 | 0.101 | 1 | 0.688 |
ERK5 |
0.839 | 0.052 | 1 | 0.874 |
LOK |
0.839 | -0.134 | -2 | 0.739 |
P38D |
0.839 | 0.197 | 1 | 0.708 |
GRK6 |
0.838 | 0.007 | 1 | 0.822 |
PINK1 |
0.838 | -0.043 | 1 | 0.899 |
MLK2 |
0.838 | -0.141 | 2 | 0.799 |
RAF1 |
0.837 | -0.135 | 1 | 0.841 |
NEK9 |
0.837 | -0.088 | 2 | 0.809 |
ROCK2 |
0.836 | -0.052 | -3 | 0.675 |
CLK3 |
0.836 | 0.229 | 1 | 0.888 |
SKMLCK |
0.836 | -0.041 | -2 | 0.771 |
PDHK4 |
0.835 | -0.196 | 1 | 0.879 |
JNK1 |
0.835 | 0.155 | 1 | 0.739 |
MLK1 |
0.834 | -0.081 | 2 | 0.784 |
ERK2 |
0.834 | 0.109 | 1 | 0.799 |
PLK2 |
0.834 | 0.173 | -3 | 0.800 |
PDHK1 |
0.833 | -0.152 | 1 | 0.878 |
GRK5 |
0.833 | -0.112 | -3 | 0.793 |
DNAPK |
0.833 | 0.069 | 1 | 0.742 |
HIPK1 |
0.832 | 0.116 | 1 | 0.860 |
CDK1 |
0.831 | 0.187 | 1 | 0.753 |
DYRK2 |
0.831 | 0.157 | 1 | 0.847 |
TAO1 |
0.830 | -0.141 | 1 | 0.770 |
MASTL |
0.830 | -0.281 | -2 | 0.783 |
TGFBR2 |
0.829 | 0.159 | -2 | 0.872 |
CDK5 |
0.829 | 0.156 | 1 | 0.814 |
CHAK2 |
0.829 | -0.079 | -1 | 0.832 |
TSSK2 |
0.829 | -0.065 | -5 | 0.808 |
PIM1 |
0.829 | 0.027 | -3 | 0.668 |
ATM |
0.828 | 0.062 | 1 | 0.784 |
PKN3 |
0.828 | -0.059 | -3 | 0.741 |
NEK3 |
0.828 | -0.148 | 1 | 0.813 |
NEK6 |
0.827 | 0.161 | -2 | 0.900 |
NEK2 |
0.827 | -0.147 | 2 | 0.776 |
SLK |
0.827 | -0.136 | -2 | 0.694 |
MLK4 |
0.827 | -0.019 | 2 | 0.704 |
PIM3 |
0.827 | 0.016 | -3 | 0.741 |
NEK7 |
0.827 | 0.019 | -3 | 0.769 |
ERK1 |
0.826 | 0.132 | 1 | 0.760 |
DAPK1 |
0.826 | -0.093 | -3 | 0.683 |
RIPK1 |
0.826 | -0.220 | 1 | 0.846 |
WNK4 |
0.826 | -0.207 | -2 | 0.780 |
BUB1 |
0.825 | 0.005 | -5 | 0.774 |
CDK2 |
0.825 | 0.138 | 1 | 0.833 |
ULK2 |
0.824 | -0.052 | 2 | 0.790 |
IRAK4 |
0.824 | -0.155 | 1 | 0.841 |
MLK3 |
0.824 | -0.031 | 2 | 0.714 |
TBK1 |
0.824 | -0.004 | 1 | 0.766 |
MAK |
0.824 | 0.073 | -2 | 0.645 |
MTOR |
0.823 | -0.064 | 1 | 0.847 |
PKCD |
0.823 | -0.039 | 2 | 0.769 |
WNK1 |
0.823 | -0.137 | -2 | 0.781 |
GSK3A |
0.823 | 0.113 | 4 | 0.501 |
SRPK3 |
0.823 | 0.096 | -3 | 0.651 |
HIPK3 |
0.822 | 0.075 | 1 | 0.862 |
CHK1 |
0.822 | -0.099 | -3 | 0.714 |
PIM2 |
0.822 | -0.025 | -3 | 0.639 |
CDKL5 |
0.822 | -0.020 | -3 | 0.704 |
P70S6KB |
0.822 | -0.046 | -3 | 0.691 |
MRCKA |
0.821 | -0.054 | -3 | 0.638 |
HUNK |
0.821 | -0.128 | 2 | 0.821 |
CAMK2D |
0.821 | -0.009 | -3 | 0.736 |
RIPK3 |
0.821 | -0.122 | 3 | 0.755 |
DYRK1A |
0.821 | 0.069 | 1 | 0.864 |
ROCK1 |
0.821 | -0.077 | -3 | 0.640 |
HASPIN |
0.821 | -0.057 | -1 | 0.690 |
DCAMKL1 |
0.821 | -0.106 | -3 | 0.674 |
GRK2 |
0.820 | -0.073 | -2 | 0.710 |
CAMK2B |
0.820 | 0.102 | 2 | 0.887 |
CDC7 |
0.820 | -0.057 | 1 | 0.790 |
ERK7 |
0.819 | 0.004 | 2 | 0.488 |
IKKE |
0.819 | -0.002 | 1 | 0.760 |
GRK4 |
0.819 | 0.016 | -2 | 0.828 |
AMPKA1 |
0.819 | -0.124 | -3 | 0.743 |
SRPK1 |
0.818 | 0.106 | -3 | 0.671 |
CRIK |
0.818 | -0.051 | -3 | 0.590 |
MOK |
0.818 | 0.039 | 1 | 0.867 |
SMG1 |
0.818 | -0.069 | 1 | 0.818 |
CLK4 |
0.817 | 0.045 | -3 | 0.662 |
DCAMKL2 |
0.817 | -0.108 | -3 | 0.693 |
MST4 |
0.817 | -0.071 | 2 | 0.807 |
GSK3B |
0.817 | 0.009 | 4 | 0.489 |
DYRK3 |
0.817 | 0.092 | 1 | 0.870 |
HIPK4 |
0.817 | 0.076 | 1 | 0.900 |
NUAK2 |
0.816 | -0.092 | -3 | 0.729 |
CDK3 |
0.816 | 0.191 | 1 | 0.707 |
MRCKB |
0.816 | -0.071 | -3 | 0.631 |
CDK13 |
0.816 | 0.139 | 1 | 0.779 |
TTBK2 |
0.816 | -0.093 | 2 | 0.727 |
TSSK1 |
0.815 | -0.074 | -3 | 0.768 |
CDK6 |
0.815 | 0.103 | 1 | 0.767 |
GRK1 |
0.815 | 0.038 | -2 | 0.747 |
CDK8 |
0.815 | 0.141 | 1 | 0.797 |
DYRK1B |
0.814 | 0.105 | 1 | 0.795 |
CDK4 |
0.814 | 0.102 | 1 | 0.751 |
IRE2 |
0.814 | -0.059 | 2 | 0.726 |
IKKB |
0.814 | -0.038 | -2 | 0.744 |
CDK14 |
0.814 | 0.096 | 1 | 0.784 |
PKN2 |
0.813 | -0.130 | -3 | 0.732 |
CDK12 |
0.813 | 0.147 | 1 | 0.756 |
CHAK1 |
0.813 | -0.202 | 2 | 0.756 |
GCN2 |
0.813 | 0.060 | 2 | 0.823 |
DYRK4 |
0.813 | 0.151 | 1 | 0.771 |
MARK4 |
0.813 | -0.111 | 4 | 0.845 |
IRAK1 |
0.812 | -0.262 | -1 | 0.761 |
RSK2 |
0.812 | 0.002 | -3 | 0.673 |
IRE1 |
0.812 | -0.101 | 1 | 0.840 |
PAK1 |
0.811 | -0.066 | -2 | 0.702 |
PAK2 |
0.811 | -0.122 | -2 | 0.694 |
CDK17 |
0.811 | 0.143 | 1 | 0.693 |
P90RSK |
0.811 | -0.025 | -3 | 0.687 |
DRAK1 |
0.811 | -0.186 | 1 | 0.717 |
IKKA |
0.810 | 0.053 | -2 | 0.737 |
WNK3 |
0.810 | -0.302 | 1 | 0.850 |
CAMK2A |
0.810 | 0.053 | 2 | 0.892 |
PLK4 |
0.810 | 0.006 | 2 | 0.680 |
SGK3 |
0.810 | -0.076 | -3 | 0.659 |
CDK16 |
0.809 | 0.154 | 1 | 0.713 |
AKT2 |
0.809 | -0.047 | -3 | 0.587 |
ULK1 |
0.809 | -0.091 | -3 | 0.750 |
CDK18 |
0.808 | 0.156 | 1 | 0.744 |
HIPK2 |
0.808 | 0.148 | 1 | 0.767 |
MYLK4 |
0.807 | -0.116 | -2 | 0.701 |
STK33 |
0.806 | -0.134 | 2 | 0.667 |
PRKD1 |
0.806 | 0.016 | -3 | 0.720 |
CDK7 |
0.805 | 0.100 | 1 | 0.798 |
CAMK1D |
0.805 | -0.083 | -3 | 0.571 |
SGK1 |
0.805 | -0.038 | -3 | 0.508 |
AMPKA2 |
0.805 | -0.125 | -3 | 0.705 |
PKCA |
0.805 | -0.079 | 2 | 0.689 |
NDR1 |
0.804 | -0.069 | -3 | 0.727 |
PAK3 |
0.804 | -0.121 | -2 | 0.706 |
PDHK3_TYR |
0.804 | 0.204 | 4 | 0.944 |
CAMK4 |
0.803 | -0.190 | -3 | 0.699 |
CDK9 |
0.803 | 0.090 | 1 | 0.785 |
AURA |
0.803 | -0.010 | -2 | 0.572 |
MAPKAPK3 |
0.803 | -0.097 | -3 | 0.656 |
PKCZ |
0.803 | -0.133 | 2 | 0.743 |
PRKD3 |
0.802 | -0.070 | -3 | 0.643 |
RIPK2 |
0.802 | -0.285 | 1 | 0.774 |
MELK |
0.802 | -0.152 | -3 | 0.689 |
CLK1 |
0.802 | 0.036 | -3 | 0.638 |
AURB |
0.801 | -0.046 | -2 | 0.593 |
BCKDK |
0.800 | -0.113 | -1 | 0.827 |
PKCH |
0.800 | -0.145 | 2 | 0.690 |
FAM20C |
0.799 | 0.185 | 2 | 0.691 |
CHK2 |
0.799 | -0.113 | -3 | 0.526 |
RSK3 |
0.799 | -0.037 | -3 | 0.684 |
MSK1 |
0.799 | -0.041 | -3 | 0.647 |
SSTK |
0.799 | -0.108 | 4 | 0.807 |
SRPK2 |
0.798 | 0.088 | -3 | 0.588 |
AKT1 |
0.798 | -0.062 | -3 | 0.596 |
NIM1 |
0.798 | -0.166 | 3 | 0.802 |
CDK19 |
0.798 | 0.128 | 1 | 0.761 |
PKACG |
0.797 | -0.066 | -2 | 0.672 |
CAMK1G |
0.797 | -0.116 | -3 | 0.652 |
KIS |
0.797 | 0.240 | 1 | 0.830 |
LATS2 |
0.797 | -0.024 | -5 | 0.721 |
SBK |
0.797 | -0.043 | -3 | 0.465 |
RSK4 |
0.797 | -0.010 | -3 | 0.642 |
GRK3 |
0.796 | -0.058 | -2 | 0.663 |
BMPR2_TYR |
0.796 | 0.072 | -1 | 0.876 |
MSK2 |
0.796 | -0.075 | -3 | 0.645 |
CLK2 |
0.796 | 0.118 | -3 | 0.652 |
CK2A2 |
0.796 | 0.121 | 1 | 0.650 |
PKCB |
0.795 | -0.102 | 2 | 0.692 |
MAP2K6_TYR |
0.795 | 0.075 | -1 | 0.890 |
PRKD2 |
0.795 | -0.010 | -3 | 0.658 |
MARK2 |
0.795 | -0.128 | 4 | 0.733 |
TTBK1 |
0.795 | -0.109 | 2 | 0.660 |
NDR2 |
0.794 | -0.014 | -3 | 0.741 |
MAP2K4_TYR |
0.794 | -0.011 | -1 | 0.885 |
PDHK4_TYR |
0.794 | 0.070 | 2 | 0.893 |
MAPKAPK2 |
0.794 | -0.003 | -3 | 0.609 |
PKCG |
0.794 | -0.117 | 2 | 0.709 |
QIK |
0.793 | -0.235 | -3 | 0.728 |
PKG2 |
0.793 | -0.060 | -2 | 0.611 |
CDK10 |
0.792 | 0.085 | 1 | 0.768 |
PDHK1_TYR |
0.792 | 0.025 | -1 | 0.910 |
MNK2 |
0.791 | -0.069 | -2 | 0.715 |
TESK1_TYR |
0.791 | -0.091 | 3 | 0.904 |
MAP2K7_TYR |
0.791 | -0.145 | 2 | 0.872 |
PKMYT1_TYR |
0.791 | -0.073 | 3 | 0.882 |
EPHA6 |
0.791 | 0.076 | -1 | 0.889 |
PKACB |
0.790 | -0.005 | -2 | 0.611 |
P70S6K |
0.790 | -0.091 | -3 | 0.603 |
MNK1 |
0.790 | -0.092 | -2 | 0.730 |
PKCI |
0.790 | -0.145 | 2 | 0.707 |
QSK |
0.790 | -0.124 | 4 | 0.813 |
PKCE |
0.790 | -0.105 | 2 | 0.684 |
CAMK1A |
0.789 | -0.095 | -3 | 0.548 |
MARK1 |
0.789 | -0.168 | 4 | 0.793 |
EPHB4 |
0.789 | 0.062 | -1 | 0.885 |
RET |
0.788 | -0.032 | 1 | 0.858 |
PKCT |
0.787 | -0.139 | 2 | 0.698 |
CK2A1 |
0.787 | 0.091 | 1 | 0.626 |
PINK1_TYR |
0.787 | -0.182 | 1 | 0.870 |
AURC |
0.786 | -0.018 | -2 | 0.592 |
MARK3 |
0.786 | -0.130 | 4 | 0.767 |
CK1D |
0.785 | -0.102 | -3 | 0.410 |
NUAK1 |
0.785 | -0.127 | -3 | 0.676 |
MST1R |
0.784 | -0.051 | 3 | 0.844 |
YANK3 |
0.784 | -0.063 | 2 | 0.464 |
LIMK2_TYR |
0.783 | -0.080 | -3 | 0.803 |
TYK2 |
0.783 | -0.116 | 1 | 0.853 |
EPHA4 |
0.783 | 0.042 | 2 | 0.824 |
JAK2 |
0.783 | -0.063 | 1 | 0.849 |
MAPKAPK5 |
0.782 | -0.149 | -3 | 0.615 |
ABL2 |
0.782 | 0.031 | -1 | 0.841 |
EPHB2 |
0.782 | 0.073 | -1 | 0.876 |
YES1 |
0.782 | 0.034 | -1 | 0.856 |
CSF1R |
0.781 | -0.015 | 3 | 0.826 |
SIK |
0.780 | -0.134 | -3 | 0.649 |
FGR |
0.780 | -0.012 | 1 | 0.857 |
FGFR2 |
0.780 | 0.001 | 3 | 0.824 |
PHKG1 |
0.779 | -0.166 | -3 | 0.714 |
PKACA |
0.779 | -0.038 | -2 | 0.563 |
FER |
0.779 | -0.045 | 1 | 0.848 |
INSRR |
0.779 | 0.011 | 3 | 0.781 |
EPHB1 |
0.779 | 0.005 | 1 | 0.822 |
KIT |
0.779 | -0.009 | 3 | 0.834 |
SRMS |
0.778 | 0.010 | 1 | 0.820 |
TXK |
0.778 | 0.082 | 1 | 0.790 |
EPHB3 |
0.778 | 0.016 | -1 | 0.871 |
ABL1 |
0.778 | -0.000 | -1 | 0.832 |
CK1A2 |
0.778 | -0.115 | -3 | 0.407 |
TYRO3 |
0.777 | -0.120 | 3 | 0.834 |
AKT3 |
0.777 | -0.051 | -3 | 0.524 |
JAK3 |
0.777 | -0.051 | 1 | 0.821 |
LIMK1_TYR |
0.777 | -0.225 | 2 | 0.847 |
ROS1 |
0.777 | -0.114 | 3 | 0.801 |
DDR1 |
0.777 | -0.154 | 4 | 0.859 |
PAK6 |
0.777 | -0.066 | -2 | 0.647 |
HCK |
0.776 | -0.019 | -1 | 0.834 |
FGFR1 |
0.776 | -0.023 | 3 | 0.801 |
FLT3 |
0.776 | -0.048 | 3 | 0.829 |
SNRK |
0.775 | -0.286 | 2 | 0.696 |
LCK |
0.775 | 0.040 | -1 | 0.837 |
BLK |
0.775 | 0.072 | -1 | 0.850 |
PDGFRB |
0.775 | -0.081 | 3 | 0.841 |
KDR |
0.774 | -0.044 | 3 | 0.784 |
YANK2 |
0.773 | -0.088 | 2 | 0.488 |
MET |
0.773 | -0.001 | 3 | 0.823 |
ITK |
0.773 | -0.017 | -1 | 0.812 |
FLT1 |
0.773 | 0.023 | -1 | 0.876 |
PRKX |
0.772 | 0.028 | -3 | 0.567 |
BRSK1 |
0.772 | -0.131 | -3 | 0.689 |
EPHA3 |
0.771 | -0.019 | 2 | 0.799 |
FYN |
0.771 | 0.064 | -1 | 0.813 |
TNK2 |
0.771 | -0.064 | 3 | 0.797 |
TNNI3K_TYR |
0.771 | -0.039 | 1 | 0.881 |
BRSK2 |
0.771 | -0.180 | -3 | 0.703 |
PKN1 |
0.770 | -0.145 | -3 | 0.612 |
EPHA7 |
0.770 | -0.001 | 2 | 0.817 |
ERBB2 |
0.770 | -0.048 | 1 | 0.806 |
EGFR |
0.769 | 0.062 | 1 | 0.725 |
CK1E |
0.769 | -0.131 | -3 | 0.466 |
NTRK1 |
0.769 | -0.073 | -1 | 0.858 |
FGFR3 |
0.769 | -0.030 | 3 | 0.796 |
TEK |
0.769 | -0.110 | 3 | 0.778 |
EPHA5 |
0.768 | 0.039 | 2 | 0.813 |
PDGFRA |
0.767 | -0.149 | 3 | 0.844 |
LTK |
0.767 | -0.078 | 3 | 0.790 |
PHKG2 |
0.766 | -0.167 | -3 | 0.687 |
MERTK |
0.766 | -0.075 | 3 | 0.806 |
FGFR4 |
0.766 | 0.031 | -1 | 0.822 |
EPHA8 |
0.766 | 0.025 | -1 | 0.846 |
BMX |
0.766 | -0.044 | -1 | 0.738 |
LYN |
0.765 | -0.012 | 3 | 0.753 |
FLT4 |
0.765 | -0.078 | 3 | 0.781 |
JAK1 |
0.765 | -0.098 | 1 | 0.791 |
AXL |
0.765 | -0.128 | 3 | 0.804 |
TEC |
0.765 | -0.056 | -1 | 0.762 |
FRK |
0.765 | -0.028 | -1 | 0.858 |
NTRK2 |
0.764 | -0.101 | 3 | 0.793 |
PTK2B |
0.764 | 0.003 | -1 | 0.807 |
ALK |
0.764 | -0.105 | 3 | 0.771 |
NTRK3 |
0.763 | -0.053 | -1 | 0.812 |
BTK |
0.763 | -0.157 | -1 | 0.767 |
NEK10_TYR |
0.763 | -0.154 | 1 | 0.708 |
PTK6 |
0.763 | -0.148 | -1 | 0.752 |
TNK1 |
0.762 | -0.157 | 3 | 0.812 |
WEE1_TYR |
0.762 | -0.114 | -1 | 0.761 |
SRC |
0.762 | 0.005 | -1 | 0.819 |
PAK5 |
0.762 | -0.106 | -2 | 0.582 |
CSK |
0.761 | -0.055 | 2 | 0.822 |
INSR |
0.761 | -0.103 | 3 | 0.753 |
DDR2 |
0.761 | -0.034 | 3 | 0.773 |
MATK |
0.759 | -0.076 | -1 | 0.785 |
EPHA1 |
0.759 | -0.102 | 3 | 0.799 |
PTK2 |
0.759 | 0.033 | -1 | 0.797 |
SYK |
0.757 | 0.035 | -1 | 0.802 |
EPHA2 |
0.757 | 0.016 | -1 | 0.813 |
PAK4 |
0.753 | -0.093 | -2 | 0.587 |
ERBB4 |
0.752 | 0.018 | 1 | 0.715 |
IGF1R |
0.751 | -0.067 | 3 | 0.701 |
CK1G1 |
0.748 | -0.118 | -3 | 0.480 |
PKG1 |
0.747 | -0.104 | -2 | 0.535 |
MUSK |
0.747 | -0.100 | 1 | 0.723 |
CK1G3 |
0.745 | -0.093 | -3 | 0.288 |
FES |
0.733 | -0.126 | -1 | 0.724 |
ZAP70 |
0.732 | -0.020 | -1 | 0.713 |
CK1G2 |
0.723 | -0.098 | -3 | 0.391 |
CK1A |
0.711 | -0.123 | -3 | 0.328 |